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Transient receptor potential cation channel subfamily V member 4 (TrpV4) (Osm-9-like TRP channel 4) (OTRPC4) (Transient receptor potential protein 12) (TRP12) (Vanilloid receptor-like channel 2) (Vanilloid receptor-like protein 2) (Vanilloid receptor-related osmotically-activated channel) (VR-OAC)

 TRPV4_MOUSE             Reviewed;         871 AA.
Q9EPK8; A0JNY0; Q91XR5; Q9EQZ4; Q9ERZ7; Q9ES76;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 144.
RecName: Full=Transient receptor potential cation channel subfamily V member 4;
Short=TrpV4;
AltName: Full=Osm-9-like TRP channel 4;
Short=OTRPC4;
AltName: Full=Transient receptor potential protein 12;
Short=TRP12;
AltName: Full=Vanilloid receptor-like channel 2;
AltName: Full=Vanilloid receptor-like protein 2;
AltName: Full=Vanilloid receptor-related osmotically-activated channel {ECO:0000303|PubMed:11081638};
Short=VR-OAC {ECO:0000303|PubMed:11081638};
Name=Trpv4; Synonyms=Trp12, Vrl2, Vroac;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Hypothalamus;
PubMed=11081638; DOI=10.1016/S0092-8674(00)00143-4;
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;
PubMed=11094154; DOI=10.1016/S0014-5793(00)02212-2;
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;
PubMed=11025659; DOI=10.1038/35036318;
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;
PubMed=12692122; DOI=10.1074/jbc.M302561200;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CHARACTERIZATION OF CHANNEL PORE, FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ASP-672; LYS-675; MET-680 AND ASP-682.
PubMed=12093812; DOI=10.1074/jbc.M204828200;
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).
[8]
INTERACTION WITH MAP7.
PubMed=14517216; DOI=10.1074/jbc.M308212200;
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).
[9]
INTERACTION WITH LYN; SRC; FYN; HCK; LCK AND YES, PHOSPHORYLATION AT
TYR-253, AND MUTAGENESIS OF TYR-253.
PubMed=12538589; DOI=10.1074/jbc.M211061200;
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).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-253; TYR-556
AND SER-557.
PubMed=14691263; DOI=10.1073/pnas.0303329101;
Vriens J., Watanabe H., Janssens A., Droogmans G., Voets T.,
Nilius B.;
"Cell swelling, heat, and chemical agonists use distinct pathways for
the activation of the cation channel TRPV4.";
Proc. Natl. Acad. Sci. U.S.A. 101:396-401(2004).
[11]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-651, AND
GLYCOSYLATION AT ASN-651.
PubMed=16368742; DOI=10.1152/ajprenal.00245.2005;
Xu H., Fu Y., Tian W., Cohen D.M.;
"Glycosylation of the osmoresponsive transient receptor potential
channel TRPV4 on Asn-651 influences membrane trafficking.";
Am. J. Physiol. 290:F1103-F1109(2006).
[12]
FUNCTION, INTERACTION WITH AQP5, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=16571723; DOI=10.1074/jbc.M600549200;
Liu X., Bandyopadhyay B.C., Bandyopadhyay B., Nakamoto T., Singh B.,
Liedtke W., Melvin J.E., Ambudkar I.;
"A role for AQP5 in activation of TRPV4 by hypotonicity: concerted
involvement of AQP5 and TRPV4 in regulation of cell volume recovery.";
J. Biol. Chem. 281:15485-15495(2006).
[13]
SUBCELLULAR LOCATION, INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3,
MUTAGENESIS OF 142-PRO-PRO-143, AND TISSUE SPECIFICITY.
PubMed=16627472; DOI=10.1074/jbc.M602452200;
Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B.,
Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.;
"PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the
subcellular localization of TRPV4.";
J. Biol. Chem. 281:18753-18762(2006).
[14]
FUNCTION, AND INTERACTION WITH PACSIN3.
PubMed=18174177; DOI=10.1074/jbc.M706386200;
D'hoedt D., Owsianik G., Prenen J., Cuajungco M.P., Grimm C.,
Heller S., Voets T., Nilius B.;
"Stimulus-specific modulation of the cation channel TRPV4 by PACSIN
3.";
J. Biol. Chem. 283:6272-6280(2008).
[15]
FUNCTION, INTERACTION WITH PKD2, AND SUBCELLULAR LOCATION.
PubMed=18695040; DOI=10.1083/jcb.200805124;
Kottgen M., Buchholz B., Garcia-Gonzalez M.A., Kotsis F., Fu X.,
Doerken M., Boehlke C., Steffl D., Tauber R., Wegierski T.,
Nitschke R., Suzuki M., Kramer-Zucker A., Germino G.G., Watnick T.,
Prenen J., Nilius B., Kuehn E.W., Walz G.;
"TRPP2 and TRPV4 form a polymodal sensory channel complex.";
J. Cell Biol. 182:437-447(2008).
[16]
PHOSPHORYLATION AT TYR-110 AND TYR-805, AND MUTAGENESIS OF TYR-110.
PubMed=19033444; DOI=10.1074/jbc.M805357200;
Wegierski T., Lewandrowski U., Muller B., Sickmann A., Walz G.;
"Tyrosine phosphorylation modulates the activity of TRPV4 in response
to defined stimuli.";
J. Biol. Chem. 284:2923-2933(2009).
[17]
PHOSPHORYLATION AT SER-824, AND MUTAGENESIS OF SER-824.
PubMed=20043876; DOI=10.1016/j.bbrc.2009.12.140;
Peng H., Lewandrowski U., Muller B., Sickmann A., Walz G.,
Wegierski T.;
"Identification of a protein kinase C-dependent phosphorylation site
involved in sensitization of TRPV4 channel.";
Biochem. Biophys. Res. Commun. 391:1721-1725(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23021218; DOI=10.1016/j.cell.2012.08.034;
Ye L., Kleiner S., Wu J., Sah R., Gupta R.K., Banks A.S., Cohen P.,
Khandekar M.J., Bostrom P., Mepani R.J., Laznik D., Kamenecka T.M.,
Song X., Liedtke W., Mootha V.K., Puigserver P., Griffin P.R.,
Clapham D.E., Spiegelman B.M.;
"TRPV4 is a regulator of adipose oxidative metabolism, inflammation,
and energy homeostasis.";
Cell 151:96-110(2012).
[20]
INTERACTION WITH ANO1, AND SUBCELLULAR LOCATION.
PubMed=24509911; DOI=10.1096/fj.13-243436;
Takayama Y., Shibasaki K., Suzuki Y., Yamanaka A., Tominaga M.;
"Modulation of water efflux through functional interaction between
TRPV4 and TMEM16A/anoctamin 1.";
FASEB J. 28:2238-2248(2014).
[21]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION
WITH CTNBB1 AND CDH1.
PubMed=20413591; DOI=10.1074/jbc.M110.103606;
Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
"The TRPV4 channel contributes to intercellular junction formation in
keratinocytes.";
J. Biol. Chem. 285:18749-18758(2010).
-!- FUNCTION: Non-selective calcium permeant cation channel involved
in osmotic sensitivity and mechanosensitivity (PubMed:11094154).
Activation by exposure to hypotonicity within the physiological
range exhibits an outward rectification (PubMed:12093812,
PubMed:14691263, PubMed:16368742, PubMed:16571723). Also activated
by heat, low pH, citrate and phorbol esters (PubMed:14691263).
Increase of intracellular Ca(2+) potentiates currents. Channel
activity seems to be regulated by a calmodulin-dependent mechanism
with a negative feedback mechanism (By similarity). Acts as a
regulator of intracellular Ca(2+) in synoviocytes (By similarity).
Plays an obligatory role as a molecular component in the
nonselective cation channel activation induced by 4-alpha-phorbol
12,13-didecanoate and hypotonic stimulation in synoviocytes and
also regulates production of IL-8 (By similarity). Together with
PKD2, forms mechano- and thermosensitive channels in cilium
(PubMed:18695040). Promotes cell-cell junction formation in skin
keratinocytes and plays an important role in the formation and/or
maintenance of functional intercellular barriers
(PubMed:20413591). Negatively regulates expression of PPARGC1A,
UCP1, oxidative metabolism and respiration in adipocytes
(PubMed:23021218). Regulates expression of chemokines and
cytokines related to proinflammatory pathway in adipocytes
(PubMed:23021218). Together with AQP5, controls regulatory volume
decrease in salivary epithelial cells (PubMed:16571723). Required
for normal development and maintenance of bone and cartilage (By
similarity). {ECO:0000250|UniProtKB:Q9HBA0,
ECO:0000269|PubMed:11094154, ECO:0000269|PubMed:12093812,
ECO:0000269|PubMed:14691263, ECO:0000269|PubMed:16368742,
ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:18174177,
ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:20413591,
ECO:0000269|PubMed:23021218}.
-!- SUBUNIT: Homotetramer. Interacts with calmodulin (By similarity).
Interacts with CTNNB1 (PubMed:20413591). The TRPV4 and CTNNB1
complex can interact with CDH1 (PubMed:20413591). Part of a
complex containing MLC1, AQP4, HEPACAM and ATP1B1 (By similarity).
Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC,
FYN, HCK, LCK and YES (PubMed:14517216, PubMed:12538589).
Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain)
(PubMed:16627472, PubMed:18174177). Interacts with ITPR3 (By
similarity). Interacts with AQP5; the interaction is probably
indirect and regulates TRPV4 activation by hypotonicity
(PubMed:16571723). Interacts with ANO1 (PubMed:24509911).
Interacts (via C-terminus) with PKD2 (via C-terminus)
(PubMed:18695040). {ECO:0000250|UniProtKB:Q9HBA0,
ECO:0000269|PubMed:12538589, ECO:0000269|PubMed:14517216,
ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:16627472,
ECO:0000269|PubMed:18174177, ECO:0000269|PubMed:18695040,
ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:24509911}.
-!- INTERACTION:
P55088:Aqp4; NbExp=2; IntAct=EBI-7091763, EBI-6273066;
P0CG48:UBC (xeno); NbExp=3; IntAct=EBI-7091763, EBI-3390054;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:14691263, ECO:0000269|PubMed:16571723,
ECO:0000269|PubMed:16627472, ECO:0000269|PubMed:24509911,
ECO:0000305|PubMed:12093812, ECO:0000305|PubMed:16368742}; Multi-
pass membrane protein {ECO:0000305}. Cell junction, adherens
junction {ECO:0000269|PubMed:20413591}. Cell projection, cilium
{ECO:0000269|PubMed:18695040}. Note=Assembly of the putative
homotetramer occurs primarily in the endoplasmic reticulum.
{ECO:0000250|UniProtKB:Q9HBA0}.
-!- TISSUE SPECIFICITY: Detected in liver, kidney, heart, brain
cortex, cerebellum and brainstem (at protein level). Expressed in
salivary glands (at protein level) (PubMed:16571723). Expressed in
heart, lung, spleen, liver, kidney, brain, skeletal muscle 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.
{ECO:0000269|PubMed:11025659, ECO:0000269|PubMed:11081638,
ECO:0000269|PubMed:11094154, ECO:0000269|PubMed:12692122,
ECO:0000269|PubMed:16571723, ECO:0000269|PubMed:16627472}.
-!- DOMAIN: The ANK repeat region mediates interaction with Ca(2+)-
calmodulin and ATP binding. The ANK repeat region mediates
interaction with phosphatidylinositol-4,5-bisphosphate and related
phosphatidylinositides. {ECO:0000250|UniProtKB:A0A1D5PXA5}.
-!- PTM: N-glycosylated. {ECO:0000305|PubMed:16368742}.
-!- DISRUPTION PHENOTYPE: Mice display impairment of the intercellular
junction-dependent barrier function in the skin (PubMed:20413591).
Increased energy expenditure and improved insulin sensitivity in
white adipose tissues (PubMed:23021218). Reduced Ca2+ entry and
loss of regulatory volume decrease in response to hypotonicity in
acinar cells (PubMed:16571723). {ECO:0000269|PubMed:16571723,
ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:23021218}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV4 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG28028.1; Type=Frameshift; Positions=47, 50, 53, 72, 73; Evidence={ECO:0000305};
Sequence=AAK69486.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF263522; AAG28028.1; ALT_FRAME; mRNA.
EMBL; AJ296078; CAC20703.1; -; mRNA.
EMBL; AF208026; AAG17543.1; -; mRNA.
EMBL; AB021875; BAA83731.2; -; mRNA.
EMBL; AF279672; AAK69486.1; ALT_INIT; mRNA.
EMBL; BC127052; AAI27053.1; -; mRNA.
CCDS; CCDS19568.1; -.
RefSeq; NP_071300.2; NM_022017.3.
RefSeq; XP_006530495.2; XM_006530432.2.
UniGene; Mm.266450; -.
ProteinModelPortal; Q9EPK8; -.
SMR; Q9EPK8; -.
DIP; DIP-44011N; -.
IntAct; Q9EPK8; 3.
MINT; Q9EPK8; -.
STRING; 10090.ENSMUSP00000071859; -.
BindingDB; Q9EPK8; -.
ChEMBL; CHEMBL6126; -.
GuidetoPHARMACOLOGY; 510; -.
iPTMnet; Q9EPK8; -.
PhosphoSitePlus; Q9EPK8; -.
MaxQB; Q9EPK8; -.
PaxDb; Q9EPK8; -.
PRIDE; Q9EPK8; -.
Ensembl; ENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158.
Ensembl; ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158.
GeneID; 63873; -.
KEGG; mmu:63873; -.
UCSC; uc008yzu.1; mouse.
CTD; 59341; -.
MGI; MGI:1926945; Trpv4.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
GeneTree; ENSGT00550000074425; -.
HOGENOM; HOG000234630; -.
HOVERGEN; HBG054085; -.
InParanoid; Q9EPK8; -.
KO; K04973; -.
OMA; GDLEMIN; -.
OrthoDB; EOG091G016O; -.
PhylomeDB; Q9EPK8; -.
TreeFam; TF314711; -.
Reactome; R-MMU-3295583; TRP channels.
PRO; PR:Q9EPK8; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000014158; Expressed in 141 organ(s), highest expression level in intervertebral disk of lumbar vertebra.
ExpressionAtlas; Q9EPK8; baseline and differential.
Genevisible; Q9EPK8; MM.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005929; C:cilium; IDA:MGI.
GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0030175; C:filopodium; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISO:MGI.
GO; GO:0003779; F:actin binding; ISO:MGI.
GO; GO:0051015; F:actin filament binding; ISO:MGI.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
GO; GO:0005262; F:calcium channel activity; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0005261; F:cation channel activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; ISO:MGI.
GO; GO:0005034; F:osmosensor activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
GO; GO:0042169; F:SH2 domain binding; IPI:BHF-UCL.
GO; GO:0015275; F:stretch-activated, cation-selective, calcium channel activity; ISO:MGI.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0007015; P:actin filament organization; ISO:MGI.
GO; GO:0097497; P:blood vessel endothelial cell delamination; ISO:MGI.
GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
GO; GO:0006816; P:calcium ion transport; ISO:MGI.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; ISO:MGI.
GO; GO:0007043; P:cell-cell junction assembly; IMP:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
GO; GO:0071476; P:cellular hypotonic response; IDA:BHF-UCL.
GO; GO:0071477; P:cellular hypotonic salinity response; IMP:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IMP:UniProtKB.
GO; GO:0071470; P:cellular response to osmotic stress; IMP:UniProtKB.
GO; GO:0043622; P:cortical microtubule organization; ISO:MGI.
GO; GO:0002024; P:diet induced thermogenesis; IMP:UniProtKB.
GO; GO:0097009; P:energy homeostasis; IMP:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0042538; P:hyperosmotic salinity response; IMP:MGI.
GO; GO:0006971; P:hypotonic response; ISO:MGI.
GO; GO:0046785; P:microtubule polymerization; ISO:MGI.
GO; GO:0050891; P:multicellular organismal water homeostasis; ISO:MGI.
GO; GO:1903444; P:negative regulation of brown fat cell differentiation; IMP:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0007231; P:osmosensory signaling pathway; IDA:BHF-UCL.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IMP:UniProtKB.
GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IMP:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:UniProtKB.
GO; GO:0071642; P:positive regulation of macrophage inflammatory protein 1 alpha production; IMP:UniProtKB.
GO; GO:0031117; P:positive regulation of microtubule depolymerization; ISO:MGI.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
GO; GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0047484; P:regulation of response to osmotic stress; IMP:MGI.
GO; GO:0032868; P:response to insulin; IMP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IDA:MGI.
GO; GO:1903759; P:signal transduction involved in regulation of aerobic respiration; IMP:UniProtKB.
GO; GO:0030103; P:vasopressin secretion; IMP:MGI.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR024862; TRPV.
InterPro; IPR008347; TRPV1-4_channel.
InterPro; IPR008348; TRPV4_channel.
PANTHER; PTHR10582; PTHR10582; 1.
PANTHER; PTHR10582:SF4; PTHR10582:SF4; 1.
Pfam; PF00023; Ank; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01768; TRPVRECEPTOR.
PRINTS; PR01769; VRL2RECEPTOR.
SMART; SM00248; ANK; 3.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
1: Evidence at protein level;
ANK repeat; ATP-binding; Calcium; Calcium channel; Calcium transport;
Calmodulin-binding; Cell junction; Cell membrane; Cell projection;
Cilium; Complete proteome; Glycoprotein; Ion channel; Ion transport;
Lipid-binding; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 871 Transient receptor potential cation
channel subfamily V member 4.
/FTId=PRO_0000215348.
TOPO_DOM 1 469 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 470 490 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 491 507 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 508 534 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 535 547 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 548 568 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 569 572 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 573 593 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 594 608 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 609 636 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 637 665 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
INTRAMEM 666 685 Pore-forming.
{ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 686 693 Extracellular.
{ECO:0000250|UniProtKB:O35433}.
TRANSMEM 694 722 Helical. {ECO:0000250|UniProtKB:O35433}.
TOPO_DOM 723 871 Cytoplasmic.
{ECO:0000250|UniProtKB:O35433}.
REPEAT 237 266 ANK 1.
REPEAT 284 313 ANK 2.
REPEAT 369 398 ANK 3.
NP_BIND 236 239 ATP. {ECO:0000250|UniProtKB:Q9HBA0}.
REGION 249 251 Phosphatidylinositol-1,4,5-trisphosphate
binding.
{ECO:0000250|UniProtKB:A0A1D5PXA5}.
REGION 296 299 Phosphatidylinositol-1,4,5-trisphosphate
binding.
{ECO:0000250|UniProtKB:A0A1D5PXA5}.
REGION 812 831 Interaction with calmodulin and ITPR3.
{ECO:0000250|UniProtKB:Q9HBA0}.
MOTIF 679 682 Selectivity filter.
{ECO:0000305|PubMed:12093812}.
METAL 682 682 Calcium; shared with neighboring
subunits. {ECO:0000250|UniProtKB:Q9R186}.
BINDING 192 192 ATP. {ECO:0000250|UniProtKB:Q9HBA0}.
BINDING 197 197 ATP. {ECO:0000250|UniProtKB:Q9HBA0}.
BINDING 201 201 ATP. {ECO:0000250|UniProtKB:Q9HBA0}.
BINDING 248 248 ATP. {ECO:0000250|UniProtKB:Q9HBA0}.
BINDING 344 344 Phosphatidylinositol-1,4,5-trisphosphate.
{ECO:0000250|UniProtKB:A0A1D5PXA5}.
MOD_RES 110 110 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000269|PubMed:19033444}.
MOD_RES 253 253 Phosphotyrosine; by LYN.
{ECO:0000305|PubMed:12538589}.
MOD_RES 805 805 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000269|PubMed:19033444}.
MOD_RES 824 824 Phosphoserine; by PKC and PKA.
{ECO:0000269|PubMed:20043876}.
CARBOHYD 651 651 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:16368742}.
MUTAGEN 110 110 Y->F: Increases protein abundance at
plasma membrane. Greatly reduces channel
activity. {ECO:0000269|PubMed:19033444}.
MUTAGEN 142 143 PP->AL: Strongly reduced interaction with
PACSIN3. {ECO:0000269|PubMed:16627472}.
MUTAGEN 253 253 Y->F: Results are conflicting as to
whether hypotonicity-dependent channel
activity is abolished.
{ECO:0000269|PubMed:12538589,
ECO:0000269|PubMed:14691263}.
MUTAGEN 556 556 Y->A: Reduces channel activation by 4-
alpha-PDD and heat but not hypo-osmotic
cell swelling.
{ECO:0000269|PubMed:14691263}.
MUTAGEN 556 556 Y->F: No changes in channel activation by
4-alpha-PDD or heat.
{ECO:0000269|PubMed:14691263}.
MUTAGEN 557 557 S->A: No changes in channel activity.
{ECO:0000269|PubMed:14691263}.
MUTAGEN 651 651 N->Q: Loss of a probable N-glycosylation
site. Increased expression at the cell
membrane, leading to increased ion
currents. {ECO:0000269|PubMed:16368742}.
MUTAGEN 672 672 D->A: Greatly reduces Ca(2+) permeation
and channel rectification; when
associated with A-682.
{ECO:0000269|PubMed:12093812}.
MUTAGEN 675 675 K->A: No effect on channel pore
properties.
{ECO:0000269|PubMed:12093812}.
MUTAGEN 680 680 M->A: Impairs Ca(2+) permeation.
{ECO:0000269|PubMed:12093812}.
MUTAGEN 682 682 D->A: Greatly reduces Ca(2+) permeation
and channel rectification; when
associated with A-672.
{ECO:0000269|PubMed:12093812}.
MUTAGEN 805 805 Y->F: No changes in channel activity.
{ECO:0000269|PubMed:19033444}.
MUTAGEN 824 824 S->A: Loss of phosphorylation but no
significant effect on channel activity.
{ECO:0000269|PubMed:20043876}.
MUTAGEN 824 824 S->D: Phosphomimetic mutant which
enhances channel function.
{ECO:0000269|PubMed:20043876}.
CONFLICT 45 45 G -> S (in Ref. 1; AAG28028).
{ECO:0000305}.
CONFLICT 90 90 L -> R (in Ref. 3; AAG17543 and 5;
AAK69486). {ECO:0000305}.
CONFLICT 137 137 A -> T (in Ref. 4; BAA83731).
{ECO:0000305}.
CONFLICT 210 211 IP -> LQ (in Ref. 4; BAA83731).
{ECO:0000305}.
CONFLICT 477 477 S -> P (in Ref. 1; AAG28028).
{ECO:0000305}.
CONFLICT 784 784 N -> S (in Ref. 4; BAA83731).
{ECO:0000305}.
SEQUENCE 871 AA; 98027 MW; 5BAC6E33F89CEA05 CRC64;
MADPGDGPRA APGEVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS PVDASRPAGP
GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHPSDN
KRWRRKVVEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL SFLLTHKKRL
TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT
SLHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCSRLFPDS
NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD
LSSLDTCGEE VSVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC
AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLFT GVLFFFTSIK DLFTKKCPGV
NSLFVDGSFQ LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS NCTVPTYPAC
RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV TYIILTFVLL LNMLIALMGE
TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV
DEVNWSHWNQ NLGIINEDPG KSEIYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSSADE
VVVPLDNLGN PNCDGHQQGY APKWRTDDAP L


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