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Conserved domains on  [gi|1581447832|pdb|6NR2|A]
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Chain A, Transient receptor potential cation channel subfamily M member 8

Protein Classification

transient-receptor-potential channel family protein; transient-receptor-potential channel protein( domain architecture ID 1904656)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LSDAT_euk super family cl39032
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
 118-361 1.41e-69

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


The actual alignment was detected with superfamily member pfam18139:

Pssm-ID: 476852  Cd Length: 266  Bit Score: 233.62  E-value: 1.41e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         118 KYIRLSCDTDSETLYDLMTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSR-LIYIAQSKGAWIFTGGTHYGLMKYIGE 196
Cdd:pfam18139    2 KYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKgLLKAAKTTGAWIITGGTNTGVMRHVGD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         197 VVRDNTISRSSeeNVVAIGIAAWGMISNRETLIrtadsdGS-YLAHYIMDDLKRDPLYCLDNNHTHLLLVDNGTHGHPTI 275
Cdd:pfam18139   82 ALKDLGSQSRR--KIVTIGIAPWGIIKNREDLI------GKdVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         276 EAKVRTQLEKYISE-RVIPESNYGgkIPIVCFAQGGGKETLKSINVAIKS--KIPCVVVEGSGRIADVIA---SLVEAEG 349
Cdd:pfam18139  154 EIILRRRLEKYISQqKIHPRGGQG--VPVVCVVVEGGPNTIKTVLEYVRDtpPVPVVVCDGSGRAADLLAfahKYTHEDG 231

                          250
                   ....*....|..
6NR2_A         350 TLASScVKESLL 361
Cdd:pfam18139  232 QLPSS-VKEQLL 242
TRPV super family cl40437
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 659-1027 2.35e-20

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: 97.07  E-value: 2.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         659 LELAVEARDQQFIAQPGVQNFLSKQWYGEIS---RDTKNWKIILCLfffpLIGCGFISFRKK-PVEKTKKLflyyVSFFT 734
Cdd:TIGR00870  275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELDgwrRKQSVLELIVVF----VIGLKFPELSDMyLIAPLSRL----GQFKW 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         735 SPFVVFswnvIFYIAFLLLFAYVLLM----------------DFQKEPTALEIILYVLVFILLcdEVRQWYMNG-SKYFS 797
Cdd:TIGR00870  347 KPFIKF----IFHSASYLYFLYLIIFtsvayyrptrtdlrvtGLQQTPLEMLIVTWVDGLRLG--EEKLIWLGGiFEYIH 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         798 DLWNVMDTLAIFYFIAGIVFR------------------LHSDESSWYSGRVIFCLdyiVFT-LRLIHIFTVSRNLGPKI 858
Cdd:TIGR00870  421 QLWNILDFGMNSFYLATFLDRpfailfvtqaflvlrehwLRFDPTLIEEALFAFAL---VLSwLNLLYIFRGNQHLGPLQ 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         859 IMLQRMMI-DVFFFLFLFAVWMVAFGVARQGI------LRKNE------HRWEWIFR--SVIYEPYLAMFgqypddidgt 923
Cdd:TIGR00870  498 IMIGRMILgDILRFLFIYAVVLFGFACGLNQLyqyydeLKLNEcsnphaRSCEKQGNaySTLFETSQELF---------- 567

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         924 tynfdHCTFSGneskplcVELDANNQPRFPEWITIPLVcIYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQRFFLV 1003
Cdd:TIGR00870  568 -----WAIIGL-------GDLLANEHKFTEFVGLLLFG-AYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLW 634

                          410       420       430
                   ....*....|....*....|....*....|.
6NR2_A        1004 QEY-CSRLTIPFPFVI------FAYIFMVMR 1027
Cdd:TIGR00870  635 MSYeREGGTCPPPFNIipgpksFVGLFKRIE 665
 
Name Accession Description Interval E-value
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
 118-361 1.41e-69

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


Pssm-ID: 465665  Cd Length: 266  Bit Score: 233.62  E-value: 1.41e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         118 KYIRLSCDTDSETLYDLMTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSR-LIYIAQSKGAWIFTGGTHYGLMKYIGE 196
Cdd:pfam18139    2 KYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKgLLKAAKTTGAWIITGGTNTGVMRHVGD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         197 VVRDNTISRSSeeNVVAIGIAAWGMISNRETLIrtadsdGS-YLAHYIMDDLKRDPLYCLDNNHTHLLLVDNGTHGHPTI 275
Cdd:pfam18139   82 ALKDLGSQSRR--KIVTIGIAPWGIIKNREDLI------GKdVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         276 EAKVRTQLEKYISE-RVIPESNYGgkIPIVCFAQGGGKETLKSINVAIKS--KIPCVVVEGSGRIADVIA---SLVEAEG 349
Cdd:pfam18139  154 EIILRRRLEKYISQqKIHPRGGQG--VPVVCVVVEGGPNTIKTVLEYVRDtpPVPVVVCDGSGRAADLLAfahKYTHEDG 231

                          250
                   ....*....|..
6NR2_A         350 TLASScVKESLL 361
Cdd:pfam18139  232 QLPSS-VKEQLL 242
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 659-1027 2.35e-20

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: 97.07  E-value: 2.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         659 LELAVEARDQQFIAQPGVQNFLSKQWYGEIS---RDTKNWKIILCLfffpLIGCGFISFRKK-PVEKTKKLflyyVSFFT 734
Cdd:TIGR00870  275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELDgwrRKQSVLELIVVF----VIGLKFPELSDMyLIAPLSRL----GQFKW 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         735 SPFVVFswnvIFYIAFLLLFAYVLLM----------------DFQKEPTALEIILYVLVFILLcdEVRQWYMNG-SKYFS 797
Cdd:TIGR00870  347 KPFIKF----IFHSASYLYFLYLIIFtsvayyrptrtdlrvtGLQQTPLEMLIVTWVDGLRLG--EEKLIWLGGiFEYIH 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         798 DLWNVMDTLAIFYFIAGIVFR------------------LHSDESSWYSGRVIFCLdyiVFT-LRLIHIFTVSRNLGPKI 858
Cdd:TIGR00870  421 QLWNILDFGMNSFYLATFLDRpfailfvtqaflvlrehwLRFDPTLIEEALFAFAL---VLSwLNLLYIFRGNQHLGPLQ 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         859 IMLQRMMI-DVFFFLFLFAVWMVAFGVARQGI------LRKNE------HRWEWIFR--SVIYEPYLAMFgqypddidgt 923
Cdd:TIGR00870  498 IMIGRMILgDILRFLFIYAVVLFGFACGLNQLyqyydeLKLNEcsnphaRSCEKQGNaySTLFETSQELF---------- 567

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         924 tynfdHCTFSGneskplcVELDANNQPRFPEWITIPLVcIYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQRFFLV 1003
Cdd:TIGR00870  568 -----WAIIGL-------GDLLANEHKFTEFVGLLLFG-AYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLW 634

                          410       420       430
                   ....*....|....*....|....*....|.
6NR2_A        1004 QEY-CSRLTIPFPFVI------FAYIFMVMR 1027
Cdd:TIGR00870  635 MSYeREGGTCPPPFNIipgpksFVGLFKRIE 665
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 745-990 1.14e-11

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: 66.14  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         745 IFYIAFLLLFAYVLLMDFQKEP-----TALEIILYVLVFILLCDEVRQWYMNGSK--YFSDLWNVMDTLAIFYFIAGIVF 817
Cdd:pfam00520    6 LFILLLILLNTIFLALETYFQPeepltTVLEILDYVFTGIFTLEMLLKIIAAGFKkrYFRSPWNILDFVVVLPSLISLVL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         818 rlhSDESSWYSGRVIFCLdyivFTLRLIHIFTVSRNLGPKIIMLQRMMIDVFFFLFLFAVWMVAFGVARQGILRKNEHRW 897
Cdd:pfam00520   86 ---SSVGSLSGLRVLRLL----RLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         898 E------WIFRSVIYEPYLAmfgqypddidgttynFDHCTFSGneskplCVELDANNQPRFPEWITIPLVCIYMLSTNIL 971
Cdd:pfam00520  159 EnpdngrTNFDNFPNAFLWL---------------FQTMTTEG------WGDIMYDTIDGKGEFWAYIYFVSFIILGGFL 217

                          250
                   ....*....|....*....
6NR2_A         972 LVNLLVAMFGYTVGSVQEN 990
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTER 236
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 777-999 8.25e-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: 49.88  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       777 VFILLCDEVRQWYMNGSKYFSDLWNVMDTLAIFY---FIAGIVFRLhsDESSWYSGRVIFCLdyIVFTLRLIHIFTVSRN 853
Cdd:cd21882  356 VYILLGEIPYFFRRRLSRWFGFLDSYFEILFITQallVLLSMVLRF--METEGYVVPLVFSL--VLGWCNVLYYTRGFQM 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       854 LGPKIIMLQRMMI-DVFFFLFLFAVWMVAFGVARQGILRKNEHrwewifrsviyePYLAMFGQYPDdidgttynfdhCTF 932
Cdd:cd21882  432 LGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVILFQTEDP------------NKLGEFRDYPD-----------ALL 488

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
6NR2_A       933 SGNESKPLCVELDANNQPRFPEWITIPLVCiYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQR 999
Cdd:cd21882  489 ELFKFTIGMGDLPFNENVDFPFVYLILLLA-YVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
 
Name Accession Description Interval E-value
LSDAT_euk pfam18139
SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including ...
 118-361 1.41e-69

SLOG in TRPM; Family in the SLOG superfamily, found in several eukaryotic channels including diverse ciliate channels and the TRPM class of animal ion channels. Positioned near the N-terminus of all TRPM channels, it is predicted to play a regulatory role for the channel in potentially recognizing a universal nucleotide or nucleotide-derived ligand.


Pssm-ID: 465665  Cd Length: 266  Bit Score: 233.62  E-value: 1.41e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         118 KYIRLSCDTDSETLYDLMTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSR-LIYIAQSKGAWIFTGGTHYGLMKYIGE 196
Cdd:pfam18139    2 KYIRLSFDTDPEDLLHLMEKEWQLELPKLVISVHGGATNFELQPKLKRVFRKgLLKAAKTTGAWIITGGTNTGVMRHVGD 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         197 VVRDNTISRSSeeNVVAIGIAAWGMISNRETLIrtadsdGS-YLAHYIMDDLKRDPLYCLDNNHTHLLLVDNGTHGHPTI 275
Cdd:pfam18139   82 ALKDLGSQSRR--KIVTIGIAPWGIIKNREDLI------GKdVVVPYQTLGNPKSKLAVLNNNHSHFLLVDDGTVGKYGA 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         276 EAKVRTQLEKYISE-RVIPESNYGgkIPIVCFAQGGGKETLKSINVAIKS--KIPCVVVEGSGRIADVIA---SLVEAEG 349
Cdd:pfam18139  154 EIILRRRLEKYISQqKIHPRGGQG--VPVVCVVVEGGPNTIKTVLEYVRDtpPVPVVVCDGSGRAADLLAfahKYTHEDG 231

                          250
                   ....*....|..
6NR2_A         350 TLASScVKESLL 361
Cdd:pfam18139  232 QLPSS-VKEQLL 242
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 659-1027 2.35e-20

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: 97.07  E-value: 2.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         659 LELAVEARDQQFIAQPGVQNFLSKQWYGEIS---RDTKNWKIILCLfffpLIGCGFISFRKK-PVEKTKKLflyyVSFFT 734
Cdd:TIGR00870  275 LKLAIKYKQKKFVAWPNGQQLLSLYWLEELDgwrRKQSVLELIVVF----VIGLKFPELSDMyLIAPLSRL----GQFKW 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         735 SPFVVFswnvIFYIAFLLLFAYVLLM----------------DFQKEPTALEIILYVLVFILLcdEVRQWYMNG-SKYFS 797
Cdd:TIGR00870  347 KPFIKF----IFHSASYLYFLYLIIFtsvayyrptrtdlrvtGLQQTPLEMLIVTWVDGLRLG--EEKLIWLGGiFEYIH 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         798 DLWNVMDTLAIFYFIAGIVFR------------------LHSDESSWYSGRVIFCLdyiVFT-LRLIHIFTVSRNLGPKI 858
Cdd:TIGR00870  421 QLWNILDFGMNSFYLATFLDRpfailfvtqaflvlrehwLRFDPTLIEEALFAFAL---VLSwLNLLYIFRGNQHLGPLQ 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         859 IMLQRMMI-DVFFFLFLFAVWMVAFGVARQGI------LRKNE------HRWEWIFR--SVIYEPYLAMFgqypddidgt 923
Cdd:TIGR00870  498 IMIGRMILgDILRFLFIYAVVLFGFACGLNQLyqyydeLKLNEcsnphaRSCEKQGNaySTLFETSQELF---------- 567

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         924 tynfdHCTFSGneskplcVELDANNQPRFPEWITIPLVcIYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQRFFLV 1003
Cdd:TIGR00870  568 -----WAIIGL-------GDLLANEHKFTEFVGLLLFG-AYNVIMYILLLNMLIAMMGNTYQLIADDADEEWKFQRAKLW 634

                          410       420       430
                   ....*....|....*....|....*....|.
6NR2_A        1004 QEY-CSRLTIPFPFVI------FAYIFMVMR 1027
Cdd:TIGR00870  635 MSYeREGGTCPPPFNIipgpksFVGLFKRIE 665
LSDAT_prok pfam18171
SLOG in TRPM, prokaryote; Family in the SLOG superfamily, fused to or operonically associating ...
 147-365 2.77e-14

SLOG in TRPM, prokaryote; Family in the SLOG superfamily, fused to or operonically associating with SLATT domain in diverse prokaryotes. Predicted to function as ligand sensor in conjunction with the SLATT transmembrane domain.


Pssm-ID: 408001  Cd Length: 194  Bit Score: 72.71  E-value: 2.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         147 VISVTGGAKNF--ALKPRMRKIFSRLIY-IAQSKGAWIFTGGTHYGLMKYIGEVVRdntiSRSSEENVvaIGIAAWGMIs 223
Cdd:pfam18171    3 VLVLVGGASGLdpELAARLLPLFRAVLApAAEALGAVVIDGGTDTGVMRLMGRARA----ATDGRFPL--VGVAPSGTV- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         224 nretlirtadsdgsylaHYIMDDLKRDPLYCLDNNHTHLLLVDNGTHGH--PTIEAkvrtqlekyISERVipesnyGGKI 301
Cdd:pfam18171   76 -----------------AYPDEPTPTDDAARLEPHHTHFVLVPGSRWGDesPWLAR---------LATAI------AGGR 123

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
6NR2_A         302 PIVCFAQGGGKETLKSINVAIKSKIPCVVVEGSGRIADVIASlveAEGTLASSCVKESLLRFLP 365
Cdd:pfam18171  124 PSVTLLVNGGAITRLDIRASLAAGRPLLVLAGSGRLADEIAA---ALRGDSLDLARSGLLFVVD 184
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 745-990 1.14e-11

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: 66.14  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         745 IFYIAFLLLFAYVLLMDFQKEP-----TALEIILYVLVFILLCDEVRQWYMNGSK--YFSDLWNVMDTLAIFYFIAGIVF 817
Cdd:pfam00520    6 LFILLLILLNTIFLALETYFQPeepltTVLEILDYVFTGIFTLEMLLKIIAAGFKkrYFRSPWNILDFVVVLPSLISLVL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         818 rlhSDESSWYSGRVIFCLdyivFTLRLIHIFTVSRNLGPKIIMLQRMMIDVFFFLFLFAVWMVAFGVARQGILRKNEHRW 897
Cdd:pfam00520   86 ---SSVGSLSGLRVLRLL----RLLRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTW 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A         898 E------WIFRSVIYEPYLAmfgqypddidgttynFDHCTFSGneskplCVELDANNQPRFPEWITIPLVCIYMLSTNIL 971
Cdd:pfam00520  159 EnpdngrTNFDNFPNAFLWL---------------FQTMTTEG------WGDIMYDTIDGKGEFWAYIYFVSFIILGGFL 217

                          250
                   ....*....|....*....
6NR2_A         972 LVNLLVAMFGYTVGSVQEN 990
Cdd:pfam00520  218 LLNLFIAVIIDNFQELTER 236
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 777-999 8.25e-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: 49.88  E-value: 8.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       777 VFILLCDEVRQWYMNGSKYFSDLWNVMDTLAIFY---FIAGIVFRLhsDESSWYSGRVIFCLdyIVFTLRLIHIFTVSRN 853
Cdd:cd21882  356 VYILLGEIPYFFRRRLSRWFGFLDSYFEILFITQallVLLSMVLRF--METEGYVVPLVFSL--VLGWCNVLYYTRGFQM 431

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       854 LGPKIIMLQRMMI-DVFFFLFLFAVWMVAFGVARQGILRKNEHrwewifrsviyePYLAMFGQYPDdidgttynfdhCTF 932
Cdd:cd21882  432 LGIYTVMIQKMILrDLMRFCWVYLVFLFGFASAFVILFQTEDP------------NKLGEFRDYPD-----------ALL 488

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
6NR2_A       933 SGNESKPLCVELDANNQPRFPEWITIPLVCiYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQR 999
Cdd:cd21882  489 ELFKFTIGMGDLPFNENVDFPFVYLILLLA-YVILTYLLLLNMLIALMGETVNRVAQESDEIWKLQK 554
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 943-999 5.91e-05

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: 47.10  E-value: 5.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
6NR2_A       943 ELDANNQPRFPEWITIPLVCiYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQR 999
Cdd:cd22193  506 DLEFQENSTYPAVFLILLLT-YVILTFVLLLNMLIALMGETVNNVSKESKRIWKLQR 561
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 943-998 1.19e-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: 46.38  E-value: 1.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
6NR2_A       943 ELDANNQPRFPEWITIPLVCiYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQ 998
Cdd:cd22195  581 DLEMLNSAKYPAVFIILLVT-YIILTFVLLLNMLIALMGETVGQVSKESKQIWKLQ 635
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 852-1010 4.43e-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: 44.36  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       852 RNLGPKIIMLQRMMI-DVFFFLFLFAVWMVAFGVARQGILRKnehrwewifrsviyepylamfgqYPDDIDGTTYNFDHC 930
Cdd:cd22194  496 QSLGIYSVMIQKVILnDVLKFLLVYILFLLGFGVALASLIED-----------------------CPDDSECSSYGSFSD 552

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       931 TFSgnESKPLCV---ELDANNQPRFPEWITIPLVCiYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQRFFLVQEYC 1007
Cdd:cd22194  553 AVL--ELFKLTIglgDLEIQQNSKYPILFLLLLIT-YVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFE 629


                 ...
6NR2_A      1008 SRL 1010
Cdd:cd22194  630 KSL 632
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 943-999 1.35e-03

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: 42.87  E-value: 1.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
6NR2_A       943 ELDANNQPRFPEWITIPLVCiYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQR 999
Cdd:cd22196  535 DLEFTENYKFKEVFIFLLIS-YVILTYILLLNMLIALMGETVSKIAQESKNIWKLQR 590
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 943-1005 2.74e-03

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: 41.76  E-value: 2.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
6NR2_A       943 ELDANNQPRFPEWITIpLVCIYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQRFFLVQE 1005
Cdd:cd22197  539 ELAFQEQLRFRGVVLL-LLLAYVLLTYVLLLNMLIALMSETVNHVADNSWSIWKLQKAISVLE 600
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 854-998 4.43e-03

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: 41.15  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6NR2_A       854 LGPKIIMLQRMMI-DVFFFLFLFAVWMVAFGVArqgilrknehrwewifrsvIYepylAMFGQYPDDIDGTTYNFDHCTF 932
Cdd:cd22192  447 LGPFTIMIQKIIFgDLMKFCWLMFVVILGFSSA-------------------FY----MIFQTEDPDSLGHFYDFPMTLF 503

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
6NR2_A       933 SGNESKPLCVELDANNQPRFPeWITIPLVCIYMLSTNILLVNLLVAMFGYTVGSVQENNDQVWKFQ 998
Cdd:cd22192  504 STFELFLGLIDGPANYTVDLP-FMYKVLYTAFAVIAYLLMLNLLIAMMGDTHWRVAHERDELWRAQ 568
 
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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