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Conserved domains on  [gi|767978002|ref|XP_011533508|]
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short transient receptor potential channel 4 isoform X1 [Homo sapiens]

Protein Classification

transient-receptor-potential channel family protein( domain architecture ID 1750128)

transient-receptor-potential ion channel protein conducts cations such as calcium into cells; belongs to the Transient Receptor Family (TC. 1.A.4)

Gene Ontology:  GO:0070588|GO:0005262|GO:0070679
PubMed:  20025796|18535090|20861159
SCOP:  4000366
TCDB:  1.A.4

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 ...
 1-334 4.61e-165

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: 487.28  E-value: 4.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    1 MWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTA 78
Cdd:TIGR00870 410 IWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRG 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   79 NSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGI---RCEKQNNAFSTLFETLQSLFWS 154
Cdd:TIGR00870 490 NQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQGNAYSTLFETSQELFWA 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  155 IFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLP 234
Cdd:TIGR00870 570 IIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCP 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  235 TPFNVIPSPKSLWYLIKWIWTHLCKK---KMRRKPESFGTIGvrtqhRRAADNLRRH-HQYQEVMRNLVKRYVAAMIRDA 310
Cdd:TIGR00870 646 PPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTW-----ERKAETLIEDgLHYQRVMKRLIKRYVLAEQRPR 720

                         330       340
                  ....*....|....*....|....
gi 767978002  311 KtEEGLTEENFKELKQDISSFRFE 334
Cdd:TIGR00870 721 D-DEGTTEEETKELKQDISSLRFE 743
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-334 4.61e-165

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: 487.28  E-value: 4.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    1 MWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTA 78
Cdd:TIGR00870 410 IWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRG 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   79 NSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGI---RCEKQNNAFSTLFETLQSLFWS 154
Cdd:TIGR00870 490 NQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQGNAYSTLFETSQELFWA 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  155 IFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLP 234
Cdd:TIGR00870 570 IIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCP 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  235 TPFNVIPSPKSLWYLIKWIWTHLCKK---KMRRKPESFGTIGvrtqhRRAADNLRRH-HQYQEVMRNLVKRYVAAMIRDA 310
Cdd:TIGR00870 646 PPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTW-----ERKAETLIEDgLHYQRVMKRLIKRYVLAEQRPR 720

                         330       340
                  ....*....|....*....|....
gi 767978002  311 KtEEGLTEENFKELKQDISSFRFE 334
Cdd:TIGR00870 721 D-DEGTTEEETKELKQDISSLRFE 743
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 9-212 2.89e-23

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: 98.88  E-value: 2.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    9 YIHDWWNLMDFVMNSLYLATISLKIVAfvkysalnpreswdmwhptlvaeaLFAIANIFSSLRLISLFTANSHLGPLQI- 87
Cdd:pfam00520  63 YFRSPWNILDFVVVLPSLISLVLSSVG------------------------SLSGLRVLRLLRLLRLLRLIRRLEGLRTl 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   88 --SLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETkgltckGIRCEKQNNAFSTLFETLQSLFWSIF--GLINLYV 163
Cdd:pfam00520 119 vnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT------WENPDNGRTNFDNFPNAFLWLFQTMTteGWGDIMY 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767978002  164 TNVKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHAD 212
Cdd:pfam00520 193 DTIDGKGEF---WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 81-219 3.65e-10

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: 62.59  E-value: 3.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  81 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLyfyyeetkgltckgIRCEKQNNA--FSTLFETLQSLFWSIFG 157
Cdd:cd21882  431 MLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVIL--------------FQTEDPNKLgeFRDYPDALLELFKFTIG 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767978002 158 LINLyvtnvkaqhEFTE-----FVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 219
Cdd:cd21882  497 MGDL---------PFNEnvdfpFVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 4-204 1.11e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 54.95  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    4 GGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKY-SALNPRESWDMWHpTLVAEALF----------AIANIFSSLR- 71
Cdd:PLN03223 1205 GSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYaRAFEPDIHYDIYK-NLSASANFtalripnelpEMNDMFLEMKn 1283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   72 LISLFTANSHLGPLQISL--GRML--------------------LDILKFLFIYCLVLLAFANgLNQLYFYYeetkgltc 129
Cdd:PLN03223 1284 LVDYFQWYMTLSGINIILllGRILklmdfqprlgvitrtlwlagADLMHFFVIFGMVFVGYAF-IGHVIFGN-------- 1354

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767978002  130 kgircekQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSY 204
Cdd:PLN03223 1355 -------ASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAF 1422
 
Name Accession Description Interval E-value
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-334 4.61e-165

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: 487.28  E-value: 4.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    1 MWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYS--ALNPRESWDMWHPTLVAEALFAIANIFSSLRLISLFTA 78
Cdd:TIGR00870 410 IWLGGIFEYIHQLWNILDFGMNSFYLATFLDRPFAILFVTqaFLVLREHWLRFDPTLIEEALFAFALVLSWLNLLYIFRG 489

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   79 NSHLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGI---RCEKQNNAFSTLFETLQSLFWS 154
Cdd:TIGR00870 490 NQHLGPLQIMIGRMILgDILRFLFIYAVVLFGFACGLNQLYQYYDELKLNECSNPharSCEKQGNAYSTLFETSQELFWA 569

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  155 IFGLINLyvtnVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLP 234
Cdd:TIGR00870 570 IIGLGDL----LANEHKFTEFVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMSYEREGGTCP 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  235 TPFNVIPSPKSLWYLIKWIWTHLCKK---KMRRKPESFGTIGvrtqhRRAADNLRRH-HQYQEVMRNLVKRYVAAMIRDA 310
Cdd:TIGR00870 646 PPFNIIPGPKSFVGLFKRIEKHDGKKrqrWCRRVEEVNWTTW-----ERKAETLIEDgLHYQRVMKRLIKRYVLAEQRPR 720

                         330       340
                  ....*....|....*....|....
gi 767978002  311 KtEEGLTEENFKELKQDISSFRFE 334
Cdd:TIGR00870 721 D-DEGTTEEETKELKQDISSLRFE 743
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 9-212 2.89e-23

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: 98.88  E-value: 2.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    9 YIHDWWNLMDFVMNSLYLATISLKIVAfvkysalnpreswdmwhptlvaeaLFAIANIFSSLRLISLFTANSHLGPLQI- 87
Cdd:pfam00520  63 YFRSPWNILDFVVVLPSLISLVLSSVG------------------------SLSGLRVLRLLRLLRLLRLIRRLEGLRTl 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   88 --SLGRMLLDILKFLFIYCLVLLAFANGLNQLYFYYEETkgltckGIRCEKQNNAFSTLFETLQSLFWSIF--GLINLYV 163
Cdd:pfam00520 119 vnSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKT------WENPDNGRTNFDNFPNAFLWLFQTMTteGWGDIMY 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767978002  164 TNVKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHAD 212
Cdd:pfam00520 193 DTIDGKGEF---WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELTERTE 238
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 81-219 3.65e-10

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: 62.59  E-value: 3.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  81 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLyfyyeetkgltckgIRCEKQNNA--FSTLFETLQSLFWSIFG 157
Cdd:cd21882  431 MLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVIL--------------FQTEDPNKLgeFRDYPDALLELFKFTIG 496

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767978002 158 LINLyvtnvkaqhEFTE-----FVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 219
Cdd:cd21882  497 MGDL---------PFNEnvdfpFVYLILLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 81-219 4.01e-10

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: 62.52  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  81 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYfyyEETK-----GLTCKGIRCEKQNNAFSTLFETLQSLFWS 154
Cdd:cd22196  453 QMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI---EDGPpkgdvNTSQKECVCKSGYNSYNSLYSTCLELFKF 529

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767978002 155 IFGLINLYVT-NVKAQHEFTefvgaTMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 219
Cdd:cd22196  530 TIGMGDLEFTeNYKFKEVFI-----FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 82-216 3.18e-08

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: 56.56  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  82 LGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLnQLYFYYEEtkgltckgircEKQNNAFSTLFETLQSLFWSIFGLIN 160
Cdd:cd22192  447 LGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAF-YMIFQTED-----------PDSLGHFYDFPMTLFSTFELFLGLID 514

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767978002 161 LYV-TNVKaqhefTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWK 216
Cdd:cd22192  515 GPAnYTVD-----LPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWR 566
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 4-204 1.11e-07

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 54.95  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    4 GGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKY-SALNPRESWDMWHpTLVAEALF----------AIANIFSSLR- 71
Cdd:PLN03223 1205 GSYLAYFLSGWNYVDFASIGLHLATIMMWFVFSWSYaRAFEPDIHYDIYK-NLSASANFtalripnelpEMNDMFLEMKn 1283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   72 LISLFTANSHLGPLQISL--GRML--------------------LDILKFLFIYCLVLLAFANgLNQLYFYYeetkgltc 129
Cdd:PLN03223 1284 LVDYFQWYMTLSGINIILllGRILklmdfqprlgvitrtlwlagADLMHFFVIFGMVFVGYAF-IGHVIFGN-------- 1354

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767978002  130 kgircekQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSY 204
Cdd:PLN03223 1355 -------ASVHFSDMTDSINSLFENLLGDITYFNEDLKNLTGLQFVVGMIYFYSYNIFVFMILFNFLLAIICDAF 1422
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 81-247 6.48e-07

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: 52.10  E-value: 6.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  81 HLGPLQISLGRMLL-DILKFLFIYCLVLLAFANGLnqlyfyyeetKGLTCKGIRCEKQNNAFSTLFETLQSLFWSIFGLI 159
Cdd:cd22193  436 SMGIYSVMIQKVILrDLLRFLFVYLLFLFGFAVAL----------VSLIEKCSSDKKDCSSYGSFSDAVLELFKLTIGMG 505

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002 160 NLYVTNvkaQHEFtEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF--ARTKL--------WM-SYFE 228
Cdd:cd22193  506 DLEFQE---NSTY-PAVFLILLLTYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLqrAITILefeksfpeCMrKAFR 581

                        170
                 ....*....|....*....
gi 767978002 229 EGGTLPTPFNVIPSPKSLW 247
Cdd:cd22193  582 SGRLLKVGLCKDGTPDFRW 600
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 92-222 4.91e-06

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: 49.37  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  92 MLLDILKFLFIYCLVLLAFANGLNQLYfyyeetkgLTCK-GIRCEKQNNAFSTLFEtlqsLFWSIFGLINLYVTnvkaQH 170
Cdd:cd22194  509 ILNDVLKFLLVYILFLLGFGVALASLI--------EDCPdDSECSSYGSFSDAVLE----LFKLTIGLGDLEIQ----QN 572

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767978002 171 EFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF--ARTKL 222
Cdd:cd22194  573 SKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLqrARTIL 626
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 83-217 2.58e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 44.07  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  83 GPLQISLGRMLL-DILKFLFIYCLVLLAFANGLNQLYFYYEETKGLTCKGIRCE-------KQNNAFSTLfetLQSLFWS 154
Cdd:cd22195  499 GTYSIMIQKILFkDLFRFLLVYLLFMIGYASALVSLLNPCPTKETCKEDSTNCTvptypscRDSNTFSKF---LLDLFKL 575

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767978002 155 IFGLINLYVTNvKAQHEFtefVGATMFGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKF 217
Cdd:cd22195  576 TIGMGDLEMLN-SAKYPA---VFIILLVTYIILTFVLLLNMLIALMGETVGQVSKESKQIWKL 634
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 9-204 2.73e-04

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: 42.65  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002    9 YIHDWWNLMDFVMNSLYLATISLKIVAFVKYSAL------NPRESWDMWHPTLVAEALF---AIANIFSSLRLISLFTAN 79
Cdd:pfam08016  39 YLRSVWNLLDLAIVILSVVLIVLNIYRDFLADRLiksveaSPVTFIDFDRVAQLDNLYRiilAFLVFLTWLKLFKVLRFN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002   80 SHLGPLQISLGRMLLDILKFLFIYCLVLLAFAnglnQLyfyyeetkGLTCKGircekqNNA--FSTLFETLQSLFWSIFG 157
Cdd:pfam08016 119 KTMSLFTKTLSRAWKDLAGFALMFVIFFFAYA----QF--------GYLLFG------TQApnFSNFVKSILTLFRTILG 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 767978002  158 LINLYvtnvkAQHEFTEFVGATMFGTYNVISLVVLLNMLIAMMNNSY 204
Cdd:pfam08016 181 DFGYN-----EIFSGNRVLGPLLFLTFVFLVIFILLNLFLAIINDSY 222
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 92-219 7.55e-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: 42.53  E-value: 7.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767978002  92 MLLDILKFLFIYCLVLLAFANGLNQLY-----FYYEETKGLTCKGIRCEKQNNA---FSTLFETLQSLFWSIFGLINLyv 163
Cdd:cd22197  463 ILRDLLRFLLVYLVFLFGFAVALVSLSreapsPKAPEDNNSTVTEQPTVGQEEEpapYRSILDASLELFKFTIGMGEL-- 540

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767978002 164 tnvkAQHEFTEFVGATMFG--TYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFAR 219
Cdd:cd22197  541 ----AFQEQLRFRGVVLLLllAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQK 594
 
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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