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Conserved domains on  [gi|24652173|ref|NP_724822|]
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transient receptor potential-like, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
48-784 0e+00

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


The actual alignment was detected with superfamily member TIGR00870:

Pssm-ID: 454755 [Multi-domain]  Cd Length: 743  Bit Score: 685.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173     48 AVERGDMPNVRRILQKAlrhQHININCMDPLGRRAL-TLAIDNENLEMVELLVVMG--VETKDALLHAINAEFVEAVELL 124
Cdd:TIGR00870   24 AAERGDLASVYRDLEEP---KKLNINCPDRLGRSALfVAAIENENLELTELLLNLScrGAVGDTLLHAISLEYVDAVEAI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    125 LEHEELIYKEGEPYsWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVphdiRCGCEECVRLTAEDSLRHS 204
Cdd:TIGR00870  101 LLHLLAAFRKSGPL-ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPA----RACGDFFVKSQGVDSFYHG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    205 LSRVNIYRALCSPSLICLTSNDP--IITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNY 282
Cdd:TIGR00870  176 ESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNH 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    283 D--PQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDKVICIAQVAVLFPLYCLIYMC 360
Cdd:TIGR00870  256 QglTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFVIGLKFPELSDMYLI 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    361 APNCRTGQLMRKPFMKFLIHASSYLFFLFILILVSQRadddFVRIFGTtrmkkelaeqELRQRGQTPSKLELIVVMYVIG 440
Cdd:TIGR00870  336 APLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVA----YYRPTRT----------DLRVTGLQQTPLEMLIVTWVDG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    441 FVWEEVQEIFAVGMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQAteiardpQMAYIPREKWHDFDPQLIAEGLFAA 520
Cdd:TIGR00870  402 LRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVT-------QAFLVLREHWLRFDPTLIEEALFAF 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    521 ANVFSALKLVHLFSINPHLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLWYFAALEKSKCYVLPGGEAdwgsh 599
Cdd:TIGR00870  475 ALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPHARSC----- 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    600 gdsCMKWRRFGNLFESSQSLFWASFGMVGLDDFElsgiKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHS 679
Cdd:TIGR00870  550 ---EKQGNAYSTLFETSQELFWAIIGLGDLLANE----HKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDA 622
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    680 DTEWKFARTKLWMSYFEDSATLPPPFNVLPSVK----WVIRIFRKSSKTIDRQRSKKRKEQEQFSE------------YD 743
Cdd:TIGR00870  623 DEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKsfvgLFKRIEKHDGKKRQRWCRRVEEVNWTTWErkaetliedglhYQ 702
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 24652173    744 NIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYE 784
Cdd:TIGR00870  703 RVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE 743
TRP_CaM_bind1 super family cl48806
Calmodulin binding site 1 (CBS1) found in Drosophila melanogaster transient receptor potential ...
798-883 2.98e-03

Calmodulin binding site 1 (CBS1) found in Drosophila melanogaster transient receptor potential protein (TRP) and similar proteins; TRP is a light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. TRP and another retinal-specific protein, TRPL, act together in the light response, and are activated by fatty acids and metabolic stress. TRP is also required for olfactory adaptation and may be involved in olfactory system development. The TRP tail contains two calmodulin (CaM) binding sites (called CBS1 and CBS2), which binds to the CaM N-lobe and C-lobe, respectively. The model corresponds to CaM binding site 1.


The actual alignment was detected with superfamily member cd23650:

Pssm-ID: 467881  Cd Length: 66  Bit Score: 37.31  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  798 SANKKERQPrprrikvwERRLMKGFQVAPVqngceldafgnvngqgemqEIKVESIPSKPAKETAKERFQRVARTVL--L 875
Cdd:cd23650    3 AVGKKGRQM--------ERRLMKGFNIGLV-------------------EGLIKSVFESDDKKSPKDRFKRLARLIGrkK 55

                 ....*...
gi 24652173  876 QSTTHKWN 883
Cdd:cd23650   56 KKKKKDWN 63
PHA03247 super family cl33720
large tegument protein UL36; Provisional
961-1069 3.03e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   961 KPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKiSRKSSPAPTPTPTPGVSHTALSQFRNRELPlcpskliANSAPSAP 1040
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA-SLSESRESLPSPWDPADPPAAVLAPAAALP-------PAASPAGP 2827
                          90       100
                  ....*....|....*....|....*....
gi 24652173  1041 TAPPKKSAPTAPTPTYKPTThAPFSVEGG 1069
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPP-PSLPLGGS 2855
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
48-784 0e+00

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 685.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173     48 AVERGDMPNVRRILQKAlrhQHININCMDPLGRRAL-TLAIDNENLEMVELLVVMG--VETKDALLHAINAEFVEAVELL 124
Cdd:TIGR00870   24 AAERGDLASVYRDLEEP---KKLNINCPDRLGRSALfVAAIENENLELTELLLNLScrGAVGDTLLHAISLEYVDAVEAI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    125 LEHEELIYKEGEPYsWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVphdiRCGCEECVRLTAEDSLRHS 204
Cdd:TIGR00870  101 LLHLLAAFRKSGPL-ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPA----RACGDFFVKSQGVDSFYHG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    205 LSRVNIYRALCSPSLICLTSNDP--IITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNY 282
Cdd:TIGR00870  176 ESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNH 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    283 D--PQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDKVICIAQVAVLFPLYCLIYMC 360
Cdd:TIGR00870  256 QglTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFVIGLKFPELSDMYLI 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    361 APNCRTGQLMRKPFMKFLIHASSYLFFLFILILVSQRadddFVRIFGTtrmkkelaeqELRQRGQTPSKLELIVVMYVIG 440
Cdd:TIGR00870  336 APLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVA----YYRPTRT----------DLRVTGLQQTPLEMLIVTWVDG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    441 FVWEEVQEIFAVGMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQAteiardpQMAYIPREKWHDFDPQLIAEGLFAA 520
Cdd:TIGR00870  402 LRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVT-------QAFLVLREHWLRFDPTLIEEALFAF 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    521 ANVFSALKLVHLFSINPHLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLWYFAALEKSKCYVLPGGEAdwgsh 599
Cdd:TIGR00870  475 ALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPHARSC----- 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    600 gdsCMKWRRFGNLFESSQSLFWASFGMVGLDDFElsgiKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHS 679
Cdd:TIGR00870  550 ---EKQGNAYSTLFETSQELFWAIIGLGDLLANE----HKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDA 622
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    680 DTEWKFARTKLWMSYFEDSATLPPPFNVLPSVK----WVIRIFRKSSKTIDRQRSKKRKEQEQFSE------------YD 743
Cdd:TIGR00870  623 DEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKsfvgLFKRIEKHDGKKRQRWCRRVEEVNWTTWErkaetliedglhYQ 702
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 24652173    744 NIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYE 784
Cdd:TIGR00870  703 RVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
187-246 6.92e-32

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 118.46  E-value: 6.92e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    187 CGCEECVRLTAEDSLRHSLSRVNIYRALCSPSLICLTSNDPIITAFQLSWELRNLALTEQ 246
Cdd:pfam08344    1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVEP 60
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-179 1.83e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   48 AVERGDMPNVRRILQKAlrhqhININCMDPLGRRALTLAIDNENLEMVELLVVMG--VETKD-----ALLHAINAEFVEA 120
Cdd:COG0666   94 AARNGDLEIVKLLLEAG-----ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGadVNAQDndgntPLHLAAANGNLEI 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652173  121 VellleheeliykegepySW---QKVDINtAMFAPDITPLMLAAHKNNFEILRILLDRGAAV 179
Cdd:COG0666  169 V-----------------KLlleAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
538-687 1.38e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 59.05  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  538 HLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLwyfaalEKSkcyvlPGGEADWGSHGDSCMKWRR--FGNLFE 614
Cdd:cd22196  453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI------EDG-----PPKGDVNTSQKECVCKSGYnsYNSLYS 521
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652173  615 SSQSLFWASFGMVGLDDFELSGIKSYtrFWGLLMfgSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFAR 687
Cdd:cd22196  522 TCLELFKFTIGMGDLEFTENYKFKEV--FIFLLI--SYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
155-177 2.57e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.57e-03
                            10        20
                    ....*....|....*....|...
gi 24652173     155 TPLMLAAHKNNFEILRILLDRGA 177
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGA 26
TRP_CaM_bind1 cd23650
Calmodulin binding site 1 (CBS1) found in Drosophila melanogaster transient receptor potential ...
798-883 2.98e-03

Calmodulin binding site 1 (CBS1) found in Drosophila melanogaster transient receptor potential protein (TRP) and similar proteins; TRP is a light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. TRP and another retinal-specific protein, TRPL, act together in the light response, and are activated by fatty acids and metabolic stress. TRP is also required for olfactory adaptation and may be involved in olfactory system development. The TRP tail contains two calmodulin (CaM) binding sites (called CBS1 and CBS2), which binds to the CaM N-lobe and C-lobe, respectively. The model corresponds to CaM binding site 1.


Pssm-ID: 467881  Cd Length: 66  Bit Score: 37.31  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  798 SANKKERQPrprrikvwERRLMKGFQVAPVqngceldafgnvngqgemqEIKVESIPSKPAKETAKERFQRVARTVL--L 875
Cdd:cd23650    3 AVGKKGRQM--------ERRLMKGFNIGLV-------------------EGLIKSVFESDDKKSPKDRFKRLARLIGrkK 55

                 ....*...
gi 24652173  876 QSTTHKWN 883
Cdd:cd23650   56 KKKKKDWN 63
PHA03247 PHA03247
large tegument protein UL36; Provisional
961-1069 3.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   961 KPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKiSRKSSPAPTPTPTPGVSHTALSQFRNRELPlcpskliANSAPSAP 1040
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA-SLSESRESLPSPWDPADPPAAVLAPAAALP-------PAASPAGP 2827
                          90       100
                  ....*....|....*....|....*....
gi 24652173  1041 TAPPKKSAPTAPTPTYKPTThAPFSVEGG 1069
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPP-PSLPLGGS 2855
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
48-784 0e+00

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 685.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173     48 AVERGDMPNVRRILQKAlrhQHININCMDPLGRRAL-TLAIDNENLEMVELLVVMG--VETKDALLHAINAEFVEAVELL 124
Cdd:TIGR00870   24 AAERGDLASVYRDLEEP---KKLNINCPDRLGRSALfVAAIENENLELTELLLNLScrGAVGDTLLHAISLEYVDAVEAI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    125 LEHEELIYKEGEPYsWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVphdiRCGCEECVRLTAEDSLRHS 204
Cdd:TIGR00870  101 LLHLLAAFRKSGPL-ELANDQYTSEFTPGITALHLAAHRQNYEIVKLLLERGASVPA----RACGDFFVKSQGVDSFYHG 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    205 LSRVNIYRALCSPSLICLTSNDP--IITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNY 282
Cdd:TIGR00870  176 ESPLNAAACLGSPSIVALLSEDPadILTADSLGNTLLHLLVMENEFKAEYEELSCQMYNFALSLLDKLRDSKELEVILNH 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    283 D--PQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDKVICIAQVAVLFPLYCLIYMC 360
Cdd:TIGR00870  256 QglTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSLYWLEELDGWRRKQSVLELIVVFVIGLKFPELSDMYLI 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    361 APNCRTGQLMRKPFMKFLIHASSYLFFLFILILVSQRadddFVRIFGTtrmkkelaeqELRQRGQTPSKLELIVVMYVIG 440
Cdd:TIGR00870  336 APLSRLGQFKWKPFIKFIFHSASYLYFLYLIIFTSVA----YYRPTRT----------DLRVTGLQQTPLEMLIVTWVDG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    441 FVWEEVQEIFAVGMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQAteiardpQMAYIPREKWHDFDPQLIAEGLFAA 520
Cdd:TIGR00870  402 LRLGEEKLIWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVT-------QAFLVLREHWLRFDPTLIEEALFAF 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    521 ANVFSALKLVHLFSINPHLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLWYFAALEKSKCYVLPGGEAdwgsh 599
Cdd:TIGR00870  475 ALVLSWLNLLYIFRGNQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPHARSC----- 549
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    600 gdsCMKWRRFGNLFESSQSLFWASFGMVGLDDFElsgiKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHS 679
Cdd:TIGR00870  550 ---EKQGNAYSTLFETSQELFWAIIGLGDLLANE----HKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDA 622
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    680 DTEWKFARTKLWMSYFEDSATLPPPFNVLPSVK----WVIRIFRKSSKTIDRQRSKKRKEQEQFSE------------YD 743
Cdd:TIGR00870  623 DEEWKFQRAKLWMSYEREGGTCPPPFNIIPGPKsfvgLFKRIEKHDGKKRQRWCRRVEEVNWTTWErkaetliedglhYQ 702
                          730       740       750       760
                   ....*....|....*....|....*....|....*....|.
gi 24652173    744 NIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYE 784
Cdd:TIGR00870  703 RVMKRLIKRYVLAEQRPRDDEGTTEEETKELKQDISSLRFE 743
TRP_2 pfam08344
Transient receptor ion channel II; This domain is found in the transient receptor ion channel ...
187-246 6.92e-32

Transient receptor ion channel II; This domain is found in the transient receptor ion channel (Trp) family of proteins. There is strong evidence that Trp proteins are structural elements of calcium-ion entry channels activated by G protein-coupled receptors. This domain does not tend to appear with the TRP domain (pfam06011) but is often found to the C-terminus of Ankyrin repeats (pfam00023).


Pssm-ID: 462438  Cd Length: 60  Bit Score: 118.46  E-value: 6.92e-32
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    187 CGCEECVRLTAEDSLRHSLSRVNIYRALCSPSLICLTSNDPIITAFQLSWELRNLALTEQ 246
Cdd:pfam08344    1 CGCDECKAERERDSLRHSLSRLNAYRALASPAYISLTSEDPILTAFELSWELRRLAFVEP 60
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
383-680 2.89e-28

Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.


Pssm-ID: 459842 [Multi-domain]  Cd Length: 238  Bit Score: 114.29  E-value: 2.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    383 SYLFFLFILILVsqradddfvrIFGTTRMKKELAEQELRQrgqTPSKLELIVVMYVIGFVWEEVQEIFAVG-MKSYLRNM 461
Cdd:pfam00520    1 SRYFELFILLLI----------LLNTIFLALETYFQPEEP---LTTVLEILDYVFTGIFTLEMLLKIIAAGfKKRYFRSP 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    462 WNFIDFLRNSLYVSVMCLRAFayiqqateiardpqmayiprekwhdfdpqliaeGLFAAANVFSALKLVHLFSINPHLGP 541
Cdd:pfam00520   68 WNILDFVVVLPSLISLVLSSV---------------------------------GSLSGLRVLRLLRLLRLLRLIRRLEG 114
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    542 LQI---SLGRMVIDIVKFFFIYTLVLFAFACGLNQLLWYFaalekskcyvlpggeadWGSHGDSCMKWRRFGNLFESSQS 618
Cdd:pfam00520  115 LRTlvnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGK-----------------LKTWENPDNGRTNFDNFPNAFLW 177
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652173    619 LFWASFGmVGLDDFELSGIKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHSD 680
Cdd:pfam00520  178 LFQTMTT-EGWGDIMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-179 1.83e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   48 AVERGDMPNVRRILQKAlrhqhININCMDPLGRRALTLAIDNENLEMVELLVVMG--VETKD-----ALLHAINAEFVEA 120
Cdd:COG0666   94 AARNGDLEIVKLLLEAG-----ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGadVNAQDndgntPLHLAAANGNLEI 168
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652173  121 VellleheeliykegepySW---QKVDINtAMFAPDITPLMLAAHKNNFEILRILLDRGAAV 179
Cdd:COG0666  169 V-----------------KLlleAGADVN-ARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
431-673 1.96e-09

Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.


Pssm-ID: 462341 [Multi-domain]  Cd Length: 225  Bit Score: 59.21  E-value: 1.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    431 ELIVVMYVIGFVWEEVQEIFAVGmKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYI--QQATEIARDPQMAYIPRE---KW 505
Cdd:pfam08016   14 EIVFVVFFLYFVVEEILKIRKHR-PSYLRSVWNLLDLAIVILSVVLIVLNIYRDFlaDRLIKSVEASPVTFIDFDrvaQL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    506 HdfdpqlIAEGLFAAANVF-SALKLVHLFSINPHLGPLQISLGRMVIDIVKFFFIYTLVLFAFAcglnQLLwyfaaleks 584
Cdd:pfam08016   93 D------NLYRIILAFLVFlTWLKLFKVLRFNKTMSLFTKTLSRAWKDLAGFALMFVIFFFAYA----QFG--------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173    585 kcYVLPGGEADwgshgdscmkwrRFGNLFESSQSLFWASfgmvgLDDFELSGIKSYTRFWGLLMFGSYSVINVIVLLNLL 664
Cdd:pfam08016  154 --YLLFGTQAP------------NFSNFVKSILTLFRTI-----LGDFGYNEIFSGNRVLGPLLFLTFVFLVIFILLNLF 214

                   ....*....
gi 24652173    665 IAMMSNSYA 673
Cdd:pfam08016  215 LAIINDSYV 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-195 4.98e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   60 ILQKALRHQHININCMDPLGRRALTLAIDNENLEMVELLVVMG--VETKD-----ALLHAINAEFVEAVellleheELIY 132
Cdd:COG0666   68 LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGadVNARDkdgetPLHLAAYNGNLEIV-------KLLL 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652173  133 KEGepyswqkVDINtAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVPHD---------IRCGCEECVRL 195
Cdd:COG0666  141 EAG-------ADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNdgetplhlaAENGHLEIVKL 204
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
538-687 1.38e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 59.05  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  538 HLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLwyfaalEKSkcyvlPGGEADWGSHGDSCMKWRR--FGNLFE 614
Cdd:cd22196  453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI------EDG-----PPKGDVNTSQKECVCKSGYnsYNSLYS 521
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24652173  615 SSQSLFWASFGMVGLDDFELSGIKSYtrFWGLLMfgSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFAR 687
Cdd:cd22196  522 TCLELFKFTIGMGDLEFTENYKFKEV--FIFLLI--SYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
Ank_2 pfam12796
Ankyrin repeats (3 copies);
48-177 3.10e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 3.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173     48 AVERGDMPNVRRILQKalrhqHININCMDPLGRRALTLAIDNENLEMVELLVvmgvetkdallhainaefveavellleh 127
Cdd:pfam12796    4 AAKNGNLELVKLLLEN-----GADANLQDKNGRTALHLAAKNGHLEIVKLLL---------------------------- 50
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 24652173    128 eeliykegepyswQKVDINtaMFAPDITPLMLAAHKNNFEILRILLDRGA 177
Cdd:pfam12796   51 -------------EHADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGA 85
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
538-687 1.22e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 52.57  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  538 HLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLwyfaalekskcyvlpgGEADWGSHGDscmkwrrFGNLFESS 616
Cdd:cd21882  431 MLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVILF----------------QTEDPNKLGE-------FRDYPDAL 487
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24652173  617 QSLFWASFGMVglddfELSGIKSYT-RFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFAR 687
Cdd:cd21882  488 LELFKFTIGMG-----DLPFNENVDfPFVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-179 2.27e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 50.72  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   48 AVERGDMPNVRRILQKalrhqHININCMDPLGRRALTLAIDNENLEMVELLVVMG--VETKD-----ALLHAINAEFVEA 120
Cdd:COG0666  127 AAYNGNLEIVKLLLEA-----GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGadVNARDndgetPLHLAAENGHLEI 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24652173  121 VELlleheelIYKEGepyswqkVDINTAMFApDITPLMLAAHKNNFEILRILLDRGAAV 179
Cdd:COG0666  202 VKL-------LLEAG-------ADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADL 245
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
539-684 2.51e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  539 LGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLnqllwyfaalekskcYVLPGGEADwgshgDSCMKWRRFGNLFESSQ 617
Cdd:cd22192  447 LGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAF---------------YMIFQTEDP-----DSLGHFYDFPMTLFSTF 506
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24652173  618 SLFwasfgmVGLDDFELSGiKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWK 684
Cdd:cd22192  507 ELF------LGLIDGPANY-TVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
538-687 1.08e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 46.33  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  538 HLGPLQISLGRMVI-DIVKFFFIYTLVLFAFACGLNQLLwyfaalekSKCYVLPGGEADWGSHGDSCMKWRRFgnlfess 616
Cdd:cd22193  436 SMGIYSVMIQKVILrDLLRFLFVYLLFLFGFAVALVSLI--------EKCSSDKKDCSSYGSFSDAVLELFKL------- 500
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652173  617 qslfwasfgMVGLDDFELSGIKSYTRFWGLLMFgSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFAR 687
Cdd:cd22193  501 ---------TIGMGDLEFQENSTYPAVFLILLL-TYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQR 561
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
552-687 1.44e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 46.00  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  552 DIVKFFFIYTLVLFAFACGLNQLLWYF--AALEKSKCYVLPGGEADWGSHGDSCmkwrrFGNLFESSQSLFWASFGMVGL 629
Cdd:cd22197  466 DLLRFLLVYLVFLFGFAVALVSLSREApsPKAPEDNNSTVTEQPTVGQEEEPAP-----YRSILDASLELFKFTIGMGEL 540
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  630 DdfelsgIKSYTRFWGLLMFG--SYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFAR 687
Cdd:cd22197  541 A------FQEQLRFRGVVLLLllAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQK 594
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-186 2.12e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 44.56  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   48 AVERGDMPNVRRILQKalrhqHININCMDPLGRRALTLAIDNENLEMVELLVVMG--VETKD-----ALLHAINAEFVEA 120
Cdd:COG0666  160 AAANGNLEIVKLLLEA-----GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGadVNAKDndgktALDLAAENGNLEI 234
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24652173  121 VELLLEHEELIYKEGepyswqkvdintamfAPDITPLMLAAHKNNFEILRILLDRGAAVPVPHDIR 186
Cdd:COG0666  235 VKLLLEAGADLNAKD---------------KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
552-690 6.59e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  552 DIVKFFFIYTLVLFAFACGLNQLLwyfaalekSKCyvlpggeadwgSHGDSCmkwRRFGNLFESSQSLFWASfgmVGLDD 631
Cdd:cd22194  512 DVLKFLLVYILFLLGFGVALASLI--------EDC-----------PDDSEC---SSYGSFSDAVLELFKLT---IGLGD 566
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24652173  632 FELSGIKSYTRFWGLLMFgSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKF--ARTKL 690
Cdd:cd22194  567 LEIQQNSKYPILFLLLLI-TYVILTFVLLLNMLIALMGETVENVSKESERIWRLqrARTIL 626
Ank_4 pfam13637
Ankyrin repeats (many copies);
48-99 8.23e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 8.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 24652173     48 AVERGDMPNVRRILQKalrhqHININCMDPLGRRALTLAIDNENLEMVELLV 99
Cdd:pfam13637    8 AAASGHLELLRLLLEK-----GADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
155-177 2.57e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.57e-03
                            10        20
                    ....*....|....*....|...
gi 24652173     155 TPLMLAAHKNNFEILRILLDRGA 177
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGA 26
TRP_CaM_bind1 cd23650
Calmodulin binding site 1 (CBS1) found in Drosophila melanogaster transient receptor potential ...
798-883 2.98e-03

Calmodulin binding site 1 (CBS1) found in Drosophila melanogaster transient receptor potential protein (TRP) and similar proteins; TRP is a light-sensitive calcium channel that is required for inositide-mediated Ca(2+) entry in the retina during phospholipase C (PLC)-mediated phototransduction. TRP and another retinal-specific protein, TRPL, act together in the light response, and are activated by fatty acids and metabolic stress. TRP is also required for olfactory adaptation and may be involved in olfactory system development. The TRP tail contains two calmodulin (CaM) binding sites (called CBS1 and CBS2), which binds to the CaM N-lobe and C-lobe, respectively. The model corresponds to CaM binding site 1.


Pssm-ID: 467881  Cd Length: 66  Bit Score: 37.31  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173  798 SANKKERQPrprrikvwERRLMKGFQVAPVqngceldafgnvngqgemqEIKVESIPSKPAKETAKERFQRVARTVL--L 875
Cdd:cd23650    3 AVGKKGRQM--------ERRLMKGFNIGLV-------------------EGLIKSVFESDDKKSPKDRFKRLARLIGrkK 55

                 ....*...
gi 24652173  876 QSTTHKWN 883
Cdd:cd23650   56 KKKKKDWN 63
PHA03247 PHA03247
large tegument protein UL36; Provisional
961-1069 3.03e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.85  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24652173   961 KPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKiSRKSSPAPTPTPTPGVSHTALSQFRNRELPlcpskliANSAPSAP 1040
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVA-SLSESRESLPSPWDPADPPAAVLAPAAALP-------PAASPAGP 2827
                          90       100
                  ....*....|....*....|....*....
gi 24652173  1041 TAPPKKSAPTAPTPTYKPTThAPFSVEGG 1069
Cdd:PHA03247 2828 LPPPTSAQPTAPPPPPGPPP-PSLPLGGS 2855
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
155-179 3.13e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 3.13e-03
                           10        20
                   ....*....|....*....|....*
gi 24652173    155 TPLMLAAHKNNFEILRILLDRGAAV 179
Cdd:pfam13606    4 TPLHLAARNGRLEIVKLLLENGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-181 5.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.68e-03
                           10        20
                   ....*....|....*....|....*..
gi 24652173    155 TPLMLAAHKNNFEILRILLDRGAAVPV 181
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNL 44
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
155-179 9.03e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 9.03e-03
                           10        20
                   ....*....|....*....|....*.
gi 24652173    155 TPLMLAA-HKNNFEILRILLDRGAAV 179
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADV 29
 
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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