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UniProtKB/Swiss-Prot entry Q9EPK8


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRPV4_MOUSE
Primary accession number Q9EPK8
Secondary accession numbers Q91XR5 Q9EQZ4 Q9ERZ7 Q9ES76
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 61)
Name and origin of the protein
Protein name Transient receptor potential cation channel subfamily V member 4
Synonyms TrpV4
Osm-9-like TRP channel 4
OTRPC4
Vanilloid receptor-like channel 2
Vanilloid receptor-like protein 2
Vanilloid receptor-related osmotically-activated channel
VR-OAC
Transient receptor potential protein 12
TRP12
Gene name
Name: Trpv4
Synonyms: Trp12, Vrl2, Vroac
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Hypothalamus;
DOI=10.1016/S0092-8674(00)00143-4; PubMed=11081638 [NCBI, ExPASy, EBI, Israel, Japan]
Liedtke W.B., Choe Y., Marti-Renom M.A., Bell A.M., Denis C.S., Sali A., Hudspeth A.J., Friedman J.M., Heller S.;
"Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor.";
Cell 103:525-535(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
DOI=10.1016/S0014-5793(00)02212-2; PubMed=11094154 [NCBI, ExPASy, EBI, Israel, Japan]
Wissenbach U., Boedding M., Freichel M., Flockerzi V.;
"Trp12, a novel Trp related protein from kidney.";
FEBS Lett. 485:127-134(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=129/SvEv;
DOI=10.1038/35036318; PubMed=11025659 [NCBI, ExPASy, EBI, Israel, Japan]
Strotmann R., Harteneck C., Nunnenmacher K., Schultz G., Plant T.D.;
"OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity.";
Nat. Cell Biol. 2:695-702(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Kidney;
DOI=10.1074/jbc.M302561200; PubMed=12692122 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki M., Mizuno A., Kodaira K., Imai M.;
"Impaired pressure sensation in mice lacking TRPV4.";
J. Biol. Chem. 278:22664-22668(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Derst C., Schafer M.K.;
"Cloning of mouse and human vanilloid receptor-like protein 2 (VRL-2).";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[6]
CHARACTERIZATION OF CHANNEL PORE, AND MUTAGENESIS OF ASP-672; LYS-675; MET-680 AND ASP-682.
DOI=10.1074/jbc.M204828200; PubMed=12093812 [NCBI, ExPASy, EBI, Israel, Japan]
Voets T., Prenen J., Vriens J., Watanabe H., Janssens A., Wissenbach U., Bodding M., Droogmans G., Nilius B.;
"Molecular determinants of permeation through the cation channel TRPV4.";
J. Biol. Chem. 277:33704-33710(2002).
[7]
INTERACTION WITH MAP7.
DOI=10.1074/jbc.M308212200; PubMed=14517216 [NCBI, ExPASy, EBI, Israel, Japan]
Suzuki M., Hirao A., Mizuno A.;
"Microtubule-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4).";
J. Biol. Chem. 278:51448-51453(2003).
[8]
INTERACTION WITH LYN; SRC; FYN; HCK; LCK AND YES, PHOSPHORYLATION AT TYR-253, AND MUTAGENESIS OF TYR-253.
DOI=10.1074/jbc.M211061200; PubMed=12538589 [NCBI, ExPASy, EBI, Israel, Japan]
Xu H., Zhao H., Tian W., Yoshida K., Roullet J.B., Cohen D.M.;
"Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress.";
J. Biol. Chem. 278:11520-11527(2003).
Comments
  • FUNCTION: Non-selective calcium permeant cation channel probably involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by low pH, citrate and phorbol esters. Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism.
  • SUBUNIT: Interacts with calmodulin (By similarity). Interacts with Map7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES.
  • SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (Probable).
  • TISSUE SPECIFICITY: Expressed heart, liver, kidney and testis. In the central nervous system, expressed in the lamina terminalis (arched vascular organ and neurons of the subfornical organ), median preoptic area, ventral hippocampal commissure, and ependymal cells of the choroid plexus. In the cochlea, expressed in both inner and outer hair cells, and in marginal cells of the cochlear stria vascularis. Expressed in large neurons of the trigeminal ganglion. In the kidney cortex, strongly expressed by epithelial cells of tubules and much weaker in glomeruli.
  • SIMILARITY: Belongs to the transient receptor family. TrpV subfamily.
  • SIMILARITY: Contains 3 ANK repeats.
  • SEQUENCE CAUTION:
    • Sequence=AAG28028.1; Type=Frameshift; Positions=47, 50, 53, 72, 73;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF263522; AAG28028.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ296078; CAC20703.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF208026; AAG17543.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB021875; BAA83731.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF279672; AAK69486.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00112949; -.
RefSeq NP_071300.1; -.
UniGene Mm.266450
3D structure databases
ModBase Q9EPK8.
PTM databases
PhosphoSite Q9EPK8; -.
Organism-specific databases
MGI MGI:1926945; Trpv4.
Gene expression databases
ArrayExpress Q9EPK8; -.
Bgee Q9EPK8; -.
GermOnline ENSMUSG00000014158; Mus musculus.
Ontologies
GO
GO:0005929; Cellular component: cilium (inferred from direct assay from MGI).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0005262; Molecular function: calcium channel activity (inferred from direct assay from MGI).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005516; Molecular function: calmodulin binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005034; Molecular function: osmosensor activity (inferred from direct assay from MGI).
GO:0006816; Biological process: calcium ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0006874; Biological process: cellular calcium ion homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0042538; Biological process: hyperosmotic salinity response (inferred from mutant phenotype from MGI).
GO:0007231; Biological process: osmosensory signaling pathway (inferred from direct assay from MGI).
GO:0047484; Biological process: regulation of response to osmotic stress (inferred from mutant phenotype from MGI).
GO:0030103; Biological process: vasopressin secretion (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR002110; ANK.
IPR005821; Ion_trans.
IPR004729; TRP_channel.
IPR008347; Vanilpoid_rcpt.
IPR008348; Vanilpoid_rcpt_2.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.20; ANK; 1.
Pfam PF00023; Ank; 3.
PF00520; Ion_trans; 1.
Pfam graphical view of domain structure.
PRINTS PR01768; TRPVRECEPTOR.
PR01769; VRL2RECEPTOR.
SMART SM00248; ANK; 3.
SMART graphical view of domain structure.
TIGRFAMs TIGR00870; trp; 1.
PROSITE PS50297; ANK_REP_REGION; 1.
PS50088; ANK_REPEAT; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSMUSG00000014158; Mus musculus. [Contig view]
GeneID 63873; -.
KEGG mmu:63873; -.
Phylogenomic databases
HOGENOM Q9EPK8; -.
HOVERGEN Q9EPK8; -.
OMA Q9EPK8; QPPPILK.
Other
NextBio 319803; -.
SOURCE Trpv4; Mus musculus.
ProtoNet Q9EPK8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ANK repeat; Calcium; Calcium channel; Calcium transport; Calmodulin-binding; Ion transport; Ionic channel; Membrane; Phosphoprotein; Repeat; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   871  871     Transient receptor potential cation channel subfamily V member 4. PRO_0000215348
TOPO_DOM   1   465  465     Cytoplasmic (Potential). 
TRANSMEM   466   486  21     Potential. 
TOPO_DOM   487   508  22     Extracellular (Potential). 
TRANSMEM   509   529  21     Potential. 
TOPO_DOM   530   550  21     Cytoplasmic (Potential). 
TRANSMEM   551   571  21     Potential. 
TOPO_DOM   572   572  1     Extracellular (Potential). 
TRANSMEM   573   593  21     Potential. 
TOPO_DOM   594   616  23     Cytoplasmic (Potential). 
TRANSMEM   617   637  21     Potential. 
TOPO_DOM   638   690  53     Pore forming (Probable). 
TRANSMEM   691   711  21     Potential. 
TOPO_DOM   712   871  160     Cytoplasmic (Potential). 
REPEAT   237   266  30     ANK 1. 
REPEAT   284   313  30     ANK 2. 
REPEAT   369   398  30     ANK 3. 
REGION   812   831  20     Interaction with calmodulin (By similarity). 
MOD_RES   253   253        Phosphotyrosine; by LYN (Probable). 
MUTAGEN   253   253        Y->F: Abolishes hypotonicity-dependent channel activity. 
MUTAGEN   672   672        D->A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682. 
MUTAGEN   675   675        K->A: No effect on channel pore properties. 
MUTAGEN   680   680        M->A: Impairs Ca(2+) permeation. 
MUTAGEN   682   682        D->A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672. 
CONFLICT   45    45        G -> S (in Ref. 1; AAG28028). 
CONFLICT   90    90        L -> R (in Ref. 3 and 5). 
CONFLICT   137   137        A -> T (in Ref. 4; BAA83731). 
CONFLICT   210   211        IP -> LQ (in Ref. 4; BAA83731). 
CONFLICT   477   477        S -> P (in Ref. 1; AAG28028). 
CONFLICT   784   784        N -> S (in Ref. 4; BAA83731). 
Sequence information
Length: 871 AA [This is the length of the unprocessed precursor] Molecular weight: 98027 Da [This is the MW of the unprocessed precursor] CRC64: 5BAC6E33F89CEA05 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADPGDGPRA APGEVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS PVDASRPAGP 

        70         80         90        100        110        120 
GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHPSDN 

       130        140        150        160        170        180 
KRWRRKVVEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL SFLLTHKKRL 

       190        200        210        220        230        240 
TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT 

       250        260        270        280        290        300 
SLHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 

       310        320        330        340        350        360 
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCSRLFPDS 

       370        380        390        400        410        420 
NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD 

       430        440        450        460        470        480 
LSSLDTCGEE VSVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC 

       490        500        510        520        530        540 
AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLFT GVLFFFTSIK DLFTKKCPGV 

       550        560        570        580        590        600 
NSLFVDGSFQ LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 

       610        620        630        640        650        660 
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS NCTVPTYPAC 

       670        680        690        700        710        720 
RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV TYIILTFVLL LNMLIALMGE 

       730        740        750        760        770        780 
TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV 

       790        800        810        820        830        840 
DEVNWSHWNQ NLGIINEDPG KSEIYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSSADE 

       850        860        870 
VVVPLDNLGN PNCDGHQQGY APKWRTDDAP L 

Q9EPK8 in FASTA format

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