NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1937369580|ref|NP_058934|]
View 

vasoactive intestinal polypeptide receptor 2 precursor [Rattus norvegicus]

Protein Classification

hormone receptor( domain architecture ID 12183096)

hormone receptor is a class B G-protein coupled receptor (GPCR) for hormones and/or hormone-related peptides; contains a large N-terminal extracellular domain that plays a critical role in peptide hormone recognition; GPCRs transmit physiological signals from the outside of the cell to the inside via G proteins by binding to an extracellular agonist, which induces conformational changes that lead to the activation of heterotrimeric G proteins, which then bind to and activate numerous downstream effector proteins

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
122-390 3.96e-167

vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


:

Pssm-ID: 320652 [Multi-domain]  Cd Length: 269  Bit Score: 470.06  E-value: 3.96e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPgSWVGC 201
Cdd:cd15986     1 YIVVKTIYTLGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVKDDILYSSSNTEHCTVPP-SLIGC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPWW 281
Cdd:cd15986    80 KVSLVILQYCIMANFYWLLVEGLYLHTLLVVIFSENRHFIVYLLIGWGIPTVFIIAWIVARIYLEDTGCWDTNDHSVPWW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 282 VIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFELC 361
Cdd:cd15986   160 VIRIPIIISIILNFILFISIIRILLQKLRSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYIVFVYFPDSSSSNYQIFFELC 239
                         250       260
                  ....*....|....*....|....*....
gi 1937369580 362 VGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15986   240 LGSFQGLVVAILYCFLNSEVQGELKRKWR 268
HormR smart00008
Domain present in hormone receptors;
47-117 4.86e-22

Domain present in hormone receptors;


:

Pssm-ID: 214468  Cd Length: 70  Bit Score: 89.11  E-value: 4.86e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369580   47 NHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGnISKNCTSDG-WSETFPDFiDACGYNDPEDES 117
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTG-ASRNCTENGgWSPPFPNY-SNCTSNDYEELK 70
 
Name Accession Description Interval E-value
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
122-390 3.96e-167

vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320652 [Multi-domain]  Cd Length: 269  Bit Score: 470.06  E-value: 3.96e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPgSWVGC 201
Cdd:cd15986     1 YIVVKTIYTLGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVKDDILYSSSNTEHCTVPP-SLIGC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPWW 281
Cdd:cd15986    80 KVSLVILQYCIMANFYWLLVEGLYLHTLLVVIFSENRHFIVYLLIGWGIPTVFIIAWIVARIYLEDTGCWDTNDHSVPWW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 282 VIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFELC 361
Cdd:cd15986   160 VIRIPIIISIILNFILFISIIRILLQKLRSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYIVFVYFPDSSSSNYQIFFELC 239
                         250       260
                  ....*....|....*....|....*....
gi 1937369580 362 VGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15986   240 LGSFQGLVVAILYCFLNSEVQGELKRKWR 268
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
122-370 2.63e-99

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 296.88  E-value: 2.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRChdqpgSWVGC 201
Cdd:pfam00002   1 ALSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKQDLDHC-----SWVGC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAW--IATRLSLEDTGCWDTNDHSI 278
Cdd:pfam00002  76 KVVAVFLHYFFLANFFWMLVEGLYLYTLLVeVFFSERKYFWWYLLIGWGVPALVVGIWagVDPKGYGEDDGCWLSNENGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 pWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYM--VFAAFPIGISSTYQI 356
Cdd:pfam00002 156 -WWIIRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVfgLFAFNPENTLRVVFL 234
                         250
                  ....*....|....
gi 1937369580 357 LFELCVGSFQGLVV 370
Cdd:pfam00002 235 YLFLILNSFQGFFV 248
HormR smart00008
Domain present in hormone receptors;
47-117 4.86e-22

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 89.11  E-value: 4.86e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369580   47 NHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGnISKNCTSDG-WSETFPDFiDACGYNDPEDES 117
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTG-ASRNCTENGgWSPPFPNY-SNCTSNDYEELK 70
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
48-111 8.72e-21

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 85.50  E-value: 8.72e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369580  48 HRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRpGNISKNCTSDG-WSETFPDFIDACGYN 111
Cdd:pfam02793   1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSGFDPR-GNASRNCTEDGtWSEHPPSNYSNCTSN 64
 
Name Accession Description Interval E-value
7tmB1_VIP-R2 cd15986
vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of ...
122-390 3.96e-167

vasoactive intestinal polypeptide (VIP) receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 2 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320652 [Multi-domain]  Cd Length: 269  Bit Score: 470.06  E-value: 3.96e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPgSWVGC 201
Cdd:cd15986     1 YIVVKTIYTLGHSVSLIALTTGSTILCLFRKLHCTRNYIHLNLFFSFILRAISVLVKDDILYSSSNTEHCTVPP-SLIGC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPWW 281
Cdd:cd15986    80 KVSLVILQYCIMANFYWLLVEGLYLHTLLVVIFSENRHFIVYLLIGWGIPTVFIIAWIVARIYLEDTGCWDTNDHSVPWW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 282 VIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFELC 361
Cdd:cd15986   160 VIRIPIIISIILNFILFISIIRILLQKLRSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYIVFVYFPDSSSSNYQIFFELC 239
                         250       260
                  ....*....|....*....|....*....
gi 1937369580 362 VGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15986   240 LGSFQGLVVAILYCFLNSEVQGELKRKWR 268
7tmB1_Secretin_R-like cd15930
secretin receptor-like group of hormone receptors, member of the class B family of ...
122-391 5.05e-153

secretin receptor-like group of hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents G protein-coupled receptors for structurally similar peptide hormones that include secretin, growth-hormone-releasing hormone (GHRH), pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptors, which are expressed in the brain, pancreas, stomach, kidney, and liver. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. All B1 subfamily GPCRs are able to increase intracellular cAMP levels by coupling to adenylate cyclase via a stimulatory Gs protein. However, depending on its cellular location, some members of subfamily B1 are also capable of coupling to additional G proteins such as G(i/o) and/or G(q) proteins, thereby leading to activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320596 [Multi-domain]  Cd Length: 268  Bit Score: 434.17  E-value: 5.05e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRChdqPGSWVGC 201
Cdd:cd15930     1 YLTVKIIYTVGYSLSLTSLTTAMIILCLFRKLHCTRNYIHMNLFVSFILRAIAVFIKDAVLFSSEDVDHC---FVSTVGC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAIL-PPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPW 280
Cdd:cd15930    78 KASMVFFQYCVMANFFWLLVEGLYLHTLLVISFfSERRYFWWYVLIGWGAPTVFVTVWIVARLYFEDTGCWDINDESPYW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFEL 360
Cdd:cd15930   158 WIIKGPILISILVNFVLFINIIRILLQKLRSPDIGGNESSQYKRLARSTLLLIPLFGIHYIVFAFFPENISLGIRLYFEL 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1937369580 361 CVGSFQGLVVAVLYCFLNSEVQCELKRRWRG 391
Cdd:cd15930   238 CLGSFQGFVVAVLYCFLNGEVQAEIKRKWRS 268
7tmB1_VIP-R1 cd15269
vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of ...
122-390 5.83e-119

vasoactive intestinal polypeptide (VIP) receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; Vasoactive intestinal peptide (VIP) receptor 1 is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. VIP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. However, depending on its cellular location, VIP-R1 is also capable of coupling to additional G proteins such as G(q) protein, thus leading to the activation of phospholipase C and intracellular calcium influx.


Pssm-ID: 320397 [Multi-domain]  Cd Length: 268  Bit Score: 347.61  E-value: 5.83e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDqpgSWVGC 201
Cdd:cd15269     1 FGTVKTGYTIGHSLSLISLTAAMIILCLFRKLHCTRNYIHMHLFMSFILRAIAVFIKDAVLFESGEEDHCSV---ASVGC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPW 280
Cdd:cd15269    78 KAAMVFFQYCIMANFFWLLVEGLYLHTLLaVSFFSERKYFWWYILIGWGAPSVFITAWSVARIYFEDVGCWDTIIESLLW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFEL 360
Cdd:cd15269   158 WIIKTPILVSILVNFILFICIIRILVQKLHSPDIGRNESSQYSRLAKSTLLLIPLFGIHYIMFAFFPDNFKAEVKLVFEL 237
                         250       260       270
                  ....*....|....*....|....*....|
gi 1937369580 361 CVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15269   238 ILGSFQGFVVAVLYCFLNGEVQAELKRKWR 267
7tmB1_secretin cd15275
secretin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
125-390 9.75e-116

secretin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Secretin receptor is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include vasoactive intestinal peptide (VIP), growth-hormone-releasing hormone (GHRH), and pituitary adenylate cyclase activating polypeptide (PACAP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors, and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Secretin, a polypeptide secreted by entero-endocrine S cells in the small intestine, is involved in maintaining body fluid balance. This polypeptide regulates the secretion of bile and bicarbonate into the duodenum from the pancreatic and biliary ducts, as well as regulates the duodenal pH by the control of gastric acid secretion. Studies with secretin receptor-null mice indicate that secretin plays a role in regulating renal water reabsorption. Secretin mediates its biological actions by elevating intracellular cAMP via G protein-coupled secretin receptor, which is expressed in the brain, pancreas, stomach, kidney, and liver.


Pssm-ID: 320403 [Multi-domain]  Cd Length: 271  Bit Score: 339.79  E-value: 9.75e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 125 VKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPgswVGCKLS 204
Cdd:cd15275     4 LKTMYTVGYSVSLVSLAIALAILCSFRRLHCTRNYIHMQLFLSFILRAISIFIKDAVLFSSEDDNHCDIYT---VGCKVA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 205 LVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPWWVI 283
Cdd:cd15275    81 MVFSNYCIMANYSWLLVEGLYLHSLLSISFFSERKHLWwYIALGWGSPLIFIISWAIARYLHENEGCWDTRRNAWIWWII 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 284 RMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISS-TYQI--LFEL 360
Cdd:cd15275   161 RGPVILSIFVNFILFLNILRILMRKLRAPDMRGNEFSQYKRLAKSTLLLIPLFGLHYILFAFFPEDVSSgTMEIwlFFEL 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1937369580 361 CVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15275   241 ALGSFQGFVVAVLYCFLNGEVQLEIQRKWR 270
7tmB1_GHRHR2 cd15271
growth-hormone-releasing hormone receptor type 2, member of the class B family of ...
122-390 4.99e-115

growth-hormone-releasing hormone receptor type 2, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor type 2 (GHRHR2) is found in non-mammalian vertebrates such as chicken and frog. It is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), vasoactive intestinal peptide, and mammalian growth hormone-releasing hormone. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. Mammalian GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. Mammalian GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320399 [Multi-domain]  Cd Length: 267  Bit Score: 337.86  E-value: 4.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRChdqPGSWVGC 201
Cdd:cd15271     1 FSTVKLLYTVGYGTSLTSLITAVLIFCTFRKLHCTRNYIHINLFVSFILRALAVFIKDAVLFADESVDHC---TMSTVAC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFL-AYLLIGWGIPSVCIGAWIATRLSLEDTGCWDtNDHSIPW 280
Cdd:cd15271    78 KAAVTFFQFCVLANFFWLLVEGMYLQTLLLLTFTSDRKYFwWYILIGWGAPSVTVTVWVLTRLQYDNRGCWD-DLESRIW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFEL 360
Cdd:cd15271   157 WIIKTPILLSVFVNFLIFINVIRILVQKLKSPDVGGNDTSHYMRLAKSTLLLIPLFGVHYVVFAFFPEHVGVEARLYFEL 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 1937369580 361 CVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15271   237 VLGSFQGFIVALLYCFLNGEVQAEIKKRLG 266
7tmB1_PACAP-R1 cd15987
pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B ...
122-391 2.87e-112

pituitary adenylate cyclase-activating polypeptide type 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Pituitary adenylate cyclase-activating polypeptide type 1 receptor (PACAP-R1) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, growth-hormone-releasing hormone (GHRH), and vasoactive intestinal peptide (VIP). These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. VIP and PACAP exert their effects through three G protein-coupled receptors, PACAP-R1, VIP-R1 (vasoactive intestinal receptor type 1, also known as VPAC1) and VIP-R2 (or VPAC2). PACAP-R1 binds only PACAP with high affinity, whereas VIP-R1 and -R2 specifically bind and respond to both VIP and PACAP. VIP and PACAP and their receptors are widely expressed in the brain and periphery. They are upregulated in neurons and immune cells in responses to CNS injury and/or inflammation and exert potent anti-inflammatory effects, as well as play important roles in the control of circadian rhythms and stress responses, among many others. PACAP-R1 is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level.


Pssm-ID: 320653 [Multi-domain]  Cd Length: 268  Bit Score: 330.78  E-value: 2.87e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDqpgSWVGC 201
Cdd:cd15987     1 YLSVKALYTVGYSTSLVSLTTAMVILCRFRKLHCTRNFIHMNLFVSFILRAISVFIKDGVLYAEQDSDHCFV---STVEC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPW 280
Cdd:cd15987    78 KAVMVFFHYCVMSNYFWLFIEGLYLFTLLVeTFFPERRYFYWYTIIGWGTPTICVTVWAVLRLHFDDTGCWDMNDNTALW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFEL 360
Cdd:cd15987   158 WVIKGPVVGSIMINFVLFIGIIIILVQKLQSPDIGGNESSIYLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFEL 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1937369580 361 CVGSFQGLVVAVLYCFLNSEVQCELKRRWRG 391
Cdd:cd15987   238 GLGSFQGFVVAVLYCFLNGEVQSEIKRKWRS 268
7tmB1_GHRHR cd15270
growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane ...
122-391 9.56e-106

growth-hormone-releasing hormone receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Growth hormone-releasing hormone receptor (GHRHR) is a member of the group of G protein-coupled receptors for structurally similar peptide hormones that also include secretin, pituitary adenylate cyclase activating polypeptide (PACAP), and vasoactive intestinal peptide. These receptors are classified into the subfamily B1 of class B GRCRs that consists of the classical hormone receptors and have been identified in all the vertebrates, from fishes to mammals, but are not present in plants, fungi, or prokaryotes. For all class B receptors, the large N-terminal extracellular domain plays a critical role in peptide hormone recognition. GHRHR is a specific receptor for the growth hormone-releasing hormone (GHRH) that controls the synthesis and release of growth hormone (GH) from the anterior pituitary somatotrophs. Mutations in the gene encoding GHRHR have been connected to isolated growth hormone deficiency (IGHD), a short-stature condition caused by deficient production of GH or lack of GH action. GHRH is preferentially coupled to a stimulatory G(s) protein, which leads to the activation of adenylate cyclase and thereby increases in intracellular cAMP level. GHRHR is found in mammals as well as zebrafish and chicken, whereas the GHRHR type 2, an ortholog of the GHRHR, has only been identified in ray-finned fish, chicken and Xenopus. Xenopus laevis GHRHR2 has been shown to interact with both endogenous GHRH and PACAP-related peptide (PRP).


Pssm-ID: 320398 [Multi-domain]  Cd Length: 268  Bit Score: 314.04  E-value: 9.56e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDqpgSWVGC 201
Cdd:cd15270     1 FSTVKIIYTVGYSISIVSLCVAVAILVAFRRLHCPRNYIHIQLFFTFILKAIAVFIKDAALFQEDDTDHCSM---STVLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSR-CFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPW 280
Cdd:cd15270    78 KVSVVFCHYCVMTNFFWLLVEAVYLNCLLASSFPRGKrYFWWLVLLGWGLPTLCTGTWILCKLYFEDTECWDINNDSPYW 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFEL 360
Cdd:cd15270   158 WIIKGPIVISVGVNFLLFLNIIRILLKKLDPRQINFNNSAQYRRLSKSTLLLIPLFGTHYIIFNFLPDYAGLGIRLYLEL 237
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1937369580 361 CVGSFQGLVVAVLYCFLNSEVQCELKRRWRG 391
Cdd:cd15270   238 CLGSFQGFIVAVLYCFLNQEVQTEISRKWYG 268
7tmB1_PTHR cd15265
parathyroid hormone receptors, member of the class B family of seven-transmembrane G ...
128-389 3.18e-104

parathyroid hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to a G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. On the other hand, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. Moreover, the PTH3R is more closely related to the PTH1R than PTH2R. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. The PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320393 [Multi-domain]  Cd Length: 289  Bit Score: 310.85  E-value: 3.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSG-----TLRCHDQPGS----- 197
Cdd:cd15265     7 IYTVGYSISLVSLTVAVFILGYFRRLHCTRNYIHMHLFVSFMLRAVSIFVKDAVLYSGSGldeleRPSMEDLKSIveapp 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 198 -----WVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCW 271
Cdd:cd15265    87 vdksqYVGCKVAVTLFLYFLATNYYWILVEGLYLHSLIfMAFFSDKKYLWGFTLIGWGFPAVFVIPWASVRATLADTRCW 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 272 DTNDHSIpWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQS-QYKRLAKSTLLLIPLFGVHYMVFAAFPIGI 350
Cdd:cd15265   167 DLSAGNY-KWIYQVPILAAIVVNFILFLNIVRVLATKLRETNAGRCDTRqQYRKLAKSTLVLIPLFGVHYIVFMGMPYTE 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1937369580 351 SSTY---QILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15265   246 VGLLwqiRMHYELFFNSFQGFFVAIIYCFCNGEVQAEIKKRW 287
7tm_2 pfam00002
7 transmembrane receptor (Secretin family); This family is known as Family B, the ...
122-370 2.63e-99

7 transmembrane receptor (Secretin family); This family is known as Family B, the secretin-receptor family or family 2 of the G-protein-coupled receptors (GCPRs). They have been described in many animal species, but not in plants, fungi or prokaryotes. Three distinct sub-families are recognized. Subfamily B1 contains classical hormone receptors, such as receptors for secretin and glucagon, that are all involved in cAMP-mediated signalling pathways. Subfamily B2 contains receptors with long extracellular N-termini, such as the leukocyte cell-surface antigen CD97; calcium-independent receptors for latrotoxin, and brain-specific angiogenesis inhibitors amongst others. Subfamily B3 includes Methuselah and other Drosophila proteins. Other than the typical seven-transmembrane region, characteriztic structural features include an amino-terminal extracellular domain involved in ligand binding, and an intracellular loop (IC3) required for specific G-protein coupling.


Pssm-ID: 459625 [Multi-domain]  Cd Length: 248  Bit Score: 296.88  E-value: 2.63e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRChdqpgSWVGC 201
Cdd:pfam00002   1 ALSLKVIYTVGYSLSLVALLLAIAIFLLFRKLHCTRNYIHLNLFASFILRALLFLVGDAVLFNKQDLDHC-----SWVGC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAW--IATRLSLEDTGCWDTNDHSI 278
Cdd:pfam00002  76 KVVAVFLHYFFLANFFWMLVEGLYLYTLLVeVFFSERKYFWWYLLIGWGVPALVVGIWagVDPKGYGEDDGCWLSNENGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 pWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYM--VFAAFPIGISSTYQI 356
Cdd:pfam00002 156 -WWIIRGPILLIILVNFIIFINIVRILVQKLRETNMGKSDLKQYRRLAKSTLLLLPLLGITWVfgLFAFNPENTLRVVFL 234
                         250
                  ....*....|....
gi 1937369580 357 LFELCVGSFQGLVV 370
Cdd:pfam00002 235 YLFLILNSFQGFFV 248
7tmB1_GlucagonR-like cd15929
glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G ...
126-391 2.05e-94

glucagon receptor-like subfamily, member of the class B family of seven-transmembrane G protein-coupled receptors; This group represents the glucagon receptor family of G protein-coupled receptors, which includes glucagon receptor (GCGR), glucagon-like peptide-1 receptor (GLP1R), GLP2R, and closely related receptors. These receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341353 [Multi-domain]  Cd Length: 279  Bit Score: 285.48  E-value: 2.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 126 KAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPGSW------V 199
Cdd:cd15929     5 QVMYTVGYSLSLAALVLALAILLGLRKLHCTRNYIHANLFASFILRALSVLVKDALLPRRYSQKGDQDLWSTLlsnqasL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 200 GCKLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSI 278
Cdd:cd15929    85 GCRVAQVLMQYCVAANYYWLLVEGLYLHTLLVlAVFSERSIFRLYLLLGWGAPVLFVVPWGIVKYLYENTGCWTRNDNMA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 PWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDqsqYK-RLAKSTLLLIPLFGVHYMVFAAFP----IGISST 353
Cdd:cd15929   165 YWWIIRLPILLAILINFFIFVRILKILVSKLRANQMCKTD---YKfRLAKSTLTLIPLLGVHEVVFAFVTdeqaRGTLRF 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369580 354 YQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWRG 391
Cdd:cd15929   242 IKLFFELFLSSFQGLLVAVLYCFANKEVQSELRKKWHR 279
7tmB1_hormone_R cd15041
The subfamily B1 of hormone receptors (secretin-like), member of the class B family ...
122-390 6.32e-92

The subfamily B1 of hormone receptors (secretin-like), member of the class B family seven-transmembrane G protein-coupled receptors; The B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of this subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. Moreover, the B1 subfamily receptors play key roles in hormone homeostasis and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression). Furthermore, the subfamilies B2 and B3 consist of receptors that are capable of interacting with epidermal growth factors (EGF) and the Drosophila melanogaster Methuselah gene product (Mth), respectively. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 341321 [Multi-domain]  Cd Length: 273  Bit Score: 279.11  E-value: 6.32e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQP--GSWV 199
Cdd:cd15041     1 LLVVYYIYLVGYSLSLVALLPAIVIFLYFRSLRCTRIRLHINLFLSFILRAVFWIIWDLLVVYDRLTSSGVETVlmQNPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 200 GCKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSI 278
Cdd:cd15041    81 GCKLLSVLKRYFKSANYFWMLCEGLYLHRLIVVAFFSEPSSLKlYYAIGWGLPLVIVVIWAIVRALLSNESCWISYNNGH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 PWWVIRMPILISIVVNFALFISIVRILLQKL-TSPDvggNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFP--IGISSTYQ 355
Cdd:cd15041   161 YEWILYGPNLLALLVNLFFLINILRILLTKLrSHPN---AEPSNYRKAVKATLILIPLFGIQYLLTIYRPpdGSEGELVY 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1937369580 356 ILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15041   238 EYFNAILNSSQGFFVAVIYCFLNGEVQSELKRKWS 272
7tmB1_PTH1R cd15984
parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G ...
128-389 4.18e-89

parathyroid hormone 1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone (PTH) receptor family has three subtypes: PTH1R, PTH2R and PTH3R. PTH1R is expressed in bone and kidney and is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)-protein that in turn activates adenylate cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple intracellular signaling pathways. PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH3R is found in chicken and fish, but it is absent in mammals. The PTH receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320650 [Multi-domain]  Cd Length: 290  Bit Score: 272.59  E-value: 4.18e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSG----------TLRCHDQP-- 195
Cdd:cd15984     7 IYTVGYSISLGSLTVAVLILGYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGSAleemeriteeDLKSITEApp 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 196 ---GSWVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCW 271
Cdd:cd15984    87 adkAQFVGCKVAVTFFLYFLATNYYWILVEGLYLHSLIfMAFFSEKKYLWGFTLFGWGLPAVFVTIWASVRATLADTGCW 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 272 DTNDHSIPwWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGND-QSQYKRLAKSTLLLIPLFGVHYMVFAAFPI-- 348
Cdd:cd15984   167 DLSAGNLK-WIIQVPILAAIVVNFILFINIVRVLATKLRETNAGRCDtRQQYRKLLKSTLVLMPLFGVHYIVFMAMPYte 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1937369580 349 --GISSTYQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15984   246 vsGILWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSW 288
7tmB1_GLP2R cd15266
glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G ...
128-390 1.30e-88

glucagon-like peptide-2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-2 receptor (GLP2R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor (GCGR) and GLP1R. GLP2R is activated by glucagon-like peptide 2, which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. GLP2R belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320394 [Multi-domain]  Cd Length: 280  Bit Score: 270.85  E-value: 1.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTlRCHDQPG--------SWV 199
Cdd:cd15266     7 IYTIGYSLSLISLSLALLILLLLRKLHCTRNYIHMNLFASFILRALAVLIKDIVLYSTYSK-RPDDETGwisylseeSST 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 200 GCKLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSI 278
Cdd:cd15266    86 SCRVAQVFMHYFVGANYFWLLVEGLYLHTLLVtAVLSERRLLKKYMLIGWGTPVLFVVPWGVAKILLENTGCWGRNENMG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 PWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDqsqYK-RLAKSTLLLIPLFGVHYMVFAAFP----IGISST 353
Cdd:cd15266   166 IWWIIRGPILLCITVNFYIFLKILKLLLSKLKAQQMRFTD---YKyRLARSTLVLIPLLGIHEVVFSFITdeqvEGFSRH 242
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1937369580 354 YQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15266   243 IRLFIQLTLSSFQGFLVAVLYCFANGEVKAELKKRWQ 279
7tmB1_PTH-R_related cd15272
invertebrate parathyroid hormone-related receptors, member of the class B family of ...
128-390 2.29e-87

invertebrate parathyroid hormone-related receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes parathyroid hormone (PTH)-related receptors found in invertebrates such as mollusks and annelid worms. The PTH family receptors are members of the B1 subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. The parathyroid hormone type 1 receptor (PTH1R) is found in all vertebrate species and is activated by two polypeptide ligands: parathyroid hormone (PTH), an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH1R couples predominantly to G(s)- protein that in turn activates adenylyl cyclase thereby producing cAMP, but it can also couple to several G protein subtypes, including G(q/11), G(i/o), and G(12/13), resulting in activation of multiple signaling pathways.


Pssm-ID: 320400 [Multi-domain]  Cd Length: 285  Bit Score: 267.72  E-value: 2.29e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDS-----------VLYSSSGTLRCHDQPG 196
Cdd:cd15272     7 MYNIGYGLSLVSLLIAVIIMLYFKKLHCPRNTIHINLFVSFILRAVLSFIKENllvqgvgfpgdVYYDSNGVIEFKDEGS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 197 SWvGCKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTND 275
Cdd:cd15272    87 HW-ECKLFFTMFNYILGANYMWIFVEGLYLHMLIfVAVFSENSRVKWYILLGWLSPLLFVLPWVFVRATLEDTLCWNTNT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 276 HSIPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISST-- 353
Cdd:cd15272   166 NKGYFWIIRGPIVISIAINFLFFINIVRVLFTKLKASNTQESRPFRYRKLAKSTLVLIPLFGVHYMVFVVLPDSMSSDea 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1937369580 354 --YQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15272   246 elVWLYFEMFFNSFQGFIVALLFCFLNGEVQSEIKKKWQ 284
7tmB1_NPR_B7_insect-like cd15273
insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of ...
124-390 6.37e-82

insect neuropeptide receptor subgroup B7 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from invertebrates. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320401 [Multi-domain]  Cd Length: 285  Bit Score: 253.83  E-value: 6.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 124 LVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDS------------VLYSSSGTLRC 191
Cdd:cd15273     3 IIKGISQIGYIVSLITLIIAFAIFLSFKKLHCARNKLHMHLFASFILRAFMTLLKDSlfidglglladiVERNGGGNEVI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 192 HDQPGSWVgCKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGC 270
Cdd:cd15273    83 ANIGSNWV-CKAITSLWQYFIIANYSWILMEGLYLHNLIfLALFSDENNIILYILLGWGLPLIFVVPWIVARILFENSLC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 271 WDTNDHSIPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVggNDQSQYKRLAKSTLLLIPLFGVHYMVFAA--FPI 348
Cdd:cd15273   162 WTTNSNLLNFLIIRIPIMISVLINFILFLNIVRVLLVKLRSSVN--EDSRRYKKWAKSTLVLVPLFGVHYTIFLIlsYLD 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1937369580 349 GISSTYQIL---FELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15273   240 DTNEAVELIwlfCDQLFASFQGFFVALLYCFLNGEVRAEIQRKWR 284
7tmB1_PTH3R cd15983
parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G ...
128-389 7.17e-81

parathyroid hormone 3 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 3 receptor (PTH3R), one of the three subtypes of PTH receptor family, is found in chicken and fish, but it is absent in mammals. On the other hand, the PTH1R is found in all vertebrate species, whereas PTH2R is found in mammals and fish, but not in chicken or frog. PTH1R is activated by two polypeptide ligands: PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, and PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39), but not by PTHrP. PTH also strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs, suggesting that TIP-39 is a natural ligand for PTH2R. Conversely, PTH3R binds and responds to both PTH and PTHrP, but not the TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320649 [Multi-domain]  Cd Length: 285  Bit Score: 250.99  E-value: 7.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQ-------PGS--- 197
Cdd:cd15983     7 MYTIGYSISLAALLVAVCILCYFKRLHCTRNYIHIHLFASFICRAGSIFVKDAVLYSGTNEGEALDEkiefglsPGTrlq 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 198 WVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDH 276
Cdd:cd15983    87 WVGCKVTVTLFLYFLATNHYWILVEGLYLHSLIfMAFLSDKNYLWALTIIGWGLPAVFVSVWASVRVSLADTQCWDLSAG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 277 SIPwWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGND-QSQYKRLAKSTLLLIPLFGVHYMVFAAFPI----GIS 351
Cdd:cd15983   167 NLK-WIYQVPILAAILVNFFLFLNIVRVLASKLWETNTGKLDpRQQYRKLLKSTLVLMPLFGVHYVLFMAMPYtdvtGLL 245
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369580 352 STYQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15983   246 WQIQMHYEMLFNSSQGFFVAFIYCFCNGEVQAEIKKAW 283
7tmB1_GCGR cd15267
glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled ...
121-390 1.79e-78

glucagon receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon receptor (GCGR) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon-like peptide-1 receptor (GLP1R) and GLP2R. GCGR is activated by glucagon, which is derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR belongs to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320395 [Multi-domain]  Cd Length: 281  Bit Score: 244.73  E-value: 1.79e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 121 FYILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCHDQPGSWV- 199
Cdd:cd15267     2 TYSSFQVMYTVGYSLSLGALLLALAILGGFSKLHCMRNAIHMNLFASFILKASSVLVIDGLLRTRYSQKIEDDLSSTWLs 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 200 -----GCKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIGAWIATRLSLEDTGCWDT 273
Cdd:cd15267    82 deavaGCRVAAVFMQYGIVANYCWLLVEGIYLHNLLVLAVFPERSYFSlYLCIGWGAPALFVVPWVVVKCLYENVQCWTS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 274 NDHSIPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDqsqYK-RLAKSTLLLIPLFGVHYMVFAAF----PI 348
Cdd:cd15267   162 NDNMGFWWILRFPVFLAILINFFIFVRIIQILVSKLRARQMHYTD---YKfRLAKSTLTLIPLLGIHEVVFAFVtdehAQ 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1937369580 349 GISSTYQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15267   239 GTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWH 280
7tmB1_GlucagonR-like_1 cd15985
uncharacterized group of glucagon receptor-like proteins, member of the class B family of ...
126-390 1.59e-76

uncharacterized group of glucagon receptor-like proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This group consists of uncharacterized proteins with similarity to members of the glucagon receptor family of G protein-coupled receptors, which include glucagon receptor (GCGR), and glucagon-like peptide-1 receptor (GLP1R), and GLP2R. The glucagon receptors are activated by the members of the glucagon (GCG) peptide family including GCG, glucagon-like peptide 1 (GLP1), and GLP2, which are derived from the large proglucagon precursor. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320651 [Multi-domain]  Cd Length: 280  Bit Score: 239.83  E-value: 1.59e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 126 KAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSG--TLRCHD-----QPGSW 198
Cdd:cd15985     5 RMLYTVGYTLSLLTLVSALLILTSIRKLHCTRNYIHANLFASFILRAVSVIVKDTLLERRWGreIMRVADwgellSHKAA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 199 VGCKLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHS 277
Cdd:cd15985    85 IGCRMAQVVMQYCILANHYWFFVEAVYLYKLLIgAVFSEKNYYLLYLYLGWGTPVLFVVPWMLAKYLKENKECWALNENM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 278 IPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDqsqYK-RLAKSTLLLIPLFGVHYMVFA----AFPIGISS 352
Cdd:cd15985   165 AYWWIIRIPILLASLINLLIFMRILKVILSKLRANQKGYAD---YKlRLAKATLTLIPLFGIHEVVFIfatdEQTTGILR 241
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369580 353 TYQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15985   242 YIKVFFTLFLNSFQGFLVAVLYCFANKEVKSELLKKWR 279
7tmB1_PTH2R cd15982
parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G ...
128-389 8.32e-76

parathyroid hormone 2 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; The parathyroid hormone 2 receptor (PTH2R), one of the three subtypes of PTH receptor family, is found in mammals and fish, but not in chicken or frog. PTH2R is potently activated by tuberoinfundibular peptide-39 (TIP-39) but not by PTH-related peptide (PTHrP), a paracrine factor that regulates endochondral bone development. PTH, an endocrine hormone that regulates calcium homoeostasis and bone maintenance, strongly activates human PTH2R, but only weakly activates rat and zebrafish PTH2Rs. These results suggest that TIP-39 is a natural ligand for PTH2R. Conversely, PTH1R is activated by PTH and PTHrP, but not by TIP-39. The PTH family receptors are members of the B1 (or secretin-like) subfamily of class B GPCRs, which include receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), and calcitonin gene-related peptide. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways.


Pssm-ID: 320648 [Multi-domain]  Cd Length: 289  Bit Score: 238.30  E-value: 8.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRCH----DQPGS------ 197
Cdd:cd15982     7 MYTVGYSISFSSLAVAIFIIGYFRRLHCTRNYIHMHLFVSFMLRAASIFVKDKVVHTHIGVKELDavlmNDFQNavdapp 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 198 -----WVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCW 271
Cdd:cd15982    87 vdksqYVGCKIAVVMFIYFLATNYYWILVEGLYLHSLIfVAFFSDTKYLWGFTLIGWGFPAVFVAAWAVVRATLADARCW 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 272 DTNDHSIPwWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGND-QSQYKRLAKSTLLLIPLFGVHYMVFAAFP--- 347
Cdd:cd15982   167 ELSAGDIK-WIYQAPILAAIGLNFILFLNTVRVLATKIWETNAVGYDtRKQYRKLAKSTLVLVLVFGVHYIVFVCLPhtf 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1937369580 348 IGISSTYQILFELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15982   246 TGLGWEIRMHCELFFNSFQGFFVSIIYCYCNGEVQTEIKKTW 287
7tmB1_GLP1R cd15268
glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G ...
128-389 5.54e-70

glucagon-like peptide-1 receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; Glucagon-like peptide-1 receptor (GLP1R) is a member of the glucagon receptor family of G protein-coupled receptors, which also includes glucagon receptor and GLP2R. GLP1R is activated by glucagon-like peptide 1 (GLP1), which is derived from the large proglucagon precursor. Activation of GLP1R stimulates glucose-dependent insulin secretion from pancreatic beta cells, whereas activation of GLP2R stimulates intestinal epithelial proliferation and increases villus height in the small intestine. GCGR regulates blood glucose levels by control of hepatic glycogenolysis and gluconeogenesis and by regulation of insulin secretion from the pancreatic beta-cells. Receptors in this group belong to the B1 (or secretin-like) subfamily of class B GPCRs, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on their cellular location, GCGR and GLP receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 341342 [Multi-domain]  Cd Length: 279  Bit Score: 222.90  E-value: 5.54e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVL---YSSSGTLRCHDQPGSW---VGC 201
Cdd:cd15268     7 IYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALkwmYSTAAQQHQWDGLLSYqdsLSC 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPW 280
Cdd:cd15268    87 RLVFLLMQYCVAANYYWLLVEGVYLYTLLAfSVFSEQRIFRLYLSIGWGVPLLFVIPWGIVKYLYEDEGCWTRNSNMNYW 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQykRLAKSTLLLIPLFGVHYMVFA----AFPIGISSTYQI 356
Cdd:cd15268   167 LIIRLPILFAIGVNFLIFIRVICIVVSKLKANLMCKTDIKC--RLAKSTLTLIPLLGTHEVIFAfvmdEHARGTLRFVKL 244
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369580 357 LFELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15268   245 FTELSFTSFQGLMVAILYCFVNNEVQMEFRKSW 277
7tmB1_CRF-R cd15264
corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane ...
122-389 2.43e-54

corticotropin-releasing factor receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320392 [Multi-domain]  Cd Length: 265  Bit Score: 181.85  E-value: 2.43e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLysssgTLRCHDQPGSWvgC 201
Cdd:cd15264     1 YKVALIIYYLGFSISLVALAVALIIFLYFRSLRCLRNNIHCNLIVTFILRNVTWFIMQNTL-----TEIHHQSNQWV--C 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRC-FLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIPW 280
Cdd:cd15264    74 RLIVTVYNYFQVTNFFWMFVEGLYLHTMIVWAYSADKIrFWYYIVIGWCIPCPFVLAWAIVKLLYENEHCWLPKSENSYY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 -WVIRMPILISIVVNFALFISIVRILLQKL-TSPDVGGNdqsQYKRLAKSTLLLIPLFGVHYMVFAAFPiGISSTYQILF 358
Cdd:cd15264   154 dYIYQGPILLVLLINFIFLFNIVWVLITKLrASNTLETI---QYRKAVKATLVLLPLLGITYMLFFINP-GDDKTSRLVF 229
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1937369580 359 ---ELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15264   230 iyfNTFLQSFQGLFVAVFYCFLNGEVRSAIRKKF 263
7tmB1_NPR_B4_insect-like cd15260
insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of ...
124-390 6.50e-52

insect neuropeptide receptor subgroup B4 and related proteins, member of the class B family of seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Nilaparvata lugens (brown planthopper) and its closely related proteins from mollusks and annelid worms. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320388 [Multi-domain]  Cd Length: 267  Bit Score: 175.54  E-value: 6.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 124 LVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLrcHDQPgswVGCKL 203
Cdd:cd15260     3 FVNYVYIGGYSVSLIALIISLAIFFSFRSLRCTRITIHMNLFISFALNNLLWIVWYKLVVDNPEVL--LENP---IWCQA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 204 SLVFFQYCIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLED--TGCWDTNDHSipW 280
Cdd:cd15260    78 LHVLLQYFMVCNYFWMFCEGLYLHTVLVvAFISEKSLMRWFIAIGWGVPLVITAIYAGVRASLPDdtERCWMEESSY--Q 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 281 WVIRMPILISIVVNFALFISIVRILLQKLTSPDvGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISS---TYQIl 357
Cdd:cd15260   156 WILIVPVVLSLLINLIFLINIVRVLLTKLRATS-PNPAPAGLRKAVRATLILIPLLGLQFLLIPFRPEPGAPletIYQY- 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369580 358 FELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15260   234 VSALLTSLQGLCVAVLFCFCNGEVIAAIKRKWR 266
7tm_classB cd13952
class B family of seven-transmembrane G protein-coupled receptors; The class B of ...
128-385 2.47e-51

class B family of seven-transmembrane G protein-coupled receptors; The class B of seven-transmembrane GPCRs is classified into three major subfamilies: subfamily B1 (secretin-like receptor family), B2 (adhesion family), and B3 (Methuselah-like family). The class B receptors have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi or prokaryotes. The B1 subfamily comprises receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the subfamily B1 receptors preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The subfamily B2 consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Furthermore, the subfamily B3 includes Methuselah (Mth) protein, which was originally identified in Drosophila as a GPCR affecting stress resistance and aging, and its closely related proteins.


Pssm-ID: 410627 [Multi-domain]  Cd Length: 260  Bit Score: 173.55  E-value: 2.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSsgtlrchdqpgSWVGCKLSLVF 207
Cdd:cd13952     7 ITYIGCSLSLVGLLLTIITYLLFPKLRNLRGKILINLCLSLLLAQLLFLIGQLLTSSD-----------RPVLCKALAIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 208 FQYCIMANFYWLLVEGLYLHTLLVAILP--PSRCFLAYLLIGWGIPSVCIGAWIATRLSLE-------DTGCWDTNDHSI 278
Cdd:cd13952    76 LHYFLLASFFWMLVEAFDLYRTFVKVFGssERRRFLKYSLYGWGLPLLIVIITAIVDFSLYgpspgygGEYCWLSNGNAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 pWWVIRMPILISIVVNFALFISIVRILLQKLTSpDVGGNDQSQYKRLAKSTLLLIPLFGVHYMV-FAAFPIGISSTYQIL 357
Cdd:cd13952   156 -LWAFYGPVLLILLVNLVFFILTVRILLRKLRE-TPKQSERKSDRKQLRAYLKLFPLMGLTWIFgILAPFVGGSLVFWYL 233
                         250       260
                  ....*....|....*....|....*...
gi 1937369580 358 FELCVgSFQGLVVAVLYCFLNSEVQCEL 385
Cdd:cd13952   234 FDILN-SLQGFFIFLIFCLKNKEVRRLL 260
7tmB1_DH_R cd15263
insect diuretic hormone receptors, member of the class B family of seven-transmembrane G ...
128-389 1.16e-41

insect diuretic hormone receptors, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors that specifically bind to insect diuretic hormones found in Manduca sexta (moth) and Acheta domesticus (the house cricket), among others. Insect diuretic hormone and their GPCRs play critical roles in the regulation of water and ion balance. Thus they are attractive targets for developing new insecticides. Activation of the diuretic hormone receptors stimulate adenylate cyclase, thereby increasing cAMP levels in Malpighian tube. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of Gs family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx.


Pssm-ID: 320391 [Multi-domain]  Cd Length: 272  Bit Score: 148.67  E-value: 1.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTLRchdqpgswvGCKLSLVF 207
Cdd:cd15263     7 IYFIGYSLSLVALSLALWIFLYFKDLRCLRNTIHTNLMFTYILADLTWILTLTLQVSIGEDQK---------SCIILVVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 208 FQYCIMANFYWLLVEGLYLHTLLVAILPPSRC-FLAYLLIGWGIPSVCIGAWIATR------------LSLEDTGCWDTN 274
Cdd:cd15263    78 LHYFHLTNFFWMFVEGLYLYMLVVETFSGENIkLRVYAFIGWGIPAVVIVIWAIVKalaptapntaldPNGLLKHCPWMA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 275 DHSIPwWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGgnDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPigISSTY 354
Cdd:cd15263   158 EHIVD-WIFQGPAILVLAVNLVFLVRIMWVLITKLRSANTV--ETQQYRKAAKALLVLIPLLGITYILVIAGP--TEGIA 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369580 355 QILFELCVG---SFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15263   233 ANIFEYVRAvllSTQGFTVALFYCFLNTEVRNTLRHHF 270
7tmB1_calcitonin_R cd15274
calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled ...
131-389 2.29e-40

calcitonin receptor, member of the class B family of seven-transmembrane G protein-coupled receptors; This group includes G protein-coupled receptors for calcitonin (CT) and calcitonin gene-related peptides (CGRPs). Calcitonin, a 32-amino acid peptide hormone, is involved in calcium metabolism in many mammalian species and acts to reduce blood calcium levels and directly inhibits bone resorption by acting on osteoclast. Thus, CT acts as an antagonist to parathyroid hormone and is commonly used in the treatment of bone disorders. The CT receptor is predominantly found in osteoclasts, kidney, and brain, and is primarily coupled to stimulatory G(s) protein, which leads to activation of adenylate cyclase, thereby increasing cAMP production. CGRP, a member of the calcitonin family of peptides, is a potent vasodilator and may contribute to migraine. It is expressed in the peripheral and central nervous system and exists in two forms in humans (alpha-CGRP and beta-CGRP). CGRP meditates its physiological effects through calcitonin receptor-like receptor (CRLR) and receptor activity-modifying protein 1 (RAMP1), a single transmembrane domain protein. Thus, the CRLR/RAMP1 complex serves as a functional CGRP receptor. On the other hand, the CRLR/RAMP2 and CRLR/RAMP3 complexes function as adrenomedullin-specific receptors. The CT and CGRP receptors belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide.


Pssm-ID: 341343 [Multi-domain]  Cd Length: 274  Bit Score: 145.30  E-value: 2.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 131 LGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLySSSGTLRCHDQpgswVGCKLSLVFFQY 210
Cdd:cd15274    10 VGHSLSIATLLISLGIFFFFRSLSCQRVTLHKNLFLSYILNSIIIIIHLVAV-VPNGELVARNP----VSCKILHFIHQY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 211 CIMANFYWLLVEGLYLHTLLV-AILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIpWWVIRMPILI 289
Cdd:cd15274    85 MMGCNYFWMLCEGIYLHTLIVvAVFAEKQRLMWYYLLGWGFPLIPTTIHAITRAVYYNDNCWLSSETHL-LYIIHGPIMA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 290 SIVVNFALFISIVRILLQKLTspDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIG--ISSTYQILFELCVgSFQG 367
Cdd:cd15274   164 ALVVNFFFLLNIVRVLVTKLR--ETHEAESHMYLKAVKATLILVPLLGIQFVLFPWRPSGkiLGKIYDYVMHSLI-HFQG 240
                         250       260
                  ....*....|....*....|..
gi 1937369580 368 LVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15274   241 FFVATIFCFCNGEVQATLKRQW 262
7tmB1_CRF-R1 cd15445
corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane ...
122-390 2.04e-39

corticotropin-releasing factor receptor 1, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320561 [Multi-domain]  Cd Length: 265  Bit Score: 142.38  E-value: 2.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLysssgTLRCHDQPGSWvgC 201
Cdd:cd15445     1 YHIAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLITAFILRNATWFVVQLTM-----SPEVHQSNVVW--C 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCF-LAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSI-P 279
Cdd:cd15445    74 RLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDKLRkWMFICIGWCIPFPIIVAWAIGKLYYDNEKCWFGKRAGVyT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRMPILISIVVNFALFISIVRILLQKLTSPDVggNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFP--IGISSTYQIL 357
Cdd:cd15445   154 DYIYQGPMILVLLINFIFLFNIVRILMTKLRASTT--SETIQYRKAVKATLVLLPLLGITYMLFFVNPgeDEISRIVFIY 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369580 358 FELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15445   232 FNSFLESFQGFFVSVFYCFLNSEVRSAVRKRWH 264
7tmB1_CRF-R2 cd15446
corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane ...
122-389 1.09e-37

corticotropin-releasing factor receptor 2, member of the class B family of seven-transmembrane G protein-coupled receptors; The vertebrate corticotropin-releasing factor (CRF) receptors are predominantly expressed in central nervous system with high levels in cortex tissue, brain stem, and pituitary. They have two isoforms as a result of alternative splicing of the same receptor gene: CRF-R1 and CRF-R2, which differ in tissue distribution and ligand binding affinities. Recently, a third CRF receptor (CRF-R3) has been identified in catfish pituitary. The catfish CRF-R1 is highly homologous to CRF-R3. CRF is a 41-amino acid neuropeptide that plays a central role in coordinating neuroendocrine, behavioral, and autonomic responses to stress by acting as the primary neuroregulator of the hypothalamic-pituitary-adrenal axis, which controls the levels of cortisol and other stress related hormones. In addition, the CRF family of neuropeptides also includes structurally related peptides such as mammalian urocortin, fish urotensin I, and frog sauvagine. The actions of CRF and CRF-related peptides are mediated through specific binding to CRF-R1 and CRF-R2. CRF and urocortin 1 bind and activate mammalian CRF-R1 with similar high affinities. By contrast, urocortin 2 and urocortin 3 do not bind to CRF-R1 or stimulate CRF-R1-mediated cAMP formation. Urocortin 1 also shows high affinity for mammalian CRF-R2, whereas CRF has significantly lower affinity for this receptor. These evidence suggest that urocortin 1 is an endogenous ligand for CRF-R1 and CRF-R2. The CRF receptors are members of the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, and parathyroid hormone (PTH). These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. However, depending on its cellular location and function, CRF receptors can activate multiple G proteins, which can in turn stimulate different second messenger pathways.


Pssm-ID: 320562 [Multi-domain]  Cd Length: 264  Bit Score: 137.78  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSssgtlrCHDQPGSWvgC 201
Cdd:cd15446     1 YKIALIINYLGHCISVGALVVAFLLFLCLRSIRCLRNIIHWNLITTFILRNVMWFLLQMIDHN------IHESNEVW--C 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCF-LAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTND-HSIP 279
Cdd:cd15446    73 RCITTIYNYFVVTNFFWMFVEGCYLHTAIVMTYSTDKLRkWVFLFIGWCIPCPIIVAWAIGKLYYENEQCWFGKEpGKYI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRMPILISIVVNFALFISIVRILLQKLTSPDVggNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFP--IGISSTYQIL 357
Cdd:cd15446   153 DYIYQGPVILVLLINFVFLFNIVRILMTKLRASTT--SETIQYRKAVKATLVLLPLLGITYMLFFVNPgeDDISQIVFIY 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1937369580 358 FELCVGSFQGLVVAVLYCFLNSEVQCELKRRW 389
Cdd:cd15446   231 FNSFLQSFQGFFVSVFYCFLNGEVRSAARKRW 262
7tmB1_NPR_B3_insect-like cd15262
insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of ...
133-390 3.97e-37

insect neuropeptide receptor subgroup B3 and related proteins belong to subfamily B1 of hormone receptors; member of the class B secretin-like seven-transmembrane G protein-coupled receptors; This subgroup includes a neuropeptide receptor found in Bombyx mori (silk worm) and its closely related proteins from arthropods. They belong to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. The class B GPCRs have been identified in all the vertebrates, from fishes to mammals, as well as invertebrates including Caenorhabditis elegans and Drosophila melanogaster, but are not present in plants, fungi, or prokaryotes.


Pssm-ID: 320390 [Multi-domain]  Cd Length: 270  Bit Score: 136.42  E-value: 3.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 133 YSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLY----SSSGTLRCHDQPGswVGCKLSLVFF 208
Cdd:cd15262    12 LSVSVVTSLPAVFIFYSYKRLRITRVILHRNLLISIIIRNILVIISKVFVIldalTSSGDDTVMNQNA--VVCRLLSIFE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 209 QYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCW-DTNDHSipWWVIRMPI 287
Cdd:cd15262    90 RAARNAVFACMFVEGFYLHRLIVAVFAEKSSIRFLYVIGAVLPLFPVIIWAIIRALHNDHSCWvVDIEGV--QWVLDTPR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 288 LISIVVNFALFISIVRILLQKLTSpdvgGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQIL---FELCVGS 364
Cdd:cd15262   168 LFILLVNTVLLVDIIRVLVTKLRN----TEENSQTKSTTRATLFLVPLFGLHFVITAYRPSTDDCDWEDIyyyANYLIEG 243
                         250       260
                  ....*....|....*....|....*.
gi 1937369580 365 FQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15262   244 LQGFLVAILFCYINKEVHYLIKNTYR 269
7tmB1_PDFR cd15261
The pigment dispersing factor receptor, member of the class B seven-transmembrane G ...
125-390 7.56e-36

The pigment dispersing factor receptor, member of the class B seven-transmembrane G protein-coupled receptors; The pigment dispersing factor receptor (PDFR) is a G protein-coupled receptor that binds the circadian clock neuropeptide PDF, a functional ortholog of the mammalian vasoactive intestinal peptide (VIP), on the pacemaker neurons. The PDFR is implicated in regulating flight circuit development and in modulating acute flight In Drosophila melanogaster. The PDFR activation stimulates adenylate cyclase, thereby increasing cAMP levels in many different pacemakers, and the receptor signaling has been shown to regulate behavioral circadian rhythms and geotaxis in Drosophila. The PDFR belongs to the B1 subfamily of class B GPCRs, also referred to as secretin-like receptor family, which includes receptors for polypeptide hormones of 27-141 amino-acid residues such as secretin, glucagon, glucagon-like peptide (GLP), calcitonin gene-related peptide, parathyroid hormone (PTH), and corticotropin-releasing factor. . These receptors contain the large N-terminal extracellular domain (ECD), which plays a critical role in hormone recognition by binding to the C-terminal portion of the peptide. On the other hand, the N-terminal segment of the hormone induces receptor activation by interacting with the receptor transmembrane domains and connecting extracellular loops, triggering intracellular signaling pathways. All members of the B1 subfamily preferentially couple to G proteins of G(s) family, which positively stimulate adenylate cyclase, leading to increased intracellular cAMP formation and calcium influx. They play key roles in hormone homeostasis in mammals and are promising drug targets in various human diseases including diabetes, osteoporosis, obesity, neurodegenerative conditions (Alzheimer###s and Parkinson's), cardiovascular disease, migraine, and psychiatric disorders (anxiety, depression).


Pssm-ID: 320389 [Multi-domain]  Cd Length: 282  Bit Score: 133.26  E-value: 7.56e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 125 VKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAIS--VLVKDSVLYSSSGTlrcHDQPGSWVG-- 200
Cdd:cd15261     4 TRTLEIVGLCLSLVSLIISLFIFSYFRTLRNHRTRIHKNLFLAILLQVIIrlVLYIDQAITRSRGS---HTNAATTEGrt 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 201 -------CKLSLVFFQYCIMANFYWLLVEGLYLHTLL-VAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTG-CW 271
Cdd:cd15261    81 instpilCEGFYVLLEYAKTVMFMWMFIEGLYLHNIIvVSVFSGKPNYLFYYILGWGIPIVHTSAWAIVTLIKMKVNrCW 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 272 DTNDHSIPWWVIRMPILISIVVNFALFISIVRILLQKLTspDVGGNDQSQYKRLAKSTLLLIPLFGV------------- 338
Cdd:cd15261   161 FGYYLTPYYWILEGPRLAVILINLFFLLNIIRVLVSKLR--ESHSREIEQVRKAVKAAIVLLPLLGItnilqmippplts 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1937369580 339 HYMVFAAFPIGISSTYqilfelcvgSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15261   239 VIVGFAVWSYSTHFLT---------SFQGFFVALIYCFLNGEVKNVLKKFWR 281
7tmB2_Adhesion cd15040
adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G ...
132-382 1.42e-27

adhesion receptors, subfamily B2 of the class B family of seven-transmembrane G protein-coupled receptors; The B2 subfamily of class B GPCRs consists of cell-adhesion receptors with 33 members in humans and vertebrates. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing a variety of structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, linked to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320168 [Multi-domain]  Cd Length: 253  Bit Score: 109.97  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 132 GYSVSLMSLTTGSIIICLFRKLHC-TRNYIHLNLflsfmlrAISVLVKDSVLYSSSgtlrchDQPGSWVGCKLSLVFFQY 210
Cdd:cd15040    11 GCGLSLLGLLLTIITYILFRKLRKrKPTKILLNL-------CLALLLANLLFLFGI------NSTDNPVLCTAVAALLHY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 211 CIMANFYWLLVEGLYLHTLLVAI--LPPSRCFLAYLLIGWGIPSVCIGAWIATRLSL---EDTGCWDTNDHSIPWWVIrM 285
Cdd:cd15040    78 FLLASFMWMLVEALLLYLRLVKVfgTYPRHFILKYALIGWGLPLIIVIITLAVDPDSygnSSGYCWLSNGNGLYYAFL-G 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 286 PILISIVVNFALFISIVRILLQklTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFELCvGSF 365
Cdd:cd15040   157 PVLLIILVNLVIFVLVLRKLLR--LSAKRNKKKRKKTKAQLRAAVSLFFLLGLTWIFGILAIFGARVVFQYLFAIF-NSL 233
                         250
                  ....*....|....*..
gi 1937369580 366 QGLVVAVLYCFLNSEVQ 382
Cdd:cd15040   234 QGFFIFIFHCLRNKEVR 250
7tmB2_GPR133-like_Adhesion_V cd15933
orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of ...
126-383 9.81e-27

orphan GPR133 and related proteins, group V adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group V adhesion GPCRs include orphan receptors GPR133, GPR144, and closely related proteins. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the G(s) protein, leading to activation of adenylate cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320599 [Multi-domain]  Cd Length: 252  Bit Score: 107.80  E-value: 9.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 126 KAIYTLGY---SVSLMSLTTGSIIICLFRKLHCTRNYIHLNLflsfmlrAISVLVKDSVLYSSSGTLRCHdqpgswVGCK 202
Cdd:cd15933     2 RALSIISYigcGISIACLALTLIIFLVLRVLSSDRFQIHKNL-------CVALLLAQILLLAGEWAEGNK------VACK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIATRLSL--EDTGCW-DTNDHSIp 279
Cdd:cd15933    69 VVAILLHFFFMAAFSWMLVEGLHLYLMIVKVFNYKSKMRYYYFIGWGLPAIIVAISLAILFDDygSPNVCWlSLDDGLI- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 wWVIRMPILISIVVNFALFISIVRILLQKLTSPDV-GGNDQSQYKRLAKSTLLLIPLFGVHYmVFAAFPI-GISSTYQIL 357
Cdd:cd15933   148 -WAFVGPVIFIITVNTVILILVVKITVSLSTNDAKkSQGTLAQIKSTAKASVVLLPILGLTW-LFGVLVVnSQTIVFQYI 225
                         250       260
                  ....*....|....*....|....*.
gi 1937369580 358 FELcVGSFQGLVVAVLYCFLNSEVQC 383
Cdd:cd15933   226 FVI-LNSLQGLMIFLFHCVLNSEVRS 250
HormR smart00008
Domain present in hormone receptors;
47-117 4.86e-22

Domain present in hormone receptors;


Pssm-ID: 214468  Cd Length: 70  Bit Score: 89.11  E-value: 4.86e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937369580   47 NHRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRPGnISKNCTSDG-WSETFPDFiDACGYNDPEDES 117
Cdd:smart00008   1 TDLGCPATWDGIICWPQTPAGQLVEVPCPKYFSGFSYKTG-ASRNCTENGgWSPPFPNY-SNCTSNDYEELK 70
7tmB2_CELSR_Adhesion_IV cd15441
cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 ...
123-391 1.59e-21

cadherin EGF LAG seven-pass G-type receptors, group IV adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuron migration and axon guidance in the CNS.


Pssm-ID: 320557 [Multi-domain]  Cd Length: 254  Bit Score: 93.08  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKdsvlysssgtlrcHDQPGSWVGCK 202
Cdd:cd15441     2 LLLKIVTYIGIGISLVLLVIAFLVLSCLRGLQSNSNSIHKNLVACLLLAELLFLLG-------------INQTENLFPCK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIGawIATRLSLEDTG----CWDTNDHS 277
Cdd:cd15441    69 LIAILLHYFYLSAFSWLLVESLHLYRMLTEPRDINHGHMRfYYLLGYGIPAIIVG--LSVGLRPDGYGnpdfCWLSVNET 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 278 IPWWVIrMPILISIVVNFALFISIVRILLQKLTSpdvgGNDQSQYKRLAKSTLLLIPLFGVHYmVFAAFPI-GISSTYQI 356
Cdd:cd15441   147 LIWSFA-GPIAFVIVITLIIFILALRASCTLKRH----VLEKASVRTDLRSSFLLLPLLGATW-VFGLLAVnEDSELLHY 220
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1937369580 357 LFELCVGsFQGLVVAVLYCFLNSEVQCELKRRWRG 391
Cdd:cd15441   221 LFAGLNF-LQGLFIFLFYCIFNKKVRRELKNALLR 254
HRM pfam02793
Hormone receptor domain; This extracellular domain contains four conserved cysteines that ...
48-111 8.72e-21

Hormone receptor domain; This extracellular domain contains four conserved cysteines that probably for disulphide bridges. The domain is found in a variety of hormone receptors. It may be a ligand binding domain.


Pssm-ID: 397086  Cd Length: 64  Bit Score: 85.50  E-value: 8.72e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369580  48 HRACSGVWDNITCWRPADIGETVTVPCPKVFSNFYSRpGNISKNCTSDG-WSETFPDFIDACGYN 111
Cdd:pfam02793   1 GLGCPRTWDGILCWPRTPAGETVEVPCPDYFSGFDPR-GNASRNCTEDGtWSEHPPSNYSNCTSN 64
7tmB2_GPR133 cd15256
orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G ...
123-388 4.10e-18

orphan adhesion receptor GPR133, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR133 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR144. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320384 [Multi-domain]  Cd Length: 260  Bit Score: 83.82  E-value: 4.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRN---YIHLNLflSFMLRAISVLVKDSVLYSSsGTLRChdqpgswv 199
Cdd:cd15256     2 VALSSITYVGCSLSIFCLAITLVTFAVLSSVSTIRNqryHIHANL--SFAVLVAQILLLISFRFEP-GTLPC-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 200 gcKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRC-FLAYLLIGWGIPSV-CIgawIATRLSLEDTG----CWDT 273
Cdd:cd15256    71 --KIMAILLHFFFLSAFAWMLVEGLHLYSMVIKVFGSEESkHFYYYGIGWGSPLLiCI---ISLTSALDSYGesdnCWLS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 274 NDHSIPWWVIrMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYmVFAAFPI-GISS 352
Cdd:cd15256   146 LENGAIWAFV-APALFVIVVNIGILIAVTRVISRISADNYKVHGDANAFKLTAKAVAVLLPILGSSW-VFGVLAVnTHAL 223
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1937369580 353 TYQILFELcVGSFQGLVVAVLYCFLNSEVQCELKRR 388
Cdd:cd15256   224 VFQYMFAI-FNSLQGFFIFLFHCLLNSEVRAAFKHK 258
7tmB2_latrophilin-like_invertebrate cd15440
invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane ...
123-387 3.77e-16

invertebrate latrophilin-like receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; This subgroup includes latrophilin-like proteins that are found in invertebrates such as insects and worms. Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of vertebrate latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320556 [Multi-domain]  Cd Length: 259  Bit Score: 78.07  E-value: 3.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKdsvlysssgtlrcHDQPGSWVGCK 202
Cdd:cd15440     2 SALTFITYIGCIISIVCLLLAFITFTCFRNLQCDRNTIHKNLCLCLLIAEIVFLLG-------------IDQTENRTLCG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPS--VCIGAWIATRLSLEDTGCW-DTNDHSI 278
Cdd:cd15440    69 VIAGLLHYFFLAAFSWMLLEGFQLYVMLVEVFEPEKSRIKwYYLFGYGLPAliVAVSAGVDPTGYGTEDHCWlSTENGFI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 pwWVIRMPILISIVVNFA-LFISIVRILLQKLTSPDVGGNDQ-SQYKRLAKSTLLLIPLFGVHYmVFAAFPIGISSTYQI 356
Cdd:cd15440   149 --WSFVGPVIVVLLANLVfLGMAIYVMCRHSSRSASKKDASKlKNIRGWLKGSIVLVVLLGLTW-TFGLLFINQESIVMA 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1937369580 357 LFELCVGSFQGLVVAVLYCFLNSEVQCELKR 387
Cdd:cd15440   226 YIFTILNSLQGLFIFIFHCVLNEKVRKELRR 256
7tmB2_CD97 cd15438
CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
128-387 2.45e-13

CD97 antigen, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320554 [Multi-domain]  Cd Length: 261  Bit Score: 69.79  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSvlysssgtlrchdQPGSWVGCKLSLVF 207
Cdd:cd15438     7 ITKVGLSVSLFCLFLCILTFLFCRSIRGTRNTIHLHLCLSLFLAHLIFLLGIN-------------NTNNQVACAVVAGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 208 FQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYL-LIGWGIPS--VCIGAWIATRLSLEDTGCWDTNDHSIPWWVIR 284
Cdd:cd15438    74 LHYFFLAAFCWMSLEGVELYLMVVQVFNTQSLKKRYLlLIGYGVPLviVAISAAVNSKGYGTQRHCWLSLERGFLWSFLG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 285 mPILISIVVNFALFISIVRILLQKLTS--PDVGgndqsQYKRLAKSTLLLIP---LFGVHYmVFAAFPIGISSTYQILFE 359
Cdd:cd15438   154 -PVCLIILVNAIIFVITVWKLAEKFSSinPDME-----KLRKIRALTITAIAqlcILGCTW-IFGFFQFSDSTLVMSYLF 226
                         250       260
                  ....*....|....*....|....*...
gi 1937369580 360 LCVGSFQGLVVAVLYCFLNSEVQCELKR 387
Cdd:cd15438   227 TILNSLQGLFIFLLHCLLSKQVREEYSR 254
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
128-378 4.64e-12

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 65.91  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLV---KDSVLYSSSGTLrchdqpgswVGCKLS 204
Cdd:cd14964     4 ILSLLTCLGLLGNLLVLLSLVRLRKRPRSTRLLLASLAACDLLASLVVLVlffLLGLTEASSRPQ---------ALCYLI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 205 LVFFQYCIMANFYWLLVEGLYLHTLLVA-----ILPPSRCFLAYLLIGWGIPSVCIGAWIA------TRLSLEDTGCWDT 273
Cdd:cd14964    75 YLLWYGANLASIWTTLVLTYHRYFALCGplkytRLSSPGKTRVIILGCWGVSLLLSIPPLVgkgaipRYNTLTGSCYLIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 274 NDHSIPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYK-RLAKSTLLLIPLFGVHYMVFAAFPI---- 348
Cdd:cd14964   155 TTIYLTWGFLLVSFLLPLVAFLVIFSRIVLRLRRRVRAIRSAASLNTDKNlKATKSLLILVITFLLCWLPFSIVFIlhal 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369580 349 ---GISSTYQILFELCVGSFQGLVVAVLYCFLN 378
Cdd:cd14964   235 vaaGQGLNLLSILANLLAVLASTLNPFIYCLGN 267
7tmB2_GPR144 cd15255
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
196-387 1.14e-11

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR144 is an orphan receptor that belongs to the group V adhesion-GPCRs together with GPR133. The function of GPR144 has not yet been characterized, whereas GPR133 is highly expressed in the pituitary gland and is coupled to the Gs protein, leading to activation of adenylyl cyclase pathway. Moreover, genetic variations in the GPR133 have been reported to be associated with adult height and heart rate. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320383 [Multi-domain]  Cd Length: 263  Bit Score: 64.87  E-value: 1.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 196 GSWVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAI-LPPSRCFLAYLLIGWGIPSVCIGAWIATRLS--LEDTGCWd 272
Cdd:cd15255    62 GNQVACWAVTALLHLFFLAAFSWMLVEGLLLWSKVVAVnMSEDRRMKFYYVTGWGLPVVIVAVTLATSFNkyVADQHCW- 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 273 TNDHSIPWWVIRMPILISIVVNFALFISIVRILLQ------KLTSPDVGGNDQ--SQYKRLAKSTLLLIPLFGVHYMvfA 344
Cdd:cd15255   141 LNVQTDIIWAFVGPVLFVLTVNTFVLFRVVMVTVSsarrraKMLTPSSDLEKQigIQIWATAKPVLVLLPVLGLTWL--C 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1937369580 345 AFPIGISSTYQILFeLCVGSFQGLVVAVLYCFLNSEVQCELKR 387
Cdd:cd15255   219 GVLVHLSDVWAYVF-ITLNSFQGLYIFLVYAIYNSEVRNAIQR 260
7tmB2_Latrophilin_Adhesion_I cd15252
Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of ...
122-390 3.94e-11

Latrophilins and similar receptors, group I adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; Group I adhesion GPCRs consist of latrophilins (also called lectomedins or latrotoxin receptors) and ETL (EGF-TM7-latrophilin-related protein. These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320380 [Multi-domain]  Cd Length: 257  Bit Score: 63.29  E-value: 3.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDsvlysssgtlrchDQPGSWVGC 201
Cdd:cd15252     1 YNILTRITQVGIIISLVCLAICIFTFWFFRGLQSDRTTIHKNLCISLFLAELVFLIGI-------------NTTTNKIFC 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 KLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYL-LIGWGIPSVCIG--AWIATRLSLEDTGCWDTNDHSI 278
Cdd:cd15252    68 SVIAGLLHYFFLAAFAWMFIEGIQLYLMLVEVFENEGSRHKNFyIFGYGSPAVIVGvsAALGYRYYGTTKVCWLSTENYF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 PWWVIRMPILISIVVNFALFISIVRILLQKLTS-PDVGGNDQSqyKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQIL 357
Cdd:cd15252   148 IWSFIGPATLIILLNLIFLGVAIYKMFRHTAGLkPEVSCLENI--RSWARGAIALLFLLGLTWIFGVLHINHASVVMAYL 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369580 358 FELcVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15252   226 FTV-SNSLQGMFIFLFHCVLSRKVRKEYYKLFR 257
7tmB2_Latrophilin-2 cd16006
Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled ...
123-390 4.22e-10

Latrophilin-2, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320672 [Multi-domain]  Cd Length: 258  Bit Score: 59.93  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDsvlysssgtlrchDQPGSWVGCK 202
Cdd:cd16006     2 LLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGI-------------DKTEYKIACP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIG--AWIATRLSLEDTGCWDTNDHSIP 279
Cdd:cd16006    69 IFAGLLHFFFLAAFAWMCLEGVQLYLMLVEVFESEYSRKKyYYVAGYLFPATVVGvsAAIDYKSYGTEKACWLRVDNYFI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRmPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILFE 359
Cdd:cd16006   149 WSFIG-PVTFIILLNLIFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFT 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1937369580 360 LcVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd16006   228 I-FNAFQGMFIFIFHCALQKKVRKEYSKCFR 257
7tmB2_EMR_Adhesion_II cd15931
EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of ...
128-387 6.43e-10

EGF-like module receptors, group II adhesion GPCRs, member of class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the leukocyte cell-surface antigen CD97 and the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4), are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily B2 of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying numbers of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of CD97, alternative splicing results in three isoforms possessing either three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. On the other hand, EMR2 generates four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. For example, CD97, which is involved in angiogenesis and the migration and invasion of tumor cells, has been shown to promote cell aggregation in a GPS proteolysis-dependent manner. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320597 [Multi-domain]  Cd Length: 262  Bit Score: 59.45  E-value: 6.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLraisvlvkdsvlySSSGTLRCHDQPGSWVGCKLSLVF 207
Cdd:cd15931     7 INRVGVIVSLFCLGLAIFTFLLCRWIPKINTTAHLHLCLCLSM-------------SHTLFLAGIEYVENELACTVMAGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 208 FQYCIMANFYWLLVEGLYLHtLLVAILPPSRCF-------LAYLLIGWGIPSVCIG--AWIATRLSLEDTGCW-DTNDHS 277
Cdd:cd15931    74 LHYLFLASFVWMLLEALQLH-LLVRRLTKVQVIqrdglprPLLCLIGYGVPFLIVGvsALVYSDGYGEAKMCWlSQERGF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 278 IpwWVIRMPILISIVVNFALFISIVRILLQKLTspdvggNDQSQYKRLAKSTLLLIPLFGVHYM-----VFAAFPIG-IS 351
Cdd:cd15931   153 N--WSFLGPVIAIIGINWILFCATLWCLRQTLS------NMNSDISQLKDTRLLTFKAVAQLFIlgctwVLGLFQTNpVA 224
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1937369580 352 STYQILFELcVGSFQGLVVAVLYCFLNSEVQCELKR 387
Cdd:cd15931   225 LVFQYLFTI-LNSLQGAFLFLVHCLLNKEVREEYIK 259
7tmB3_Methuselah-like cd15039
Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G ...
128-390 7.12e-10

Methuselah-like subfamily B3, member of the class B family of seven-transmembrane G protein-coupled receptors; The subfamily B3 of class B GPCRs consists of Methuselah (Mth) and its closely related proteins found in bilateria. Mth was originally identified in Drosophila as a GPCR affecting stress resistance and aging. In addition to the seven transmembrane helices, Mth contains an N-terminal extracellular domain involved in ligand binding, and a third intracellular loop (IC3) required for the specificity of G-protein coupling. Drosophila Mth mutants showed an increase in average lifespan by 35% and greater resistance to a variety of stress factors, including starvation, high temperature, and paraquat-induced oxidative toxicity. Moreover, mutations in two endogenous peptide ligands of Methuselah, Stunted A and B, showed an increased in lifespan and resistance to oxidative stress induced by dietary paraquat. These results strongly suggest that the Stunted-Methuselah system plays important roles in stress response and aging.


Pssm-ID: 410632 [Multi-domain]  Cd Length: 270  Bit Score: 59.55  E-value: 7.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLH-----CTRNYIhLNLFLSFMLRAISVLVkdsvlysssgtlrchdQPGSWVGCK 202
Cdd:cd15039     7 LTLIGLIISLVFLLLTLAVYALLPELRnlhgkCLMCLV-LSLFVAYLLLLIGQLL----------------SSGDSTLCV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRC------FLAYLLIGWGIPSVCIGAWIATRLSLEDT-------- 268
Cdd:cd15039    70 ALGILLHFFFLAAFFWLNVMSFDIWRTFRGKRSSSSRskerkrFLRYSLYAWGVPLLLVAVTIIVDFSPNTDslrpgyge 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 269 -GCWDTNDHSIPWWVIrMPILISIVVNFALFISIV-RILLQKLTSPDVGGNDQSQYKRLAKSTLLLIpLFGVHYMV-FAA 345
Cdd:cd15039   150 gSCWISNPWALLLYFY-GPVALLLLFNIILFILTAiRIRKVKKETAKVQSRLRSDKQRFRLYLKLFV-IMGVTWILeIIS 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1937369580 346 FPIGISSTYQILFELCVGSfQGLVVAVLYCfLNSEVQCELKRRWR 390
Cdd:cd15039   228 WFVGGSSVLWYIFDILNGL-QGVFIFLIFV-CKRRVLRLLKKKIR 270
7tmB2_EMR cd15439
epidermal growth factor-like module-containing mucin-like hormone receptors, member of the ...
128-389 7.32e-10

epidermal growth factor-like module-containing mucin-like hormone receptors, member of the class B2 family of seven-transmembrane G protein-coupled receptors; group II adhesion GPCRs, including the epidermal growth factor (EGF)-module-containing, mucin-like hormone receptor (EMR1-4) and the leukocyte cell-surface antigen CD97, are primarily expressed in cells of the immune system. All EGF-TM7 receptors, which belong to the B2 subfamily of adhesion GPCRs, are members of group II, except for ETL (EGF-TM7-latrophilin related protein), which is classified into group I. Members of the EGF-TM7 receptors are characterized by the presence of varying number of N-terminal EGF-like domains, which play critical roles in ligand recognition and cell adhesion, linked by a stalk region to a class B seven-transmembrane domain. In the case of EMR2, alternative splicing results in four isoforms possessing either two (EGF1,2), three (EGF1,2,5), four (EGF1,2,3,5) or five (EGF1,2,3,4,5) EGF-like domains. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. EMR2 shares strong sequence homology with CD97, differing by only six amino acids. CD97 is widely expressed on lymphocytes, monocytes, macrophages, dendritic cells, granulocytes and smooth muscle cells as well as in a variety of human tumors including colorectal, gastric, esophageal pancreatic, and thyroid carcinoma. However, unlike CD97, EMR2 is not found in those of CD97-positive tumor cells and is not expressed on lymphocytes but instead on monocytes, macrophages and granulocytes. CD97 has three known ligands: CD55, decay-accelerating factor for regulation of complement system; chondroitin sulfate, a glycosaminoglycan found in the extracellular matrix; and the integrin alpha5beta1, which play a role in angiogenesis. Although EMR2 does not effectively interact with CD55, the fourth EGF-like domain of this receptor binds to chondroitin sulfate to mediate cell attachment.


Pssm-ID: 320555 [Multi-domain]  Cd Length: 263  Bit Score: 59.28  E-value: 7.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKdsvlysssgtlrcHDQPGSWVGCKLSLVF 207
Cdd:cd15439     7 ITYVGLIISLLCLFLAILTFLLCRSIRNTSTSLHLQLSLCLFLADLLFLVG-------------IDRTDNKVLCSIIAGF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 208 FQYCIMANFYWLLVEGLYLHTLL-----VAILPPSRCFLAYL-LIGWGIPSVCIGAWIATRLSLEDTG--CWDTNDHSIP 279
Cdd:cd15439    74 LHYLFLACFAWMFLEAVHLFLTVrnlkvVNYFSSHRFKKRFMyPVGYGLPAVIVAISAAVNPQGYGTPkhCWLSMEKGFI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRmPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMV--FAAFPIGISSTYqiL 357
Cdd:cd15439   154 WSFLG-PVCVIIVINLVLFCLTLWILREKLSSLNAEVSTLKNTRLLTFKAIAQLFILGCTWILglFQVGPVATVMAY--L 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1937369580 358 FELCvGSFQGLVVAVLYCFLNSEVQcELKRRW 389
Cdd:cd15439   231 FTIT-NSLQGVFIFLVHCLLNRQVR-EEYRRW 260
7tmB2_Latrophilin-1 cd16007
Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled ...
123-390 9.76e-10

Latrophilin-1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320673 [Multi-domain]  Cd Length: 258  Bit Score: 58.78  E-value: 9.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDsvlysssgtlrchDQPGSWVGCK 202
Cdd:cd16007     2 LLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLIGI-------------DKTQYQIACP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIG--AWIATRLSLEDTGCWDTNDHSIP 279
Cdd:cd16007    69 IFAGLLHFFFLAAFSWLCLEGVQLYLMLVEVFESEYSRKKyYYLCGYCFPALVVGisAAIDYRSYGTEKACWLRVDNYFI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRmPILISIVVNFALFISIVRILLQKLT--SPDVGGNDQSQYKRLAKSTLLLipLFGVHYmVFAAFPIGISSTYQIL 357
Cdd:cd16007   149 WSFIG-PVSFVIVVNLVFLMVTLHKMIRSSSvlKPDSSRLDNIKSWALGAITLLF--LLGLTW-AFGLLFINKESVVMAY 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369580 358 FELCVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd16007   225 LFTTFNAFQGMFIFIFHCALQKKVHKEYSKCLR 257
7tmB2_ETL cd15437
Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; ...
122-387 1.61e-09

Epidermal Growth Factor, latrophilin and seven transmembrane domain-containing protein 1; member of the class B2 family of seven-transmembrane G protein-coupled receptors; ETL (EGF-TM7-latrophilin-related protein) belongs to Group I adhesion GPCRs, which also include latrophilins (also called lectomedins or latrotoxin receptors). All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. ETL, for instance, contains EGF-like repeats, which also present in other EGF-TM7 adhesion GPCRs, such as Cadherin EGF LAG seven-pass G-type receptors (CELSR1-3), EGF-like module receptors (EMR1-3), CD97, and Flamingo. ETL is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320553 [Multi-domain]  Cd Length: 258  Bit Score: 58.35  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 122 YILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKdsvLYSSSGTLRCHDQPGswvgc 201
Cdd:cd15437     1 YNVLTRITQLGIIISLICLSMCIFTFWFFSEIQSTRTTIHKNLCCSLFLAELIFLIG---INMNANKLFCSIIAG----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 202 klslvFFQYCIMANFYWLLVEGLYLHTLLVAILpPSRCFL--AYLLIGWGIPSVCIG--AWIATRLSLEDTGCWDTNDHS 277
Cdd:cd15437    73 -----LLHYFFLAAFAWMCIEGIHLYLIVVGVI-YNKGFLhkNFYIFGYGSPAVVVGisAALGYKYYGTTKVCWLSTENN 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 278 IPWWVIRMPILIsIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQIL 357
Cdd:cd15437   147 FIWSFIGPACLI-ILVNLLAFGVIIYKVFRHTAMLKPEVSCYENIRSCARGALALLFLLGATWIFGVLHVVYGSVVTAYL 225
                         250       260       270
                  ....*....|....*....|....*....|
gi 1937369580 358 FELcVGSFQGLVVAVLYCFLNSEVQCELKR 387
Cdd:cd15437   226 FTI-SNAFQGMFIFIFLCVLSRKIQEEYYR 254
7tmB2_CELSR3 cd15993
Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of ...
134-394 2.98e-09

Cadherin EGF LAG seven-pass G-type receptor 3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. Celsr3 is expressed in both the developing and adult mouse brain. It has been functionally implicated in proper neuronal migration and axon guidance in the CNS. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320659 [Multi-domain]  Cd Length: 254  Bit Score: 57.54  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 134 SVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVkdsvlysssGTLRCHDQpgswVGCKLSLVFFQYCIM 213
Cdd:cd15993    13 SASLAALVLTFSVLTCLRGLKSNTRGIHSNIAAALFLSELLFLL---------GINRTENQ----FLCTVVAILLHYFFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 214 ANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIGawIATRLSLEDTG----CWdTNDHSIPWWVIRMPIL 288
Cdd:cd15993    80 STFAWLFVQGLHIYRMQTEARNVNFGAMRfYYAIGWGVPAIITG--LAVGLDPEGYGnpdfCW-ISIHDKLVWSFAGPIV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 289 ISIVVNFALFISIVRILlqklTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHYMvFAAFPIGISSTYQILFELCVGSFQGL 368
Cdd:cd15993   157 VVIVMNGVMFLLVARMS----CSPGQKETKKTSVLMTLRSSFLLLLLISATWL-FGLLAVNNSVLAFHYLHAILCCLQGL 231
                         250       260
                  ....*....|....*....|....*.
gi 1937369580 369 VVAVLYCFLNSEVQcelkRRWRGLCL 394
Cdd:cd15993   232 AVLLLFCVLNEEVQ----EAWKLACL 253
7tmB2_Latrophilin-3 cd16005
Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled ...
123-384 4.71e-09

Latrophilin-3, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320671 [Multi-domain]  Cd Length: 258  Bit Score: 56.88  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKdsvlysssgtLRCHDQPgswVGCK 202
Cdd:cd16005     2 LLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIG----------INRTDQP---IACA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYL-LIGWGIPS--VCIGAWIATRLSLEDTGCWDTNDHSIP 279
Cdd:cd16005    69 VFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFyLVGYGMPAliVAVSAAVDYRSYGTDKVCWLRLDTYFI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRMPILISIVVNFALFISIVRILLQK-LTSPDVGGNDQsqYKRLAKSTLLLIPLFGVHYmVFAAFPIGISSTYQILF 358
Cdd:cd16005   149 WSFIGPATLIIMLNVIFLGIALYKMFHHTaILKPESGCLDN--IKSWVIGAIALLCLLGLTW-AFGLMYINESTVIMAYL 225
                         250       260
                  ....*....|....*....|....*.
gi 1937369580 359 ELCVGSFQGLVVAVLYCFLNSEVQCE 384
Cdd:cd16005   226 FTIFNSLQGMFIFIFHCVLQKKVRKE 251
7tmB2_Latrophilin cd15436
Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; ...
123-390 1.23e-08

Latrophilins, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Latrophilins (also called lectomedins or latrotoxin receptors) belong to Group I adhesion GPCRs, which also include ETL (EGF-TM7-latrophilin-related protein). These receptors are a member of the adhesion family (subclass B2) that belongs to the class B GPCRs. Three subtypes of latrophilins have been identified: LPH1 (latrophilin-1), LPH2, and LPH3. The latrophilin-1 is a brain-specific calcium-independent receptor of alpha-latrotoxin, a potent presynaptic neurotoxin from the venom of the black widow spider that induces massive neurotransmitter release from sensory and motor neurons as well as endocrine cells, leading to nerve-terminal degeneration. Latrophilin-2 and -3, although sharing strong sequence homology to latrophilin-1, do not bind alpha-latrotoxin. While latrophilin-3 is also brain specific, latrophilin-2 is ubiquitously distributed. The endogenous ligands for these two receptors are unknown. ETL, a seven transmembrane receptor containing EGF-like repeats is highly expressed in heart, where developmentally regulated, as well as in normal smooth cells. The function of the ETL is unknown. All adhesion GPCRs possess large N-terminal extracellular domains containing multiple structural motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, coupled to a seven-transmembrane domain. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320552 [Multi-domain]  Cd Length: 258  Bit Score: 55.57  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 123 ILVKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKdsvlysssgtlrcHDQPGSWVGCK 202
Cdd:cd15436     2 LLLFVITWVGIVISLVCLLICIFTFCFFRGLQTDRNTIHKNLCINLFIAELLFLIG-------------INRTQYTIACP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 203 LSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYL-LIGWGIPS--VCIGAWIATRLSLEDTGCWDTNDHSIP 279
Cdd:cd15436    69 IFAGLLHFFFLAAFCWLCLEGVQLYLLLVEVFESEYSRRKYFyLCGYSFPAlvVAVSAAIDYRSYGTEKACWLRVDNYFI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRmPILISIVVNFA-LFISIVRILLQKLTSPDVGGNdQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTYQILF 358
Cdd:cd15436   149 WSFIG-PVTFVITLNLVfLVITLHKMVSHSDLLKPDSSR-LDNIKSWALGAIALLFLLGLTWSFGLMFINEESVVMAYLF 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1937369580 359 ELcVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15436   227 TI-FNAFQGVFIFIFHCALQKKVRKEYSKCLR 257
7tmB2_CELSR1 cd15991
Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of ...
125-391 1.65e-08

Cadherin EGF LAG seven-pass G-type receptor 1, member of the class B2 family of seven-transmembrane G protein-coupled receptors; The group IV adhesion GPCRs include the cadherin EGF LAG seven-pass G-type receptors (CELSRs) and their Drosophila homolog Flamingo (also known as Starry night). These receptors are also classified as that belongs to the EGF-TM7 group of subfamily B2 adhesion GPCRs, because they contain EGF-like domains. Functionally, the group IV receptors act as key regulators of many physiological processes such as endocrine cell differentiation, neuronal migration, dendrite growth, axon, guidance, lymphatic vessel and valve formation, and planar cell polarity (PCP) during embryonic development. Three mammalian orthologs of Flamingo, Celsr1-3, are widely expressed in the nervous system from embryonic development until the adult stage. Each Celsr exhibits different expression patterns in the developing brain, suggesting that they serve distinct functions. Mutations of CELSR1 cause neural tube defects in the nervous system, while mutations of CELSR2 are associated with coronary heart disease. Moreover, CELSR1 and several other PCP signaling molecules, such as dishevelled, prickle, frizzled, have been shown to be upregulated in B lymphocytes of chronic lymphocytic leukemia patients. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. In the case of CELSR/Flamingo/Starry night, their extracellular domains comprise nine cadherin repeats linked to a series of epidermal growth factor (EGF)-like and laminin globular (G)-like domains. The cadherin repeats contain sequence motifs that mediate calcium-dependent cell-cell adhesion by homophilic interactions. Moreover, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320657 [Multi-domain]  Cd Length: 254  Bit Score: 55.24  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 125 VKAIYTLGYSVSLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDsvlysssgtlrchDQPGSWVGCKLS 204
Cdd:cd15991     4 LKIITYTTVSLSLVALLITFILLVLIRTLRSNLHSIHKNLVAALFFSELIFLIGI-------------NQTENPFVCTVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 205 LVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLA-YLLIGWGIPSVCIGawIATRLSLEDTG----CWdTNDHSIP 279
Cdd:cd15991    71 AILLHYFYMSTFAWMFVEGLHIYRMLTEVRNINTGHMRfYYVVGWGIPAIITG--LAVGLDPQGYGnpdfCW-LSVQDTL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 WWVIRMPILISIVVNFALFISIVRILLQKltspdvggnDQSQYKRLAKSTLLLIPlFGVHYMVFAAFPIGISS------T 353
Cdd:cd15991   148 IWSFAGPIGIVVIINTVIFVLAAKASCGR---------RQRYFEKSGVISMLRTA-FLLLLLISATWLLGLMAvnsdtlS 217
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1937369580 354 YQILFELcVGSFQGLVVAVLYCFLNSEVQCELKRRWRG 391
Cdd:cd15991   218 FHYLFAI-FSCLQGIFIFFFHCIFNKEVRKHLKNVLTG 254
7tmB2_GPR113 cd15253
orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G ...
128-388 5.26e-08

orphan adhesion receptor GPR113, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR113 is an orphan receptor that belongs to group VI adhesion-GPCRs along with GPR110, GPR111, GPR115, and GPR116. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in ligand recognition as well as cell-cell adhesion and cell-matrix interactions, linked by a stalk region to a class B seven-transmembrane domain. GPR113 contains a hormone binding domain and one EGF (epidermal grown factor) domain, and is primarily expressed in a subset of taste receptor cells. In addition, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions. However, several adhesion GPCRs, including GPR 111, GPR115, and CELSR1, are predicted to be non-cleavable at the GAIN domain because of the lack of a consensus catalytic triad sequence (His-Leu-Ser/Thr) within their GPS.


Pssm-ID: 320381 [Multi-domain]  Cd Length: 271  Bit Score: 54.00  E-value: 5.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLhCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGTlrchdQPGSWVGCKLSLVF 207
Cdd:cd15253     7 LSQVGLGASILALLLCLGIYRLVWRS-VVRNKISYFRHMTLVNIAFSLLLADTCFLGATFL-----SAGHESPLCLAAAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 208 F-QYCIMANFYWLLVEGLYL--------HTLLVAILPPSRCFLAYLlIGWGIPSVCIGAWIATRLSLEDTGCWdTNDHSI 278
Cdd:cd15253    81 LcHFFYLATFFWMLVQALMLfhqllfvfHQLAKRSVLPLMVTLGYL-CPLLIAAATVAYYYPKRQYLHEGACW-LNGESG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 279 PWWVIRMPILISIVVNFAlfisIVRILLQKLTSPDVG----GNDQSQYKRLAKSTLLLIPLFGVHYMVFAAFPIGISSTY 354
Cdd:cd15253   159 AIYAFSIPVLAIVLVNLL----VLFVVLMKLMRPSVSegppPEERKALLSIFKALLVLTPVFGLTWGLGVATLTGESSQV 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1937369580 355 QILFELCVGSFQGLVVAVLYCFLNSEVQCELKRR 388
Cdd:cd15253   235 SHYGFAILNAFQGVFILLFGCLMDKKVREALLKR 268
7tmB2_BAI_Adhesion_VII cd15251
brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 ...
131-390 6.79e-08

brain-specific angiogenesis inhibitors, group VII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediate direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320379  Cd Length: 253  Bit Score: 53.41  E-value: 6.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 131 LGYSVSLMSLTTGSII-ICLFRKLHCTRNYIHLNLFLSFMLRAISVLVkdsvlysssGTLRCHDQpgswVGCKLSLVFFQ 209
Cdd:cd15251    10 VGCGVSCLALLTLLAIyAAFWRYIRSERSIILINFCLSIISSNILILV---------GQTQTLNK----GVCTMTAAFLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 210 YCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIA---TRLSLEDTGCWDTNDHSIPWWVIRmP 286
Cdd:cd15251    77 FFFLSSFCWVLTEAWQSYMAVTGRMRTRLIRKRFLCLGWGLPALVVAVSVGftrTKGYGTSSYCWLSLEGGLLYAFVG-P 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 287 ILISIVVNFALFIsivrILLQKLTSPDvGGNDQSQYKRLakSTLLLIPLFGVHYM-VFAAFPIGISSTYQILFELcVGSF 365
Cdd:cd15251   156 AAAVVLVNMVIGI----LVFNKLVSRD-GISDNAMASLW--SSCVVLPLLALTWMsAVLAMTDRRSVLFQILFAV-FDSL 227
                         250       260
                  ....*....|....*....|....*
gi 1937369580 366 QGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15251   228 QGFVIVMVHCILRREVQDAVKCRMG 252
7tmB2_GPR126-like_Adhesion_VIII cd15258
orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family ...
128-387 1.42e-06

orphan GPR126 and related proteins, group VIII adhesion GPCRs, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Group VIII adhesion GPCRs include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. GPR126, on the other hand, is required for Schwann cells, but not oligodendrocyte myelination in the peripheral nervous system. Gpr64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320386 [Multi-domain]  Cd Length: 267  Bit Score: 49.34  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKLhcTRNY---IHLNLFLSFMLRAISVLVKDSVLYSSSGTLrchdqpgswvgCKLS 204
Cdd:cd15258     7 ISYVGCGISAIFLAITILTYIAFRKL--RRDYpskIHMNLCAALLLLNLAFLLSSWIASFGSDGL-----------CIAV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 205 LVFFQYCIMANFYWLLVEGLYLHTLLVAILPP--SRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTGCWDTNDHSIP--- 279
Cdd:cd15258    74 AVALHYFLLACLTWMGLEAFHLYLLLVKVFNTyiRRYILKLCLVGWGLPALLVTLVLSVRSDNYGPITIPNGEGFQNdsf 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 280 -WwvIRMPILISIVV----------NFALFISIVRILLQKLTSPDVGGNDQSQYKrlAKSTLLLIPLFGVHY--MVFAAF 346
Cdd:cd15258   154 cW--IRDPVVFYITVvgyfgltflfNMVMLATVLVQICRLREKAQATPRKRALHD--LLTLLGLTFLLGLTWglAFFAWG 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1937369580 347 PIGISSTYqiLFELCvGSFQGLVVAVLYCFLNSEVQCELKR 387
Cdd:cd15258   230 PFNLPFLY--LFAIF-NSLQGFFIFIWYCSMKENVRKQWRA 267
7tmB2_BAI2 cd15988
brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 ...
131-382 2.02e-05

brain-specific angiogenesis inhibitor 2, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320654 [Multi-domain]  Cd Length: 291  Bit Score: 46.10  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 131 LGYSVSLMSLTTGSIIICLF-RKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGtlrchdqpgswvgCKLSLVFFQ 209
Cdd:cd15988    10 IGCAVSCMALLILLAIYAAFwRFIRSERSIILLNFCLSILASNILILVGQSQTLSKGV-------------CTMTAAFLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 210 YCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIA-TRLSLEDTG--CWDTNDHSIPWWVIRmP 286
Cdd:cd15988    77 FFFLSSFCWVLTEAWQSYLAVIGRMRTRLVRKRFLCLGWGLPALVVAVSVGfTRTKGYGTAsyCWLSLEGGLLYAFVG-P 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 287 ILISIVVNFALFIsivrILLQKLTSPDvGGNDQSQYKRL-----AKSTLLL----------------------------- 332
Cdd:cd15988   156 AAVIVLVNMLIGI----IVFNKLMSRD-GISDKSKKQRAgseaePCSSLLLkcskcgvvssaamssatassamaslwssc 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1937369580 333 --IPLFGVHYM-VFAAFPIGISSTYQILFELcVGSFQGLVVAVLYCFLNSEVQ 382
Cdd:cd15988   231 vvLPLLALTWMsAVLAMTDRRSILFQVLFAV-FNSVQGFVIITVHCFLRREVQ 282
7tmB2_GPR112 cd15997
Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane ...
201-390 2.76e-05

Probable G protein-coupled receptor 112, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR112 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR114, and GPR126. GPR112 is specifically expressed in normal enterochromatin cells and gastrointestinal neuroendocrine carcinoma cells, but its biological function is unknown. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320663  Cd Length: 269  Bit Score: 45.42  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 201 CKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPP--SRCFLAYLLIGWGIPSVCIGAWIATRLSLEDTG--------- 269
Cdd:cd15997    70 CITVAAFLHYFLLASFTWMGLEAVHMYFALVKVFNIyiPNYILKFCIAGWGIPAVVVALVLAINKDFYGNElssdslhps 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 270 ---CWDTNDHSIPWWVIRMPILIsIVVNFALFIsIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVHY-MVFAA 345
Cdd:cd15997   150 tpfCWIQDDVVFYISVVAYFCLI-FLCNISMFI-TVLIQIRSMKAKKPSRNWKQGFLHDLKSVASLTFLLGLTWgFAFFA 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1937369580 346 F-PIGISSTYqiLFELCvGSFQGLVVAVLYCFLNSEVQcelkRRWR 390
Cdd:cd15997   228 WgPVRIFFLY--LFSIC-NTLQGFFIFVFHCLMKENVR----KQWR 266
7tmB2_GPR126 cd15996
orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G ...
201-390 2.68e-04

orphan adhesion receptor GPR126, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR126 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR64, GPR97, GPR112, and GPR114. GPR126 is required in Schwann cells for proper differentiation and myelination via G-Protein Activation. GPR126 is believed to couple to G(s)-protein, which leads to activation of adenylate cyclase for cAMP production. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320662  Cd Length: 271  Bit Score: 42.57  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 201 CKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPP--SRCFLAYLLIGWGIPSVCIGAWIATRLSLE------------ 266
Cdd:cd15996    70 CITVAVLLHFFLLATFTWMGLEAIHMYIALVKVFNTyiRRYILKFCIIGWGLPALIVSIVLASTNDNYgygyygkdkdgq 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 267 --DTGCWDTNDhSIPWWVIRMPILISIVVNFALFIsIVRILLQKLTSPDVGGNDQSQYKRLAKSTLLLIPLFGVH--YMV 342
Cdd:cd15996   150 ggDEFCWIKNP-VVFYVTCAAYFGIMFLMNVAMFI-VVMVQICGRNGKRSNRTLREEILRNLRSVVSLTFLLGMTwgFAF 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1937369580 343 FAAFPIGISSTYqiLFELcVGSFQGLVVAVLYCFLNSEVQcelkRRWR 390
Cdd:cd15996   228 FAWGPVNLAFMY--LFTI-FNSLQGLFIFVFHCALKENVQ----KQWR 268
7tmB2_BAI3 cd15989
brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 ...
131-390 8.44e-04

brain-specific angiogenesis inhibitor 3, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320655 [Multi-domain]  Cd Length: 293  Bit Score: 41.21  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 131 LGYSVSLMSLTTGSII-ICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGtlrchdqpgswvgCKLSLVFFQ 209
Cdd:cd15989    12 VGCGLSCLALITLAVVyAALWRYIRSERSIILINFCLSIISSNILILVGQTQTHNKGI-------------CTMTTAFLH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 210 YCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWIA---TRLSLEDTGCWDTNDHSIPWWVI--- 283
Cdd:cd15989    79 FFFLASFCWVLTEAWQSYMAVTGKIRTRLIRKRFLCLGWGLPALVVAISMGftkAKGYGTPHYCWLSLEGGLLYAFVgpa 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 284 RMPILISIVVNFALFISIVR---ILLQKL------------------------TSPDVGGNDQSQYKRLAKSTLLLIPLF 336
Cdd:cd15989   159 AAVVLVNMVIGILVFNKLVSrdgILDKKLkhragqmsephsgltlkcakcgvvSTTALSATTASNAMASLWSSCVVLPLL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1937369580 337 GVHYM-VFAAFPIGISSTYQILFELcVGSFQGLVVAVLYCFLNSEVQCELKRRWR 390
Cdd:cd15989   239 ALTWMsAVLAMTDKRSILFQILFAV-FDSLQGFVIVMVHCILRREVQDAFRCRLR 292
7tmB2_GPR128 cd15257
orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G ...
201-376 1.60e-03

orphan adhesion receptor GPR128, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR128 is an orphan receptor of the adhesion family (subclass B2) that belongs to the class B GPCRs. Expression of GPR128 was detected in the mouse intestinal mucosa and is thought to be involved in energy balance, as its knockout mice showed a decrease in body weight gain and an increase in intestinal contraction frequency compared to wild-type controls. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. These include, for example, EGF (epidermal growth factor)-like domains in CD97, Celsr1 (cadherin family member), Celsr2, Celsr3, EMR1 (EGF-module-containing mucin-like hormone receptor-like 1), EMR2, EMR3, and Flamingo; two laminin A G-type repeats and nine cadherin domains in Flamingo and its human orthologs Celsr1, Celsr2 and Celsr3; olfactomedin-like domains in the latrotoxin receptors; and five or four thrombospondin type 1 repeats in BAI1 (brain-specific angiogenesis inhibitor 1), BAI2 and BAI3. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320385 [Multi-domain]  Cd Length: 303  Bit Score: 40.24  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 201 CKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYL--LIGWGIPSVCIGAWIATRLSLEDTGCWDTNDH-- 276
Cdd:cd15257    93 CTAVAALLHYFLLVTFMWNAVYSAQLYLLLIRMMKPLPEMFILQasAIGWGIPAVVVAITLGATYRFPTSLPVFTRTYrq 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 277 -SIPW---------------WVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRLakSTLLLIPLFGVHY 340
Cdd:cd15257   173 eEFCWlaaldknfdikkpllWGFLLPVGLILITNVILFIMTSQKVLKKNNKKLTTKKRSYMKKIY--ITVSVAVVFGITW 250
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1937369580 341 mVFAAFPI----GISSTYQILFELCvGSFQGLVVAVLYCF 376
Cdd:cd15257   251 -ILGYLMLvnndLSKLVFSYIFCIT-NTTQGVQIFILYTW 288
7tmB2_BAI1 cd15990
brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 ...
180-388 2.04e-03

brain-specific angiogenesis inhibitor 1, a group VII adhesion GPCR, member of the class B2 family of seven-transmembrane G protein-coupled receptors; Brain-specific angiogenesis inhibitors (BAI1-3) constitute the group VII of cell-adhesion receptors that have been implicated in vascularization of glioblastomas. They belong to the B2 subfamily of class B GPCRs, are predominantly expressed in the brain, and are only present in vertebrates. Three BAIs, like all adhesion receptors, are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. For example, BAI1 N-terminus contain an integrin-binding RGD (Arg-Gly-Asp) motif in addition to five thrombospondin type 1 repeats (TSRs), which are known to regulate the anti-angiogenic activity of thrombospondin-1, whereas BAI2 and BAI3 have four TSRs, but do not possess RGD motifs. The TSRs are functionally involved in cell attachment, activation of latent TGF-beta, inhibition of angiogenesis and endothelial cell migration. The TSRs of BAI1 mediates direct binding to phosphatidylserine, which enables both recognition and internalization of apoptotic cells by phagocytes. Thus, BAI1 functions as a phosphatidylserine receptor that forms a trimeric complex with ELMO and Dock180, leading to activation of Rac-GTPase which promotes the binding and phagocytosis of apoptotic cells. BAI3 can also interact with the ELMO-Dock180 complex to activate the Rac pathway and can also bind to secreted C1ql proteins of the C1Q complement family via its N-terminal TSRs. BAI3 and its ligands C1QL1 are highly expressed during synaptogenesis and are involved in synapse specificity. Moreover, BAI2 acts as a transcription repressor to regulate vascular endothelial growth factor (VEGF) expression through interaction with GA-binding protein gamma (GABP). The N-terminal extracellular domains of all three BAIs also contain an evolutionarily conserved GPCR-autoproteolysis inducing (GAIN) domain, which undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif to generate N- and C-terminal fragments (NTF and CTF), a putative hormone-binding domain (HBD), and multiple N-glycosylation sites. The C-terminus of each BAI subtype ends with a conserved Gln-Thr-Glu-Val (QTEV) motif known to interact with PDZ domain-containing proteins, but only BAI1 possesses a proline-rich region, which may be involved in protein-protein interactions.


Pssm-ID: 320656  Cd Length: 267  Bit Score: 39.97  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 180 SVLYSSSGTLRCHDQPGSWVGCKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPPSRCFLAYLLIGWGIPSVCIGAWI 259
Cdd:cd15990    50 SIISSNALILIGQTQTRNKVVCTLVAAFLHFFFLSSFCWVLTEAWQSYMAVTGRLRNRIIRKRFLCLGWGLPALVVAISV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 260 A-TRLSLEDTG--CWDTNDHSIPWWVIRmPILISIVVNFALFIsivrILLQKLTSPDvGGNDQSQYKRLAKS---TLLLI 333
Cdd:cd15990   130 GfTKAKGYGTVnyCWLSLEGGLLYAFVG-PAAAVVLVNMVIGI----LVFNKLVSKD-GITDKKLKERAGASlwsSCVVL 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1937369580 334 PLFGVHYM-VFAAFPIGISSTYQILFELcVGSFQGLVVAVLYCFLNSEVQCELKRR 388
Cdd:cd15990   204 PLLALTWMsAVLAITDRRSALFQILFAV-FDSLEGFVIVMVHCILRREVQDAVKCR 258
7tmB2_GPR97 cd15442
orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G ...
127-377 3.98e-03

orphan adhesion receptor GPR97, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR97 is an orphan receptor that has been classified into the group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR112, GPR114, and GPR126. GPR97 is identified as a lymphatic adhesion receptor that is specifically expressed in lymphatic endothelium, but not in blood vascular endothelium, and is shown to regulate migration of lymphatic endothelial cells via the small GTPases RhoA and cdc42. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320558 [Multi-domain]  Cd Length: 277  Bit Score: 39.01  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 127 AIYTLGYSVSLMSLttgSIIICLFRKLHCTRNY--------IHLNLFLSFMLRAISVLVKDSVLYSSSGTLrchdqpgsw 198
Cdd:cd15442     6 TISSAGCGVSMVFL---IFTIILYFFLRFTYQKfksedapkIHVNLSSSLLLLNLAFLLNSGVSSRAHPGL--------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 199 vgCKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPP--SRCFLAYLLIGWGIPSVCI---------GAW----IATRL 263
Cdd:cd15442    74 --CKALGGVTHYFLLCCFTWMAIEAFHLYLLAIKVFNTyiHHYFAKLCLVGWGFPALVVtitgsinsyGAYtimdMANRT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 264 SLEdtGCWDTNDHSIPWWVIRMPILISIVVNFALFISIVRILLQKLTSPDVGGnDQSQYKRLAKSTLLLIPLFGVHYMVF 343
Cdd:cd15442   152 TLH--LCWINSKHLTVHYITVCGYFGLTFLFNTVVLGLVAWKIFHLQSATAGK-EKCQAWKGGLTVLGLSCLLGVTWGLA 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1937369580 344 AAFPIGISSTYQILFELcVGSFQGLVVAVLYCFL 377
Cdd:cd15442   229 FFTYGSMSVPTVYIFAL-LNSLQGLFIFIWFVIL 261
7tmB2_GPR114 cd15443
orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G ...
128-255 4.15e-03

orphan adhesion receptor GPR114, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR114 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include GPR56, GPR64, GPR97, GPR112, and GPR126. GPR114 is mainly found in granulocytes (polymorphonuclear leukocytes), and GPR114-transfected cells induced an increase in cAMP levels via coupling to G(s) protein. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320559 [Multi-domain]  Cd Length: 268  Bit Score: 38.97  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 128 IYTLGYSVSLMSLTTGSIIICLFRKL-HCTRNYIHLNLFLSFMLRAISVLVKDSVLYSSSGtlrchdqpgswVGCKLSLV 206
Cdd:cd15443     7 ISIVGCSISAAASLLTILLHFFSRKQpKDSTTRIHMNLLGSLFLLNGSFLLSPPLATSQST-----------WLCRAAAA 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1937369580 207 FFQYCIMANFYWLLVEGLYLHTLLVAI--LPPSRCFLAYLLIGWGIPSVCI 255
Cdd:cd15443    76 LLHYSLLCCLTWMAIEGFHLYLLLVKVynIYIRRYVLKLCVLGWGLPALIV 126
7tmB2_GPR56 cd15995
orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G ...
136-251 4.41e-03

orphan adhesion receptor GPR56, member of the class B2 family of seven-transmembrane G protein-coupled receptors; GPR56 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR64, GPR97, GPR112, GPR114, and GPR126. GPR56 is involved in the regulation of oligodendrocyte development and myelination in the central nervous system via coupling to G(12/13) proteins, which leads to the activation of RhoA GTPase. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320661  Cd Length: 269  Bit Score: 38.66  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 136 SLMSLTTGSIIICLFRKLHCTRNYIHLNLFLSFMLRAISVLVKDSVLYSssgtlrchdqpGSWVGCKLSLVFFQYCIMAN 215
Cdd:cd15995    16 ALASVFTIAFYLCSRRKPRDYTIYVHMNLLLAIFLLDTSFLISEPLALT-----------GSEAACRAGGMFLHFSLLAC 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1937369580 216 FYWLLVEGLYLHTLLVAILPP--SRCFLAYLLIGWGIP 251
Cdd:cd15995    85 LTWMGIEGYNLYRLVVEVFNTyvPHFLLKLCAVGWGLP 122
7tmB2_GPR64 cd15444
orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B ...
201-390 5.37e-03

orphan adhesion receptor GPR64 and related proteins, member of subfamily B2 of the class B secretin-like receptors of seven-transmembrane G protein-coupled receptors; GPR64 is an orphan receptor that has been classified as that belongs to the Group VIII of adhesion GPCRs. Other members of the Group VII include orphan GPCRs such as GPR56, GPR97, GPR112, GPR114, and GPR126. GPR64 is mainly expressed in the epididymis of male reproductive tract, and targeted deletion of GPR64 causes sperm stasis and efferent duct blockage due to abnormal fluid reabsorption, resulting in male infertility. GPR64 is also over-expressed in Ewing's sarcoma (ES), as well as upregulated in other carcinomas from kidney, prostate or lung, and promotes invasiveness and metastasis in ES via the upregulation of placental growth factor (PGF) and matrix metalloproteinase (MMP) 1. The adhesion receptors are characterized by the presence of large N-terminal extracellular domains containing multiple adhesion motifs, which play critical roles in cell-cell adhesion and cell-matrix interactions, that are coupled to a class B seven-transmembrane domain. Furthermore, almost all adhesion receptors, except GPR123, contain an evolutionarily conserved GPCR- autoproteolysis inducing (GAIN) domain that undergoes autoproteolytic processing at the GPCR proteolysis site (GPS) motif located immediately N-terminal to the first transmembrane region, to generate N- and C-terminal fragments (NTF and CTF), which may serve important biological functions.


Pssm-ID: 320560 [Multi-domain]  Cd Length: 271  Bit Score: 38.65  E-value: 5.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 201 CKLSLVFFQYCIMANFYWLLVEGLYLHTLLVAILPP--SRCFLAYLLIGWGIPSVCIGAWIATRLSL------------- 265
Cdd:cd15444    71 CISVAVFLHYFLLVSFTWMGLEAFHMYLALVKVFNTyiRKYILKFCIVGWGVPAVVVAIVLAVSKDNyglgsygkspngs 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369580 266 EDTGCWDTNDHSIPWWVIRMPILIsIVVNFALFISIVRILLQKLTSPDVGGNDQSQYKRL---AKSTLLLIPLFGVHYmv 342
Cdd:cd15444   151 TDDFCWINNNIVFYITVVGYFCVI-FLLNISMFIVVLVQLCRIKKQKQLGAQRKTSLQDLrsvAGITFLLGITWGFAF-- 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1937369580 343 FAAFPIGISSTYqiLFELcVGSFQGLVVAVLYCFLNSEVqcelKRRWR 390
Cdd:cd15444   228 FAWGPVNLAFMY--LFAI-FNTLQGFFIFIFYCVAKENV----RKQWR 268
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH