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Conserved domains on  [gi|357394757|ref|NP_001239417|]
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cation channel sperm-associated protein 3 isoform 3 [Mus musculus]

Protein Classification

ion transporter( domain architecture ID 11997982)

ion transporter such as a voltage-gated cation channel, which enables the selective translocation of cations such as sodium, calcium, or potassium across cell membranes

CATH:  1.10.287.70
Gene Ontology:  GO:0034220|GO:0005216|GO:0005886|GO:0034702
PubMed:  15816170
TCDB:  1.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 100-218 7.87e-17

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: 78.46  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357394757  100 LRILKLISYSRGIRTLIIAVGETVYTVASVLTLLFLLMFVFAILGFCLFGVTDRGDLE------NWGNLASAFFTLFSLA 173
Cdd:pfam00520 103 LRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENpdngrtNFDNFPNAFLWLFQTM 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 357394757  174 TVDGWTD-LQEELDKRKFTVSRAFTILFILLASFIFLNMFVGVMIM 218
Cdd:pfam00520 183 TTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIID 228
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 100-218 7.87e-17

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: 78.46  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357394757  100 LRILKLISYSRGIRTLIIAVGETVYTVASVLTLLFLLMFVFAILGFCLFGVTDRGDLE------NWGNLASAFFTLFSLA 173
Cdd:pfam00520 103 LRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENpdngrtNFDNFPNAFLWLFQTM 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 357394757  174 TVDGWTD-LQEELDKRKFTVSRAFTILFILLASFIFLNMFVGVMIM 218
Cdd:pfam00520 183 TTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIID 228
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 99-241 3.45e-03

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: 39.36  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357394757  99 SLRILKLISYSRGIRTL-IIAVgeTVYTVASVLTLLFLLMFVFAILGFclfGVT---------DRGDLENWGNLASAFFT 168
Cdd:cd22194  482 ALGWANMLYYTRGFQSLgIYSV--MIQKVILNDVLKFLLVYILFLLGF---GVAlasliedcpDDSECSSYGSFSDAVLE 556

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357394757 169 LFSLATvdGWTDLQEELDKRKFTVSRAFTILFILLASFIFLNMFVGVMIMHTEDSMKKFERDLTLERNLAIME 241
Cdd:cd22194  557 LFKLTI--GLGDLEIQQNSKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILE 627
 
Name Accession Description Interval E-value
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 100-218 7.87e-17

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: 78.46  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357394757  100 LRILKLISYSRGIRTLIIAVGETVYTVASVLTLLFLLMFVFAILGFCLFGVTDRGDLE------NWGNLASAFFTLFSLA 173
Cdd:pfam00520 103 LRLLRLIRRLEGLRTLVNSLIRSLKSLGNLLLLLLLFLFIFAIIGYQLFGGKLKTWENpdngrtNFDNFPNAFLWLFQTM 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 357394757  174 TVDGWTD-LQEELDKRKFTVSRAFTILFILLASFIFLNMFVGVMIM 218
Cdd:pfam00520 183 TTEGWGDiMYDTIDGKGEFWAYIYFVSFIILGGFLLLNLFIAVIID 228
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 99-241 3.45e-03

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: 39.36  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357394757  99 SLRILKLISYSRGIRTL-IIAVgeTVYTVASVLTLLFLLMFVFAILGFclfGVT---------DRGDLENWGNLASAFFT 168
Cdd:cd22194  482 ALGWANMLYYTRGFQSLgIYSV--MIQKVILNDVLKFLLVYILFLLGF---GVAlasliedcpDDSECSSYGSFSDAVLE 556

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357394757 169 LFSLATvdGWTDLQEELDKRKFTVSRAFTILFILLASFIFLNMFVGVMIMHTEDSMKKFERDLTLERNLAIME 241
Cdd:cd22194  557 LFKLTI--GLGDLEIQQNSKYPILFLLLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILE 627
 
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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