NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039777461|ref|XP_017177501|]
View 

transient receptor potential cation channel subfamily M member 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
 520-575 5.57e-25

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


:

Pssm-ID: 465156  Cd Length: 56  Bit Score: 98.17  E-value: 5.57e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777461 520 DERIRVTSERVENMSMRLEEINERENFMKTSLQTVDLRLSQLEELSGRMVSALENL 575
Cdd:pfam16519   1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 97-451 5.26e-24

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: 108.24  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461  97 LKLAVAAKHRDFIAHTCSQMLLTDMWMGRL-RMRKNPGLKVIMGIlippTILFLEFRTYDDFsYQTSKENEDGKEKEE-- 173
Cdd:TIGR00870 275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELdGWRRKQSVLELIVV----FVIGLKFPELSDM-YLIAPLSRLGQFKWKpf 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 174 ------ENVISYLGYLLLFN---YVILVRMDGW-----PSPQEWIVISYIVSLALEKIREILMsepgklsQKIKVWLQEY 239
Cdd:TIGR00870 350 ikfifhSASYLYFLYLIIFTsvaYYRPTRTDLRvtglqQTPLEMLIVTWVDGLRLGEEKLIWL-------GGIFEYIHQL 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 240 WNITDLVAISMFM-------------VGAILRLQSQ-----PYMGYgRVIYCVDIILWYIRVLDIFGVNKYLGPYVMMIG 301
Cdd:TIGR00870 423 WNILDFGMNSFYLatfldrpfailfvTQAFLVLREHwlrfdPTLIE-EALFAFALVLSWLNLLYIFRGNQHLGPLQIMIG 501

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 302 KMMI-DMLYFVVIMLVVLMSFGVARQAILH---PEEKPSWKLARNIFYMPYWMIYGEVFADQIDLYAMEINppcGENLYD 377
Cdd:TIGR00870 502 RMILgDILRFLFIYAVVLFGFACGLNQLYQyydELKLNECSNPHARSCEKQGNAYSTLFETSQELFWAIIG---LGDLLA 578

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777461 378 EEGKRLPpcipgaWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIM-TFHDRPVLPPP 451
Cdd:TIGR00870 579 NEHKFTE------FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMsYEREGGTCPPP 647
 
Name Accession Description Interval E-value
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
 520-575 5.57e-25

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


Pssm-ID: 465156  Cd Length: 56  Bit Score: 98.17  E-value: 5.57e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777461 520 DERIRVTSERVENMSMRLEEINERENFMKTSLQTVDLRLSQLEELSGRMVSALENL 575
Cdd:pfam16519   1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 97-451 5.26e-24

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: 108.24  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461  97 LKLAVAAKHRDFIAHTCSQMLLTDMWMGRL-RMRKNPGLKVIMGIlippTILFLEFRTYDDFsYQTSKENEDGKEKEE-- 173
Cdd:TIGR00870 275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELdGWRRKQSVLELIVV----FVIGLKFPELSDM-YLIAPLSRLGQFKWKpf 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 174 ------ENVISYLGYLLLFN---YVILVRMDGW-----PSPQEWIVISYIVSLALEKIREILMsepgklsQKIKVWLQEY 239
Cdd:TIGR00870 350 ikfifhSASYLYFLYLIIFTsvaYYRPTRTDLRvtglqQTPLEMLIVTWVDGLRLGEEKLIWL-------GGIFEYIHQL 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 240 WNITDLVAISMFM-------------VGAILRLQSQ-----PYMGYgRVIYCVDIILWYIRVLDIFGVNKYLGPYVMMIG 301
Cdd:TIGR00870 423 WNILDFGMNSFYLatfldrpfailfvTQAFLVLREHwlrfdPTLIE-EALFAFALVLSWLNLLYIFRGNQHLGPLQIMIG 501

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 302 KMMI-DMLYFVVIMLVVLMSFGVARQAILH---PEEKPSWKLARNIFYMPYWMIYGEVFADQIDLYAMEINppcGENLYD 377
Cdd:TIGR00870 502 RMILgDILRFLFIYAVVLFGFACGLNQLYQyydELKLNECSNPHARSCEKQGNAYSTLFETSQELFWAIIG---LGDLLA 578

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777461 378 EEGKRLPpcipgaWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIM-TFHDRPVLPPP 451
Cdd:TIGR00870 579 NEHKFTE------FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMsYEREGGTCPPP 647
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 176-425 5.80e-19

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: 86.94  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 176 VISYLGYLLLFNYVILVRMDGWPSPQ-------EWIVISYIVSLALEKIREILMSEPgklsqkIKVWLQEYWNITDLVAI 248
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEeplttvlEILDYVFTGIFTLEMLLKIIAAGF------KKRYFRSPWNILDFVVV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 249 SMFMVGAILRLQSQPYMGygRVIycvdIILWYIRVLDIFGVNKYLGPYVMMIGKMMIDMLYFVVIMLVVLMSFGVARQAI 328
Cdd:pfam00520  77 LPSLISLVLSSVGSLSGL--RVL----RLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 329 LHPEEKpSWKLARNIFYMpyWMIYGEVFadqidLYAMEINppCGENLYDEegkrLPPCIP--GAWLTPALMACYLLVANI 406
Cdd:pfam00520 151 FGGKLK-TWENPDNGRTN--FDNFPNAF-----LWLFQTM--TTEGWGDI----MYDTIDgkGEFWAYIYFVSFIILGGF 216

                         250
                  ....*....|....*....
gi 1039777461 407 LLVNLLIAVFNNTFFEVKS 425
Cdd:pfam00520 217 LLLNLFIAVIIDNFQELTE 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 291-434 2.90e-09

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: 60.80  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 291 KYLGPYVMMIGKMMI-DMLYFVVIMLVVLMSFGVARQAILHPEEkPSWklarnifyMPYWMIYGEVFADQIDLYAMEINP 369
Cdd:cd22192   445 QMLGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAFYMIFQTED-PDS--------LGHFYDFPMTLFSTFELFLGLIDG 515

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777461 370 PcgenlydeegkrLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQ 434
Cdd:cd22192   516 P------------ANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQ 568
 
Name Accession Description Interval E-value
TRPM_tetra pfam16519
tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil ...
 520-575 5.57e-25

tetramerization domain of TRPM; TRPM7_tetra is a short anti-parallel coiled-coil tetramerization domain of the transient receptor potential cation channel subfamily M member proteins 1-8. It is held together by extensive core packing and interstrand polar interactions. Transient receptor potential (TRP) channels comprise a large family of tetrameric cation-selective ion channels that respond to diverse forms of sensory input. The presence of cytoplasmic domains that direct channel assembly appears to be a feature of many voltage-gated ion channel superfamily members.


Pssm-ID: 465156  Cd Length: 56  Bit Score: 98.17  E-value: 5.57e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777461 520 DERIRVTSERVENMSMRLEEINERENFMKTSLQTVDLRLSQLEELSGRMVSALENL 575
Cdd:pfam16519   1 DERIRVTTERVENMSMKVEEVNEKENFQKASLQSLDFRLGKLEDLSAQTVDTLSVL 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 97-451 5.26e-24

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: 108.24  E-value: 5.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461  97 LKLAVAAKHRDFIAHTCSQMLLTDMWMGRL-RMRKNPGLKVIMGIlippTILFLEFRTYDDFsYQTSKENEDGKEKEE-- 173
Cdd:TIGR00870 275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELdGWRRKQSVLELIVV----FVIGLKFPELSDM-YLIAPLSRLGQFKWKpf 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 174 ------ENVISYLGYLLLFN---YVILVRMDGW-----PSPQEWIVISYIVSLALEKIREILMsepgklsQKIKVWLQEY 239
Cdd:TIGR00870 350 ikfifhSASYLYFLYLIIFTsvaYYRPTRTDLRvtglqQTPLEMLIVTWVDGLRLGEEKLIWL-------GGIFEYIHQL 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 240 WNITDLVAISMFM-------------VGAILRLQSQ-----PYMGYgRVIYCVDIILWYIRVLDIFGVNKYLGPYVMMIG 301
Cdd:TIGR00870 423 WNILDFGMNSFYLatfldrpfailfvTQAFLVLREHwlrfdPTLIE-EALFAFALVLSWLNLLYIFRGNQHLGPLQIMIG 501

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 302 KMMI-DMLYFVVIMLVVLMSFGVARQAILH---PEEKPSWKLARNIFYMPYWMIYGEVFADQIDLYAMEINppcGENLYD 377
Cdd:TIGR00870 502 RMILgDILRFLFIYAVVLFGFACGLNQLYQyydELKLNECSNPHARSCEKQGNAYSTLFETSQELFWAIIG---LGDLLA 578

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777461 378 EEGKRLPpcipgaWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIM-TFHDRPVLPPP 451
Cdd:TIGR00870 579 NEHKFTE------FVGLLLFGAYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLWMsYEREGGTCPPP 647
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 176-425 5.80e-19

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: 86.94  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 176 VISYLGYLLLFNYVILVRMDGWPSPQ-------EWIVISYIVSLALEKIREILMSEPgklsqkIKVWLQEYWNITDLVAI 248
Cdd:pfam00520   3 YFELFILLLILLNTIFLALETYFQPEeplttvlEILDYVFTGIFTLEMLLKIIAAGF------KKRYFRSPWNILDFVVV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 249 SMFMVGAILRLQSQPYMGygRVIycvdIILWYIRVLDIFGVNKYLGPYVMMIGKMMIDMLYFVVIMLVVLMSFGVARQAI 328
Cdd:pfam00520  77 LPSLISLVLSSVGSLSGL--RVL----RLLRLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 329 LHPEEKpSWKLARNIFYMpyWMIYGEVFadqidLYAMEINppCGENLYDEegkrLPPCIP--GAWLTPALMACYLLVANI 406
Cdd:pfam00520 151 FGGKLK-TWENPDNGRTN--FDNFPNAF-----LWLFQTM--TTEGWGDI----MYDTIDgkGEFWAYIYFVSFIILGGF 216

                         250
                  ....*....|....*....
gi 1039777461 407 LLVNLLIAVFNNTFFEVKS 425
Cdd:pfam00520 217 LLLNLFIAVIIDNFQELTE 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 291-434 2.90e-09

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: 60.80  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 291 KYLGPYVMMIGKMMI-DMLYFVVIMLVVLMSFGVARQAILHPEEkPSWklarnifyMPYWMIYGEVFADQIDLYAMEINP 369
Cdd:cd22192   445 QMLGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSAFYMIFQTED-PDS--------LGHFYDFPMTLFSTFELFLGLIDG 515

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039777461 370 PcgenlydeegkrLPPCIPGAWLTPALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQ 434
Cdd:cd22192   516 P------------ANYTVDLPFMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQ 568
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 291-435 2.99e-08

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: 57.58  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 291 KYLGPYVMMIGKMMI-DMLYFVVIMLVVLMSFGVARQAILHPEEKPSWKLARNIfYMPYWMIYgEVFADQIDLyameinp 369
Cdd:cd21882   430 QMLGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVILFQTEDPNKLGEFRDY-PDALLELF-KFTIGMGDL------- 500

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039777461 370 PCGENlYDeegkrlppcIPGAWLTpaLMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQR 435
Cdd:cd21882   501 PFNEN-VD---------FPFVYLI--LLLAYVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 175-442 1.53e-06

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: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 175 NVISYLGYLLLFNYVILVR-MDGWPSPQ--------------EWIVISYIVSLALEKIREILMSEPGKLSQKIKVWLQEY 239
Cdd:cd22193   311 SFCFYLFYMIIFTLVAYYRpREDEPPPPlakttkmdymrllgEILVLLGGVYFFVKEIAYFLLRRSDLQSSFSDSYFEIL 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 240 WNITDLVAIsmfmVGAILRLqsqpyMGYGRVIYCVDI--------ILWYIRVLdifgvnKYLGPYVMMIGKMMI-DMLYF 310
Cdd:cd22193   391 FFVQAVLVI----LSVVLYL-----FAYKEYLACLVLalalgwanMLYYTRGF------QSMGIYSVMIQKVILrDLLRF 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 311 VVIMLVVLMSFGVARQAILHPEEKPSWKLArnifymPYWMIYGEVfadqIDLYAMEINppCGENLYDEEGKrlppcIPGA 390
Cdd:cd22193   456 LFVYLLFLFGFAVALVSLIEKCSSDKKDCS------SYGSFSDAV----LELFKLTIG--MGDLEFQENST-----YPAV 518

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039777461 391 WLTpaLMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVWKFQRYQLIMTF 442
Cdd:cd22193   519 FLI--LLLTYVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQRAITILEF 568
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 277-450 2.55e-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: 51.30  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 277 ILWYIRVLDIFGVnkylgpYVMMIGKMMI-DMLYFVVIMLVVLMSFGVARQAILH-----PEEKPSWKLARNIFympywm 350
Cdd:cd22194   488 MLYYTRGFQSLGI------YSVMIQKVILnDVLKFLLVYILFLLGFGVALASLIEdcpddSECSSYGSFSDAVL------ 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 351 iygEVFADQIDLYAMEInppcgenlyDEEGKrlppcIPGAWLtpALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQV 430
Cdd:cd22194   556 ---ELFKLTIGLGDLEI---------QQNSK-----YPILFL--LLLITYVILTFVLLLNMLIALMGETVENVSKESERI 616

                         170       180
                  ....*....|....*....|
gi 1039777461 431 WKFQRYQLIMTFHDRpvLPP 450
Cdd:cd22194   617 WRLQRARTILEFEKS--LPE 634
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 277-435 4.01e-06

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: 50.57  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 277 ILWYIRVLdifgvnKYLGPYVMMIGKMMI-DMLYFVVIMLVVLMSFGVARQAILhpEEKPSWKLARNIFYM----PYWMI 351
Cdd:cd22196   444 VLYYTRGF------QQMGIYSVMIQKMILrDICRFLFVYLVFLFGFSAALVTLI--EDGPPKGDVNTSQKEcvckSGYNS 515

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039777461 352 YGEVFADQIDLYAMEINppCGENLYDEEGKRLPPCIpgawltpALMACYLLVANILLVNLLIAVFNNTFFEVKSISNQVW 431
Cdd:cd22196   516 YNSLYSTCLELFKFTIG--MGDLEFTENYKFKEVFI-------FLLISYVILTYILLLNMLIALMGETVSKIAQESKNIW 586


                  ....
gi 1039777461 432 KFQR 435
Cdd:cd22196   587 KLQR 590
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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