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Conserved domains on  [gi|755503680|ref|XP_011238378|]
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probable G-protein coupled receptor 149 isoform X1 [Mus musculus]

Protein Classification

G protein-coupled receptor family protein; olfactory receptor subfamily 2A protein( domain architecture ID 11606634)

G protein-coupled receptor family protein is a seven-transmembrane G protein-coupled receptor (7TM-GPCR) family protein which typically transmits an extracellular signal into the cell by the conformational rearrangement of the 7TM helices and by the subsequent binding and activation of an intracellular heterotrimeric G protein; GPCR ligands include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters| olfactory receptor (OR) subfamily 2A protein, such as human olfactory receptor 2A2 and related proteins in other mammals and sauropsids; ORs play a central role in olfaction, the sense of smell, and belong to the class A rhodopsin-like family of seven-transmembrane G protein-coupled receptors (7TM GPCRs)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
37-375 8.66e-109

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. All GPCRs have 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.


:

Pssm-ID: 320139  Cd Length: 256  Bit Score: 325.18  E-value: 8.66e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  37 LFCLICIMTLAALVGSIFSLVSLLTMQYRTVLSILVTSWSVDDLLSVLSVAIFMVLQWPKEaqGYFQSLCTTSALLYMCQ 116
Cdd:cd15011    2 LFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETD--GLPQPLCTTSALLYLFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 117 GLSSNLKATLIVCYNFYTMNRTVESQSSSwRLGQVLGVTLTVWAVSLLLASLPLCGWGVFVRTPWGCLTDCSSPYVLLLF 196
Cdd:cd15011   80 GLSSNLKASLIASYNFYTTKKLGWLQTTK-RSVRVPWAVLTIWAASLLLSALPLCGWGSFVPTSWGCLVDCQSSYILFLF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 197 AVYASAFGLLAVLSVPLTHQLLCSEEPlrlhanyqeisrgastpgtpaaagrvlclppedveipalrctggcspssdVVF 276
Cdd:cd15011  159 SLYSLCFCILVVLSVPLTYQLLCSDET--------------------------------------------------VSF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 277 apgqpaasgagagrrenpgtpqgtnsfplslAQKRFSLILALTKVILWLPMMIHMVVKHVVGFQSLPVDMLSFLLSLLAS 356
Cdd:cd15011  189 -------------------------------AQKRFSLILALTKVILWLPMMIQMVVQHVTGFQSLSLETLSFLLTLLAA 237
                        330
                 ....*....|....*....
gi 755503680 357 SVTPVFVLSKRWAHLPCGC 375
Cdd:cd15011  238 AVTPLFVLSERWIHLPCGC 256
 
Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
37-375 8.66e-109

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. All GPCRs have 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.


Pssm-ID: 320139  Cd Length: 256  Bit Score: 325.18  E-value: 8.66e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  37 LFCLICIMTLAALVGSIFSLVSLLTMQYRTVLSILVTSWSVDDLLSVLSVAIFMVLQWPKEaqGYFQSLCTTSALLYMCQ 116
Cdd:cd15011    2 LFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETD--GLPQPLCTTSALLYLFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 117 GLSSNLKATLIVCYNFYTMNRTVESQSSSwRLGQVLGVTLTVWAVSLLLASLPLCGWGVFVRTPWGCLTDCSSPYVLLLF 196
Cdd:cd15011   80 GLSSNLKASLIASYNFYTTKKLGWLQTTK-RSVRVPWAVLTIWAASLLLSALPLCGWGSFVPTSWGCLVDCQSSYILFLF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 197 AVYASAFGLLAVLSVPLTHQLLCSEEPlrlhanyqeisrgastpgtpaaagrvlclppedveipalrctggcspssdVVF 276
Cdd:cd15011  159 SLYSLCFCILVVLSVPLTYQLLCSDET--------------------------------------------------VSF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 277 apgqpaasgagagrrenpgtpqgtnsfplslAQKRFSLILALTKVILWLPMMIHMVVKHVVGFQSLPVDMLSFLLSLLAS 356
Cdd:cd15011  189 -------------------------------AQKRFSLILALTKVILWLPMMIQMVVQHVTGFQSLSLETLSFLLTLLAA 237
                        330
                 ....*....|....*....
gi 755503680 357 SVTPVFVLSKRWAHLPCGC 375
Cdd:cd15011  238 AVTPLFVLSERWIHLPCGC 256
 
Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
37-375 8.66e-109

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. All GPCRs have 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.


Pssm-ID: 320139  Cd Length: 256  Bit Score: 325.18  E-value: 8.66e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  37 LFCLICIMTLAALVGSIFSLVSLLTMQYRTVLSILVTSWSVDDLLSVLSVAIFMVLQWPKEaqGYFQSLCTTSALLYMCQ 116
Cdd:cd15011    2 LFCLTLIIALLTLLGSIYSLLSLLKMRNKTTLSVLVASLSVDDLLSVVPVSIFMLMQWETD--GLPQPLCTTSALLYLFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 117 GLSSNLKATLIVCYNFYTMNRTVESQSSSwRLGQVLGVTLTVWAVSLLLASLPLCGWGVFVRTPWGCLTDCSSPYVLLLF 196
Cdd:cd15011   80 GLSSNLKASLIASYNFYTTKKLGWLQTTK-RSVRVPWAVLTIWAASLLLSALPLCGWGSFVPTSWGCLVDCQSSYILFLF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 197 AVYASAFGLLAVLSVPLTHQLLCSEEPlrlhanyqeisrgastpgtpaaagrvlclppedveipalrctggcspssdVVF 276
Cdd:cd15011  159 SLYSLCFCILVVLSVPLTYQLLCSDET--------------------------------------------------VSF 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 277 apgqpaasgagagrrenpgtpqgtnsfplslAQKRFSLILALTKVILWLPMMIHMVVKHVVGFQSLPVDMLSFLLSLLAS 356
Cdd:cd15011  189 -------------------------------AQKRFSLILALTKVILWLPMMIQMVVQHVTGFQSLSLETLSFLLTLLAA 237
                        330
                 ....*....|....*....
gi 755503680 357 SVTPVFVLSKRWAHLPCGC 375
Cdd:cd15011  238 AVTPLFVLSERWIHLPCGC 256
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
37-243 3.71e-23

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: 99.04  E-value: 3.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  37 LFCLICIMTLAALVGSIFSLVSLLTMQYR-TVLSILVTSWSVDDLLSVLSVAIFMVLQWPKEAQGYFQSLCTTSALLYMC 115
Cdd:cd14964    1 TTIILSLLTCLGLLGNLLVLLSLVRLRKRpRSTRLLLASLAACDLLASLVVLVLFFLLGLTEASSRPQALCYLIYLLWYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 116 QGLSSnLKATLIVCYNFYTMNRTVESQSSSWRLGQVLGVTLTVWAVSLLLASLPLCGWGVFVRTPWgcltdCSSPYVLLL 195
Cdd:cd14964   81 ANLAS-IWTTLVLTYHRYFALCGPLKYTRLSSPGKTRVIILGCWGVSLLLSIPPLVGKGAIPRYNT-----LTGSCYLIC 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755503680 196 FAVYASAFGLLAVLSVPLTHQLLCSEEPLRLHANYQEISRGASTPGTP 243
Cdd:cd14964  155 TTIYLTWGFLLVSFLLPLVAFLVIFSRIVLRLRRRVRAIRSAASLNTD 202
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
37-209 8.39e-12

rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor superfamily; Class A rhodopsin-like receptors constitute about 90% of all GPCRs. The class A GPCRs include the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. All GPCRs have 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. Based on sequence similarity, GPCRs can be divided into six major classes: class A (rhodopsin-like family), class B (Methuselah-like, adhesion and secretin-like receptor family), class C (metabotropic glutamate receptor family), class D (fungal mating pheromone receptors), class E (cAMP receptor family), and class F (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: 410626 [Multi-domain]  Cd Length: 275  Bit Score: 65.77  E-value: 8.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  37 LFCLICIMTLAALVGSIFSLVSLL-TMQYRTVLSILVTSWSVDDLLSVLSVAIFMVLQWPKEAQGYFQSLCTTSALLYMC 115
Cdd:cd00637    1 LAVLYILIFVVGLVGNLLVILVILrNRRLRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLGRWWFGDALCKLLGFLQSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 116 QGLSSNLKATLI-------VCYNFYTMNRtvesqsssWRLGQVLGVTLTVWAVSLLLASLPLCGWGVFVRTPWGCLTDCS 188
Cdd:cd00637   81 SLLASILTLTAIsvdrylaIVHPLRYRRR--------FTRRRAKLLIALIWLLSLLLALPPLLGWGVYDYGGYCCCCLCW 152
                        170       180
                 ....*....|....*....|....*...
gi 755503680 189 SP-------YVLLLFAVYASAFGLLAVL 209
Cdd:cd00637  153 PDltlskayTIFLFVLLFLLPLLVIIVC 180
7tmA_GPR135 cd15212
G protein-coupled receptor 135, member of the class A family of seven-transmembrane G ...
40-181 1.15e-03

G protein-coupled receptor 135, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR135, also known as the somatostatin- and angiotensin-like peptide receptor (SALPR), is found in various tissues including eye, brain, cervix, stomach, and testis. Pharmacological studies have shown that relaxin-3 (R3) is a high-affinity endogenous ligand for GPR135. R3 has recently been identified as a new member of the insulin/relaxin family of peptide hormones and is exclusively expressed in the brain neurons. In addition to GPR135, R3 also acts as an agonist for GPR142, a pseudogene in the rat, and can activate LGR7 (leucine repeat-containing G-protein receptor-7), which is the main receptor for relaxin-1 (R1) and relaxin-2 (R2). While R1 and R2 are hormones primarily associated with reproduction and pregnancy, R3 is involved in neuroendocrine and sensory processing. All GPCRs have 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.


Pssm-ID: 320340 [Multi-domain]  Cd Length: 285  Bit Score: 40.91  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  40 LICIMTLAALVGSIFSLVSLLTMQYRTVLSILVTSWSVDDLLSV---LSVAIFMVLQWPKEAQGyfQSLCTTSALLYMCQ 116
Cdd:cd15212    7 LLAIFLLSSLGNCAVIGVIVKHRQLRTVTNAFILSLSLSDLLTAllcLPFAFLTLFSRPGWLFG--DRLCLANGFFNACF 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755503680 117 GLSSNLKATLIVCYNFYTMNRTVESQSSSWRLGQVLGVtltVWAVSLLLaSLPlcgWGVFVRTPW 181
Cdd:cd15212   85 GIVSTLTMTLISFDRYYAIVRQPQGKIGRRRALQLLAA---AWLTALGF-SLP---WYLLASAPE 142
7tmA_Prostanoid_R cd14981
G protein-coupled receptors for prostanoids, member of the class A family of ...
43-219 1.38e-03

G protein-coupled receptors for prostanoids, member of the class A family of seven-transmembrane G protein-coupled receptors; Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters.


Pssm-ID: 320112 [Multi-domain]  Cd Length: 288  Bit Score: 40.69  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  43 IMTLAALVGSIFSLVSLL---TMQYRTVLSILVTSWSVDDLLSVLSVAIFMVLQWPKEAQGYF-QSLCTTSALLYMCQGL 118
Cdd:cd14981    9 LMFVFGVLGNLLALIVLArssKSHKWSVFYRLVAGLAITDLLGILLTSPVVLAVYASNFEWDGgQPLCDYFGFMMSFFGL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 119 SSnlkaTLIVC---------------YNFYTMNRtvesqssswRLGQVLGVtltVWAVSLLLASLPLCGWGVFVRTPWG- 182
Cdd:cd14981   89 SS----LLIVCamaverflaithpffYNSHVKKR---------RARLMLGA---VWAFALLIASLPLLGLGSYVLQYPGt 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755503680 183 -CLTDCSSPYVLLlfAVYASAFGLLAVLSVPLThqLLC 219
Cdd:cd14981  153 wCFLDFYSKNTGD--AAYAYLYSILGLLILLVT--LLC 186
7tmA_MCHR2 cd15339
melanin concentrating hormone receptor 2, member of the class A family of seven-transmembrane ...
40-218 9.34e-03

melanin concentrating hormone receptor 2, member of the class A family of seven-transmembrane G protein-coupled receptors; Melanin-concentrating hormone receptor (MCHR) binds melanin concentrating hormone and is presumably involved in the neuronal regulation of food intake and energy homeostasis. Despite strong homology with somatostatin receptors, MCHR does not appear to bind somatostatin. Two MCHRs have been characterized in vertebrates, MCHR1 and MCHR2. MCHR1 is expressed in all mammals, whereas MCHR2 is only expressed in the higher order mammals, such as humans, primates, and dogs, and is not found in rodents. All GPCRs have 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.


Pssm-ID: 320461 [Multi-domain]  Cd Length: 283  Bit Score: 38.26  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680  40 LICIMTLAALVGSIFSLVSLLTMQYRTVLSILVTSWSVDDLLSVLsVAIFMVLQWPKEAQGYFQS-LCTTSALLYMCQGL 118
Cdd:cd15339    6 FIGILCSTGLVGNILVLFTIIRSRKKTVPDIYVCNLAVADLVHII-VMPFLIHQWARGGEWVFGSpLCTIITSLDTCNQF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503680 119 SSNLKATLIVCYNFYTM---NRTVESQSSSWrlgqVLGVTLTVWAVSLLLAsLPLCGWGVFVRTPWG---CLTDCSSPYV 192
Cdd:cd15339   85 ACSAIMTAMSLDRYIALvhpFRLTSLRTRSK----TIRINLLVWAASFILV-LPVWVYAKVIKFRDGlesCAFNLTSPDD 159
                        170       180
                 ....*....|....*....|....*.
gi 755503680 193 LLLFAVYASAFGLLAVLSVPLTHQLL 218
Cdd:cd15339  160 VLWYTLYQTITTFFFPLPLILICYIL 185
7tmA_photoreceptors_insect cd15079
insect photoreceptors R1-R6 and similar proteins, member of the class A family of ...
149-192 9.83e-03

insect photoreceptors R1-R6 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes the insect photoreceptors and their closely related proteins. The Drosophila eye is composed of about 800 unit eyes called ommatidia, each of which contains eight photoreceptor cells (R1-R8). The six outer photoreceptors (R1-R6) function like the vertebrate rods and are responsible for motion detection in dim light and image formation. The R1-R6 photoreceptors express a blue-absorbing pigment, Rhodopsin 1(Rh1). The inner photoreceptors (R7 and R8) are considered the equivalent of the color-sensitive vertebrate cone cells, which express a range of different pigments. The R7 photoreceptors express one of two different UV absorbing pigments, either Rh3 or Rh4. Likewise, the R8 photoreceptors express either the blue absorbing pigment Rh5 or green absorbing pigment Rh6. These photoreceptors belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320207 [Multi-domain]  Cd Length: 292  Bit Score: 38.33  E-value: 9.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 755503680 149 GQVLGVTLTVWAVSLLLASLPLC-GWGVFVrtPWGCLTDCSSPYV 192
Cdd:cd15079  113 GKALLLILFIWLYALPWALLPLLfGWGRYV--PEGFLTSCSFDYL 155
 
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.
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