Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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) (VRL-2) (Vanilloid receptor-related osmotically-activated channel) (VR-OAC)

 TRPV4_HUMAN             Reviewed;         871 AA.
Q9HBA0; B7ZKQ6; Q17R79; Q2Y122; Q2Y123; Q2Y124; Q86YZ6; Q8NDY7;
Q8NG64; Q96Q92; Q96RS7; Q9HBC0;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
05-DEC-2018, entry version 161.
RecName: Full=Transient receptor potential cation channel subfamily V member 4;
Short=TrpV4;
AltName: Full=Osm-9-like TRP channel 4;
Short=OTRPC4 {ECO:0000303|PubMed:11025659};
AltName: Full=Transient receptor potential protein 12;
Short=TRP12;
AltName: Full=Vanilloid receptor-like channel 2;
AltName: Full=Vanilloid receptor-like protein 2;
Short=VRL-2;
AltName: Full=Vanilloid receptor-related osmotically-activated channel {ECO:0000303|PubMed:11081638};
Short=VR-OAC {ECO:0000303|PubMed:11081638};
Name=TRPV4; Synonyms=VRL2, VROAC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORM 1), AND FUNCTION.
TISSUE=Kidney cortex;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ishibashi K.;
"Molecular cloning of a new member of vanilloid receptor channel-like
proteins.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kelsell R.E.;
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT MTD PRO-618.
TISSUE=Aortic endothelium;
Xu F., Satoh E., Iijima T.;
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6), FUNCTION (ISOFORMS
1; 2; 4; 5 AND 6), SUBCELLULAR LOCATION (ISOFORMS 1; 2; 4; 5 AND 6),
SELF-ASSOCIATION, AND GLYCOSYLATION.
PubMed=16293632; DOI=10.1074/jbc.M511456200;
Arniges M., Fernandez-Fernandez J.M., Albrecht N., Schaefer M.,
Valverde M.A.;
"Human TRPV4 channel splice variants revealed a key role of ankyrin
domains in multimerization and trafficking.";
J. Biol. Chem. 281:1580-1586(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 69-871.
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.
[11]
FUNCTION, INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF
186-ARG--SER-824 AND ARG-828.
PubMed=12724311; DOI=10.1074/jbc.M302590200;
Strotmann R., Schultz G., Plant T.D.;
"Ca2+-dependent potentiation of the nonselective cation channel TRPV4
is mediated by a C-terminal calmodulin binding site.";
J. Biol. Chem. 278:26541-26549(2003).
[12]
FUNCTION, INTERACTION WITH ITPR3, AND SUBCELLULAR LOCATION.
PubMed=18826956; DOI=10.1074/jbc.C800184200;
Garcia-Elias A., Lorenzo I.M., Vicente R., Valverde M.A.;
"IP3 receptor binds to and sensitizes TRPV4 channel to osmotic stimuli
via a calmodulin-binding site.";
J. Biol. Chem. 283:31284-31288(2008).
[13]
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).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19759329; DOI=10.1152/ajpcell.00204.2009;
Itoh Y., Hatano N., Hayashi H., Onozaki K., Miyazawa K., Muraki K.;
"An environmental sensor, TRPV4 is a novel regulator of intracellular
Ca2+ in human synoviocytes.";
Am. J. Physiol. 297:C1082-C1090(2009).
[15]
INVOLVEMENT IN SSQTL1, AND ASSOCIATION OF VARIANT SER-19 WITH
HYPONATREMIA.
PubMed=19666518; DOI=10.1073/pnas.0904084106;
Tian W., Fu Y., Garcia-Elias A., Fernandez-Fernandez J.M., Vicente R.,
Kramer P.L., Klein R.F., Hitzemann R., Orwoll E.S., Wilmot B.,
McWeeney S., Valverde M.A., Cohen D.M.;
"A loss-of-function nonsynonymous polymorphism in the osmoregulatory
TRPV4 gene is associated with human hyponatremia.";
Proc. Natl. Acad. Sci. U.S.A. 106:14034-14039(2009).
[16]
SUBUNIT.
PubMed=22328087; DOI=10.1093/hmg/dds032;
Lanciotti A., Brignone M.S., Molinari P., Visentin S., De Nuccio C.,
Macchia G., Aiello C., Bertini E., Aloisi F., Petrucci T.C.,
Ambrosini E.;
"Megalencephalic leukoencephalopathy with subcortical cysts protein 1
functionally cooperates with the TRPV4 cation channel to activate the
response of astrocytes to osmotic stress: dysregulation by
pathological mutations.";
Hum. Mol. Genet. 21:2166-2180(2012).
[17]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, DOMAIN,
MUTAGENESIS OF LYS-251; ASN-296; HIS-299 AND LYS-344, AND
CHARACTERIZATION OF VARIANTS CMT2C CYS-232; HIS-269; TRP-315 AND
HIS-316.
PubMed=25256292; DOI=10.1038/ncomms5994;
Takahashi N., Hamada-Nakahara S., Itoh Y., Takemura K., Shimada A.,
Ueda Y., Kitamata M., Matsuoka R., Hanawa-Suetsugu K., Senju Y.,
Mori M.X., Kiyonaka S., Kohda D., Kitao A., Mori Y., Suetsugu S.;
"TRPV4 channel activity is modulated by direct interaction of the
ankyrin domain to PI(4,5)P.";
Nat. Commun. 5:4994-4994(2014).
[18]
FUNCTION, VARIANT MTD LEU-799, AND CHARACTERIZATION OF VARIANT MTD
LEU-799.
PubMed=26249260; DOI=10.1002/ajmg.a.37182;
Hurd L., Kirwin S.M., Boggs M., Mackenzie W.G., Bober M.B.,
Funanage V.L., Duncan R.L.;
"A mutation in TRPV4 results in altered chondrocyte calcium signaling
in severe metatropic dysplasia.";
Am. J. Med. Genet. A 167A:2286-2293(2015).
[19]
INVOLVEMENT IN ANFH2.
PubMed=27330106; DOI=10.1136/jmedgenet-2016-103829;
Mah W., Sonkusare S.K., Wang T., Azeddine B., Pupavac M.,
Carrot-Zhang J., Hong K., Majewski J., Harvey E.J., Russell L.,
Chalk C., Rosenblatt D.S., Nelson M.T., Seguin C.;
"Gain-of-function mutation in TRPV4 identified in patients with
osteonecrosis of the femoral head.";
J. Med. Genet. 53:705-709(2016).
[20]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 149-397 ALONE AND IN COMPLEX
WITH ATP, MUTAGENESIS OF PHE-231, CHARACTERIZATION OF VARIANTS MTD
ARG-197; PHE-199; ALA-295; PHE-331; THR-331 AND PHE-342,
CHARACTERIZATION OF VARIANTS SMDK LYS-278 AND GLY-333,
CHARACTERIZATION OF VARIANTS CMT2C CYS-232; HIS-269; TRP-315 AND
CYS-316, CHARACTERIZATION OF VARIANT SPSMA CYS-316, CHARACTERIZATION
OF VARIANT LYS-183, AND CHARACTERIZATION OF VARIANTS HMN8 CYS-232 AND
HIS-269.
PubMed=22702953; DOI=10.1021/bi300279b;
Inada H., Procko E., Sotomayor M., Gaudet R.;
"Structural and biochemical consequences of disease-causing mutations
in the ankyrin repeat domain of the human TRPV4 channel.";
Biochemistry 51:6195-6206(2012).
[21]
VARIANTS BCYM3 GLN-616 AND ILE-620, AND CHARACTERIZATION OF VARIANTS
BCYM3 GLN-616 AND ILE-620.
PubMed=18587396; DOI=10.1038/ng.166;
Rock M.J., Prenen J., Funari V.A., Funari T.L., Merriman B.,
Nelson S.F., Lachman R.S., Wilcox W.R., Reyno S., Quadrelli R.,
Vaglio A., Owsianik G., Janssens A., Voets T., Ikegawa S., Nagai T.,
Rimoin D.L., Nilius B., Cohn D.H.;
"Gain-of-function mutations in TRPV4 cause autosomal dominant
brachyolmia.";
Nat. Genet. 40:999-1003(2008).
[22]
VARIANTS SMDK GLY-333; HIS-594 AND SER-716, AND VARIANTS MTD PHE-331
AND LEU-799.
PubMed=19232556; DOI=10.1016/j.ajhg.2009.01.021;
Krakow D., Vriens J., Camacho N., Luong P., Deixler H., Funari T.L.,
Bacino C.A., Irons M.B., Holm I.A., Sadler L., Okenfuss E.B.,
Janssens A., Voets T., Rimoin D.L., Lachman R.S., Nilius B.,
Cohn D.H.;
"Mutations in the gene encoding the calcium-permeable ion channel
TRPV4 produce spondylometaphyseal dysplasia, Kozlowski type and
metatropic dysplasia.";
Am. J. Hum. Genet. 84:307-315(2009).
[23]
VARIANTS MTD ILE-89; ARG-197; PHE-331; PHE-471 DEL; MET-604; LEU-617;
PRO-618; LYS-797 AND LEU-799.
PubMed=20425821; DOI=10.1002/ajmg.a.33392;
Camacho N., Krakow D., Johnykutty S., Katzman P.J., Pepkowitz S.,
Vriens J., Nilius B., Boyce B.F., Cohn D.H.;
"Dominant TRPV4 mutations in nonlethal and lethal metatropic
dysplasia.";
Am. J. Med. Genet. A 152:1169-1177(2010).
[24]
INVOLVEMENT IN SEDM, VARIANT PSTD HIS-594, AND VARIANTS LYS-183;
CYS-602; LYS-797 AND LEU-799.
PubMed=20503319; DOI=10.1002/ajmg.a.33414;
Nishimura G., Dai J., Lausch E., Unger S., Megarbane A., Kitoh H.,
Kim O.H., Cho T.J., Bedeschi F., Benedicenti F., Mendoza-Londono R.,
Silengo M., Schmidt-Rimpler M., Spranger J., Zabel B., Ikegawa S.,
Superti-Furga A.;
"Spondylo-epiphyseal dysplasia, Maroteaux type (pseudo-Morquio
syndrome type 2), and parastremmatic dysplasia are caused by TRPV4
mutations.";
Am. J. Med. Genet. A 152:1443-1449(2010).
[25]
VARIANTS MTD PHE-199; ALA-295; THR-331; PHE-342; PHE-471 DEL; LEU-592;
LYS-775; ALA-799; SER-799; LEU-799 AND ARG-799, AND VARIANTS SMDK
LYS-278; HIS-594; PRO-596; TRP-600; ILE-625; MET-709; TYR-777 AND
LYS-797.
PubMed=20577006; DOI=10.1136/jmg.2009.075358;
Dai J., Kim O.H., Cho T.J., Schmidt-Rimpler M., Tonoki H.,
Takikawa K., Haga N., Miyoshi K., Kitoh H., Yoo W.J., Choi I.H.,
Song H.R., Jin D.K., Kim H.T., Kamasaki H., Bianchi P.,
Grigelioniene G., Nampoothiri S., Minagawa M., Miyagawa S.I.,
Fukao T., Marcelis C., Jansweijer M.C., Hennekam R.C., Bedeschi F.,
Mustonen A., Jiang Q., Ohashi H., Furuichi T., Unger S., Zabel B.,
Lausch E., Superti-Furga A., Nishimura G., Ikegawa S.;
"Novel and recurrent TRPV4 mutations and their association with
distinct phenotypes within the TRPV4 dysplasia family.";
J. Med. Genet. 47:704-709(2010).
[26]
VARIANTS CMT2C TRP-315 AND CYS-316, VARIANT HMN8 HIS-269, AND
SUBCELLULAR LOCATION.
PubMed=20037588; DOI=10.1038/ng.508;
Auer-Grumbach M., Olschewski A., Papic L., Kremer H., McEntagart M.E.,
Uhrig S., Fischer C., Frohlich E., Balint Z., Tang B., Strohmaier H.,
Lochmuller H., Schlotter-Weigel B., Senderek J., Krebs A., Dick K.J.,
Petty R., Longman C., Anderson N.E., Padberg G.W., Schelhaas H.J.,
van Ravenswaaij-Arts C.M., Pieber T.R., Crosby A.H., Guelly C.;
"Alterations in the ankyrin domain of TRPV4 cause congenital distal
SMA, scapuloperoneal SMA and HMSN2C.";
Nat. Genet. 42:160-164(2010).
[27]
VARIANT CMT2C HIS-269, VARIANT SPSMA CYS-316, AND SUBCELLULAR
LOCATION.
PubMed=20037587; DOI=10.1038/ng.509;
Deng H.X., Klein C.J., Yan J., Shi Y., Wu Y., Fecto F., Yau H.J.,
Yang Y., Zhai H., Siddique N., Hedley-Whyte E.T., Delong R.,
Martina M., Dyck P.J., Siddique T.;
"Scapuloperoneal spinal muscular atrophy and CMT2C are allelic
disorders caused by alterations in TRPV4.";
Nat. Genet. 42:165-169(2010).
[28]
VARIANTS CMT2C CYS-269 AND HIS-269, CHARACTERIZATION OF VARIANTS CMT2C
CYS-269 AND HIS-269, AND FUNCTION.
PubMed=20037586; DOI=10.1038/ng.512;
Landoure G., Zdebik A.A., Martinez T.L., Burnett B.G., Stanescu H.C.,
Inada H., Shi Y., Taye A.A., Kong L., Munns C.H., Choo S.S.,
Phelps C.B., Paudel R., Houlden H., Ludlow C.L., Caterina M.J.,
Gaudet R., Kleta R., Fischbeck K.H., Sumner C.J.;
"Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C.";
Nat. Genet. 42:170-174(2010).
[29]
VARIANTS CMT2C TRP-315 AND TYR-542.
PubMed=21115951; DOI=10.1212/WNL.0b013e3181ffe4bb;
Chen D.H., Sul Y., Weiss M., Hillel A., Lipe H., Wolff J.,
Matsushita M., Raskind W., Bird T.;
"CMT2C with vocal cord paresis associated with short stature and
mutations in the TRPV4 gene.";
Neurology 75:1968-1975(2010).
[30]
VARIANTS FDAB VAL-270; PRO-271 AND LEU-273, CHARACTERIZATION OF
VARIANTS FDAB VAL-270; PRO-271 AND LEU-273, FUNCTION, SUBCELLULAR
LOCATION, AND GLYCOSYLATION.
PubMed=21964574; DOI=10.1038/ng.945;
Lamande S.R., Yuan Y., Gresshoff I.L., Rowley L., Belluoccio D.,
Kaluarachchi K., Little C.B., Botzenhart E., Zerres K., Amor D.J.,
Cole W.G., Savarirayan R., McIntyre P., Bateman J.F.;
"Mutations in TRPV4 cause an inherited arthropathy of hands and
feet.";
Nat. Genet. 43:1142-1146(2011).
[31]
VARIANTS CMT2C CYS-232 AND HIS-316, AND CHARACTERIZATION OF VARIANTS
CMT2C CYS-232; CYS-269; HIS-269 AND HIS-316.
PubMed=21288981; DOI=10.1212/WNL.0b013e31820f2de3;
Klein C.J., Shi Y., Fecto F., Donaghy M., Nicholson G.,
McEntagart M.E., Crosby A.H., Wu Y., Lou H., McEvoy K.M., Siddique T.,
Deng H.X., Dyck P.J.;
"TRPV4 mutations and cytotoxic hypercalcemia in axonal Charcot-Marie-
Tooth neuropathies.";
Neurology 76:887-894(2011).
[32]
VARIANTS HMN8 ARG-97 AND CYS-232, AND CHARACTERIZATION OF VARIANT HMN8
ARG-97.
PubMed=22526352; DOI=10.1007/s10048-012-0328-7;
Fiorillo C., Moro F., Brisca G., Astrea G., Nesti C., Balint Z.,
Olschewski A., Meschini M.C., Guelly C., Auer-Grumbach M., Battini R.,
Pedemonte M., Romano A., Menchise V., Biancheri R., Santorelli F.M.,
Bruno C.;
"TRPV4 mutations in children with congenital distal spinal muscular
atrophy.";
Neurogenetics 13:195-203(2012).
-!- FUNCTION: Non-selective calcium permeant cation channel involved
in osmotic sensitivity and mechanosensitivity. Activation by
exposure to hypotonicity within the physiological range exhibits
an outward rectification (PubMed:18826956, PubMed:18695040). Also
activated by heat, low pH, citrate and phorbol esters
(PubMed:16293632, PubMed:18826956, PubMed:18695040,
PubMed:25256292, PubMed:20037586, PubMed:21964574). Increase of
intracellular Ca(2+) potentiates currents. Channel activity seems
to be regulated by a calmodulin-dependent mechanism with a
negative feedback mechanism (PubMed:12724311, PubMed:18826956).
Promotes cell-cell junction formation in skin keratinocytes and
plays an important role in the formation and/or maintenance of
functional intercellular barriers (By similarity). Acts as a
regulator of intracellular Ca(2+) in synoviocytes
(PubMed:19759329). 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
(PubMed:19759329). Together with PKD2, forms mechano- and
thermosensitive channels in cilium (PubMed:18695040). Negatively
regulates expression of PPARGC1A, UCP1, oxidative metabolism and
respiration in adipocytes (By similarity). Regulates expression of
chemokines and cytokines related to proinflammatory pathway in
adipocytes (By similarity). Together with AQP5, controls
regulatory volume decrease in salivary epithelial cells (By
similarity). Required for normal development and maintenance of
bone and cartilage (PubMed:26249260).
{ECO:0000250|UniProtKB:Q9EPK8, ECO:0000269|PubMed:11025659,
ECO:0000269|PubMed:12724311, ECO:0000269|PubMed:16293632,
ECO:0000269|PubMed:18587396, ECO:0000269|PubMed:18695040,
ECO:0000269|PubMed:18826956, ECO:0000269|PubMed:19759329,
ECO:0000269|PubMed:20037586, ECO:0000269|PubMed:21964574,
ECO:0000269|PubMed:25256292, ECO:0000269|PubMed:26249260}.
-!- FUNCTION: Isoform 5: Non-selective calcium permeant cation channel
involved in osmotic sensitivity and mechanosensitivity. Activation
by exposure to hypotonicity within the physiological range
exhibits an outward rectification. Also activated by phorbol
esters. Has the same channel activity as isoform 1, and is
activated by the same stimuli. {ECO:0000269|PubMed:16293632}.
-!- FUNCTION: Isoform 2: Lacks channel activity, due to impaired
oligomerization and intracellular retention.
{ECO:0000269|PubMed:16293632}.
-!- FUNCTION: Isoform 4: Lacks channel activity, due to impaired
oligomerization and intracellular retention.
{ECO:0000269|PubMed:16293632}.
-!- FUNCTION: Isoform 6: Lacks channel activity, due to impaired
oligomerization and intracellular retention.
{ECO:0000269|PubMed:16293632}.
-!- ACTIVITY REGULATION: Channel activation is inhibited by binding to
phosphatidylinositol-4,5-bisphosphate, and to a much lesser degree
by phosphatidylinositol-3,4,5-trisphosphate. Not inhibited by
phosphatidylinositol-3,4-bisphosphate and phosphatidylinositol-
3,5-bisphosphate. {ECO:0000269|PubMed:25256292}.
-!- SUBUNIT: Homotetramer (Probable). Self-associates in a isoform-
specific manner (PubMed:16293632). Isoform 1 and isoform 5 can
oligomerize, but isoform 2, isoform 4 and isoform 6 cannnot
oligomerize (PubMed:16293632). Interacts with calmodulin
(PubMed:12724311). Interacts with Map7 and Src family Tyr protein
kinases LYN, SRC, FYN, HCK, LCK and YES (By similarity). Interacts
with CTNNB1 (By similarity). The TRPV4 and CTNNB1 complex can
interact with CDH1 (By similarity). Interacts with PACSIN1,
PACSIN2 and PACSIN3 (via SH3 domain) (By similarity). Part of a
complex containing MLC1, AQP4, HEPACAM and ATP1B1
(PubMed:22328087). Interacts with ITPR3 (PubMed:18826956).
Interacts with AQP5; the interaction is probably indirect and
regulates TRPV4 activation by hypotonicity (By similarity).
Interacts with ANO1 (By similarity). Interacts (via C-terminus)
with PKD2 (via C-terminus) (PubMed:18695040).
{ECO:0000250|UniProtKB:Q9EPK8, ECO:0000269|PubMed:12724311,
ECO:0000269|PubMed:16293632, ECO:0000269|PubMed:18695040,
ECO:0000269|PubMed:18826956, ECO:0000269|PubMed:22328087,
ECO:0000269|PubMed:22702953, ECO:0000305}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-962786, EBI-962786;
A0A0G2K4I1:Aqp4 (xeno); NbExp=2; IntAct=EBI-962786, EBI-15907702;
P47863-1:Aqp4 (xeno); NbExp=2; IntAct=EBI-962786, EBI-15907676;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:18826956}; Multi-
pass membrane protein {ECO:0000305}. Cell junction, adherens
junction {ECO:0000250|UniProtKB:Q9EPK8}. Cell projection, cilium
{ECO:0000269|PubMed:18695040}. Note=Assembly of the putative
homotetramer occurs primarily in the endoplasmic reticulum.
{ECO:0000269|PubMed:16293632, ECO:0000269|PubMed:20037587,
ECO:0000269|PubMed:20037588}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:16293632, ECO:0000269|PubMed:21964574,
ECO:0000269|PubMed:25256292}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane
{ECO:0000269|PubMed:16293632}.
-!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum
{ECO:0000269|PubMed:16293632}.
-!- SUBCELLULAR LOCATION: Isoform 4: Endoplasmic reticulum
{ECO:0000269|PubMed:16293632}.
-!- SUBCELLULAR LOCATION: Isoform 6: Endoplasmic reticulum
{ECO:0000269|PubMed:16293632}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=A;
IsoId=Q9HBA0-1; Sequence=Displayed;
Name=2; Synonyms=B, OTRPC4beta;
IsoId=Q9HBA0-2; Sequence=VSP_013436;
Note=Lacks channel activity, due to impaired oligomerization and
intracellular retention. {ECO:0000269|PubMed:16293632};
Name=3; Synonyms=TRPV-SV;
IsoId=Q9HBA0-3; Sequence=VSP_013437;
Name=4; Synonyms=C;
IsoId=Q9HBA0-4; Sequence=VSP_026615;
Note=Lacks channel activity, due to impaired oligomerization and
intracellular retention. {ECO:0000269|PubMed:16293632};
Name=5; Synonyms=D;
IsoId=Q9HBA0-5; Sequence=VSP_026614;
Note=Forms active ion channels. {ECO:0000269|PubMed:16293632};
Name=6; Synonyms=E;
IsoId=Q9HBA0-6; Sequence=VSP_026615, VSP_013436;
Note=Lacks channel activity, due to impaired oligomerization and
intracellular retention. {ECO:0000269|PubMed:16293632};
-!- TISSUE SPECIFICITY: Found in the synoviocytes from patients with
(RA) and without (CTR) rheumatoid arthritis (at protein level).
{ECO:0000269|PubMed:19759329}.
-!- DOMAIN: The ANK repeat region mediates interaction with Ca(2+)-
calmodulin and ATP binding (By similarity). The ANK repeat region
mediates interaction with phosphatidylinositol-4,5-bisphosphate
and related phosphatidylinositides (PubMed:25256292).
{ECO:0000250|UniProtKB:A0A1D5PXA5, ECO:0000269|PubMed:25256292}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:16293632,
ECO:0000269|PubMed:21964574}.
-!- POLYMORPHISM: Genetic variations in TRPV4 determine the sodium
serum level quantitative trait locus 1 (SSQTL1) [MIM:613508]. In
some populations, variant Pro19Ser has been shown to be
significantly associated with hyponatremia defined as serum sodium
concentration below or equal to 135 mEq/L.
-!- DISEASE: Brachyolmia 3 (BCYM3) [MIM:113500]: A form of
brachyolmia, a clinically and genetically heterogeneous skeletal
dysplasia primarily affecting the spine and characterized by a
short trunk, short stature, and platyspondyly. BCYM3 is an
autosomal dominant form with severe scoliosis with or without
kyphosis, and flattened irregular cervical vertebrae.
{ECO:0000269|PubMed:18587396}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spondylometaphyseal dysplasia Kozlowski type (SMDK)
[MIM:184252]: A form of spondylometaphyseal dysplasia, a group of
short stature disorders distinguished by abnormalities in the
vertebrae and the metaphyses of the tubular bones. It is
characterized by postnatal dwarfism, significant scoliosis and
mild metaphyseal abnormalities in the pelvis. The vertebrae
exhibit platyspondyly and overfaced pedicles.
{ECO:0000269|PubMed:19232556, ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:22702953}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Metatropic dysplasia (MTD) [MIM:156530]: A severe
spondyloepimetaphyseal dysplasia characterized by short limbs with
limitation and enlargement of joints and usually severe
kyphoscoliosis. Radiologic features include severe platyspondyly,
severe metaphyseal enlargement and shortening of long bones.
{ECO:0000269|PubMed:19232556, ECO:0000269|PubMed:20425821,
ECO:0000269|PubMed:20577006, ECO:0000269|PubMed:22702953,
ECO:0000269|PubMed:26249260, ECO:0000269|Ref.6}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Neuronopathy, distal hereditary motor, 8 (HMN8)
[MIM:600175]: A clinically variable, neuromuscular disorder
characterized by congenital lower motor neuron disorder restricted
to the lower part of the body. Clinical manifestations include
non-progressive muscular atrophy, thigh muscle atrophy, weak thigh
adductors, weak knee and foot extensors, minimal jaw muscle and
neck flexor weakness, flexion contractures of knees and pes
equinovarus. Tendon reflexes are normal.
{ECO:0000269|PubMed:20037588, ECO:0000269|PubMed:22526352,
ECO:0000269|PubMed:22702953}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Charcot-Marie-Tooth disease 2C (CMT2C) [MIM:606071]: An
axonal form of Charcot-Marie-Tooth disease, a disorder of the
peripheral nervous system, characterized by progressive weakness
and atrophy, initially of the peroneal muscles and later of the
distal muscles of the arms. Charcot-Marie-Tooth disease is
classified in two main groups on the basis of electrophysiologic
properties and histopathology: primary peripheral demyelinating
neuropathies (designated CMT1 when they are dominantly inherited)
and primary peripheral axonal neuropathies (CMT2). Neuropathies of
the CMT2 group are characterized by signs of axonal degeneration
in the absence of obvious myelin alterations, normal or slightly
reduced nerve conduction velocities, and progressive distal muscle
weakness and atrophy. {ECO:0000269|PubMed:20037586,
ECO:0000269|PubMed:20037587, ECO:0000269|PubMed:20037588,
ECO:0000269|PubMed:21115951, ECO:0000269|PubMed:21288981,
ECO:0000269|PubMed:22702953, ECO:0000269|PubMed:25256292}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Scapuloperoneal spinal muscular atrophy (SPSMA)
[MIM:181405]: A clinically variable neuromuscular disorder
characterized by neurogenic scapuloperoneal amyotrophy, laryngeal
palsy, congenital absence of muscles, progressive scapuloperoneal
atrophy and progressive distal weakness and amyotrophy.
{ECO:0000269|PubMed:20037587, ECO:0000269|PubMed:22702953}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Spondyloepiphyseal dysplasia Maroteaux type (SEDM)
[MIM:184095]: A clinically variable spondyloepiphyseal dysplasia
with manifestations limited to the musculoskeletal system.
Clinical features include short stature, brachydactyly,
platyspondyly, short and stubby hands and feet, epiphyseal
hypoplasia of the large joints, and iliac hypoplasia. Intelligence
is normal. {ECO:0000269|PubMed:20503319,
ECO:0000269|PubMed:22702953}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Parastremmatic dwarfism (PSTD) [MIM:168400]: A bone
dysplasia characterized by severe dwarfism, kyphoscoliosis,
distortion and bowing of the extremities, and contractures of the
large joints. Radiographically, the disease is characterized by a
combination of decreased bone density, bowing of the long bones,
platyspondyly and striking irregularities of endochondral
ossification with areas of calcific stippling and streaking in
radiolucent epiphyses, metaphyses and apophyses.
{ECO:0000269|PubMed:20503319}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Digital arthropathy-brachydactyly, familial (FDAB)
[MIM:606835]: A disorder characterized by irregularities in the
proximal articular surfaces of the distal interphalangeal joints
of the hand. Individuals appear normal at birth, with no clinical
or radiographic evidence of a developmental skeletal dysplasia.
The earliest changes appear during the first decade of life. By
adulthood, all interphalangeal, metacarpophalangeal, and
metatarsophalangeal joints are affected by a deforming, painful
osteoarthritis. The remainder of the skeleton is clinically and
radiographically unaffected. {ECO:0000269|PubMed:21964574}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Avascular necrosis of the femoral head, primary 2 (ANFH2)
[MIM:617383]: A disease characterized by mechanical failure of the
subchondral bone, and degeneration of the hip joint. It usually
leads to destruction of the hip joint in the third to fifth decade
of life. The clinical manifestations, such as pain on exertion, a
limping gait, and a discrepancy in leg length, cause considerable
disability. {ECO:0000269|PubMed:27330106}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV4 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF263523; AAG28029.1; -; mRNA.
EMBL; AF258465; AAG16127.1; -; mRNA.
EMBL; AB100308; BAC55864.1; -; mRNA.
EMBL; AB032427; BAB69040.1; -; mRNA.
EMBL; AB073669; BAC06573.1; -; mRNA.
EMBL; AJ296305; CAC82937.1; -; mRNA.
EMBL; DQ059644; AAZ04918.1; -; mRNA.
EMBL; DQ059645; AAZ04919.1; -; mRNA.
EMBL; DQ059646; AAZ04920.1; -; mRNA.
EMBL; CH471054; EAW97879.1; -; Genomic_DNA.
EMBL; BC117426; AAI17427.1; -; mRNA.
EMBL; BC143315; AAI43316.1; -; mRNA.
EMBL; AF279673; AAK69487.1; -; mRNA.
CCDS; CCDS53827.1; -. [Q9HBA0-6]
CCDS; CCDS53828.1; -. [Q9HBA0-4]
CCDS; CCDS53829.1; -. [Q9HBA0-5]
CCDS; CCDS9134.1; -. [Q9HBA0-1]
CCDS; CCDS9135.1; -. [Q9HBA0-2]
RefSeq; NP_001170899.1; NM_001177428.1. [Q9HBA0-4]
RefSeq; NP_001170902.1; NM_001177431.1. [Q9HBA0-5]
RefSeq; NP_001170904.1; NM_001177433.1. [Q9HBA0-6]
RefSeq; NP_067638.3; NM_021625.4. [Q9HBA0-1]
RefSeq; NP_671737.1; NM_147204.2. [Q9HBA0-2]
RefSeq; XP_005253975.1; XM_005253918.1. [Q9HBA0-1]
RefSeq; XP_016875263.1; XM_017019774.1. [Q9HBA0-1]
UniGene; Hs.506713; -.
PDB; 4DX1; X-ray; 2.85 A; A/B=149-397.
PDB; 4DX2; X-ray; 2.95 A; A/B=149-397.
PDBsum; 4DX1; -.
PDBsum; 4DX2; -.
ProteinModelPortal; Q9HBA0; -.
SMR; Q9HBA0; -.
BioGrid; 121883; 12.
CORUM; Q9HBA0; -.
DIP; DIP-35702N; -.
IntAct; Q9HBA0; 8.
MINT; Q9HBA0; -.
STRING; 9606.ENSP00000261740; -.
BindingDB; Q9HBA0; -.
ChEMBL; CHEMBL3119; -.
GuidetoPHARMACOLOGY; 510; -.
iPTMnet; Q9HBA0; -.
PhosphoSitePlus; Q9HBA0; -.
BioMuta; TRPV4; -.
DMDM; 62901470; -.
EPD; Q9HBA0; -.
MaxQB; Q9HBA0; -.
PaxDb; Q9HBA0; -.
PeptideAtlas; Q9HBA0; -.
PRIDE; Q9HBA0; -.
ProteomicsDB; 81511; -.
ProteomicsDB; 81512; -. [Q9HBA0-2]
ProteomicsDB; 81513; -. [Q9HBA0-3]
ProteomicsDB; 81514; -. [Q9HBA0-4]
ProteomicsDB; 81515; -. [Q9HBA0-5]
ProteomicsDB; 81516; -. [Q9HBA0-6]
Ensembl; ENST00000261740; ENSP00000261740; ENSG00000111199. [Q9HBA0-1]
Ensembl; ENST00000418703; ENSP00000406191; ENSG00000111199. [Q9HBA0-1]
Ensembl; ENST00000536838; ENSP00000444336; ENSG00000111199. [Q9HBA0-5]
Ensembl; ENST00000537083; ENSP00000442738; ENSG00000111199. [Q9HBA0-2]
Ensembl; ENST00000541794; ENSP00000442167; ENSG00000111199. [Q9HBA0-4]
Ensembl; ENST00000544971; ENSP00000443611; ENSG00000111199. [Q9HBA0-6]
GeneID; 59341; -.
KEGG; hsa:59341; -.
UCSC; uc001tpg.3; human. [Q9HBA0-1]
CTD; 59341; -.
DisGeNET; 59341; -.
EuPathDB; HostDB:ENSG00000111199.10; -.
GeneCards; TRPV4; -.
GeneReviews; TRPV4; -.
HGNC; HGNC:18083; TRPV4.
HPA; HPA007150; -.
MalaCards; TRPV4; -.
MIM; 113500; phenotype.
MIM; 156530; phenotype.
MIM; 168400; phenotype.
MIM; 181405; phenotype.
MIM; 184095; phenotype.
MIM; 184252; phenotype.
MIM; 600175; phenotype.
MIM; 605427; gene.
MIM; 606071; phenotype.
MIM; 606835; phenotype.
MIM; 613508; phenotype.
MIM; 617383; phenotype.
neXtProt; NX_Q9HBA0; -.
OpenTargets; ENSG00000111199; -.
Orphanet; 93304; Autosomal dominant brachyolmia.
Orphanet; 99937; Autosomal dominant Charcot-Marie-Tooth disease type 2C.
Orphanet; 1216; Autosomal dominant congenital benign spinal muscular atrophy.
Orphanet; 86820; Familial avascular necrosis of femoral head.
Orphanet; 85169; Familial digital arthropathy-brachydactyly.
Orphanet; 2635; Metatropic dysplasia.
Orphanet; 2646; Parastremmatic dwarfism.
Orphanet; 431255; Scapuloperoneal spinal muscular atrophy.
Orphanet; 263482; Spondyloepiphyseal dysplasia, Maroteaux type.
Orphanet; 93314; Spondylometaphyseal dysplasia, Kozlowski type.
PharmGKB; PA38293; -.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
GeneTree; ENSGT00940000158615; -.
HOVERGEN; HBG054085; -.
InParanoid; Q9HBA0; -.
KO; K04973; -.
OMA; LNPCANL; -.
OrthoDB; EOG091G016O; -.
PhylomeDB; Q9HBA0; -.
TreeFam; TF314711; -.
Reactome; R-HSA-3295583; TRP channels.
SignaLink; Q9HBA0; -.
SIGNOR; Q9HBA0; -.
ChiTaRS; TRPV4; human.
GeneWiki; TRPV4; -.
GenomeRNAi; 59341; -.
PRO; PR:Q9HBA0; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111199; Expressed in 125 organ(s), highest expression level in cartilage tissue.
ExpressionAtlas; Q9HBA0; baseline and differential.
Genevisible; Q9HBA0; HS.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005929; C:cilium; IBA:GO_Central.
GO; GO:0030864; C:cortical actin cytoskeleton; ISS:BHF-UCL.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; ISS:BHF-UCL.
GO; GO:0005925; C:focal adhesion; ISS:BHF-UCL.
GO; GO:0030426; C:growth cone; ISS:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:BHF-UCL.
GO; GO:0003779; F:actin binding; ISS:BHF-UCL.
GO; GO:0051015; F:actin filament binding; ISS:BHF-UCL.
GO; GO:0043014; F:alpha-tubulin binding; ISS:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0048487; F:beta-tubulin binding; ISS:BHF-UCL.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IMP:UniProtKB.
GO; GO:0005261; F:cation channel activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
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; ISS:BHF-UCL.
GO; GO:0005034; F:osmosensor activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0005080; F:protein kinase C binding; ISS:BHF-UCL.
GO; GO:0042169; F:SH2 domain binding; ISS:BHF-UCL.
GO; GO:0015275; F:stretch-activated, cation-selective, calcium channel activity; IMP:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:BHF-UCL.
GO; GO:0007015; P:actin filament organization; ISS:BHF-UCL.
GO; GO:0097497; P:blood vessel endothelial cell delamination; IMP:UniProtKB.
GO; GO:0070509; P:calcium ion import; ISS:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:UniProtKB.
GO; GO:0006884; P:cell volume homeostasis; TAS:UniProtKB.
GO; GO:0007043; P:cell-cell junction assembly; ISS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
GO; GO:0071476; P:cellular hypotonic response; IMP:UniProtKB.
GO; GO:0071477; P:cellular hypotonic salinity response; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0071470; P:cellular response to osmotic stress; ISS:UniProtKB.
GO; GO:0043622; P:cortical microtubule organization; ISS:BHF-UCL.
GO; GO:0002024; P:diet induced thermogenesis; IEA:Ensembl.
GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0042538; P:hyperosmotic salinity response; IEA:Ensembl.
GO; GO:0046785; P:microtubule polymerization; ISS:BHF-UCL.
GO; GO:0050891; P:multicellular organismal water homeostasis; IMP:UniProtKB.
GO; GO:1903444; P:negative regulation of brown fat cell differentiation; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0007231; P:osmosensory signaling pathway; ISS:BHF-UCL.
GO; GO:0071651; P:positive regulation of chemokine (C-C motif) ligand 5 production; IEA:Ensembl.
GO; GO:2000340; P:positive regulation of chemokine (C-X-C motif) ligand 1 production; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Ensembl.
GO; GO:0071642; P:positive regulation of macrophage inflammatory protein 1 alpha production; IEA:Ensembl.
GO; GO:0031117; P:positive regulation of microtubule depolymerization; ISS:BHF-UCL.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
GO; GO:0043117; P:positive regulation of vascular permeability; IMP:UniProtKB.
GO; GO:0047484; P:regulation of response to osmotic stress; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; TAS:UniProtKB.
GO; GO:1903759; P:signal transduction involved in regulation of aerobic respiration; IEA:Ensembl.
GO; GO:0030103; P:vasopressin secretion; IEA:Ensembl.
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; 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.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; ATP-binding; Calcium;
Calcium channel; Calcium transport; Calmodulin-binding; Cell junction;
Cell membrane; Cell projection; Charcot-Marie-Tooth disease; Cilium;
Complete proteome; Disease mutation; Dwarfism; Endoplasmic reticulum;
Ion channel; Ion transport; Lipid-binding; Membrane; Metal-binding;
Neurodegeneration; Neuropathy; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 871 Transient receptor potential cation
channel subfamily V member 4.
/FTId=PRO_0000215347.
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:0000244|PDB:4DX2,
ECO:0000269|PubMed:22702953}.
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:0000269|PubMed:12724311,
ECO:0000269|PubMed:18826956}.
MOTIF 679 682 Selectivity filter.
{ECO:0000250|UniProtKB:O35433}.
METAL 682 682 Calcium; shared with neighboring
subunits. {ECO:0000250|UniProtKB:Q9R186}.
BINDING 192 192 ATP. {ECO:0000244|PDB:4DX2,
ECO:0000269|PubMed:22702953}.
BINDING 197 197 ATP. {ECO:0000244|PDB:4DX2,
ECO:0000269|PubMed:22702953}.
BINDING 201 201 ATP. {ECO:0000244|PDB:4DX2,
ECO:0000269|PubMed:22702953}.
BINDING 248 248 ATP. {ECO:0000244|PDB:4DX2,
ECO:0000269|PubMed:22702953}.
BINDING 344 344 Phosphatidylinositol-1,4,5-trisphosphate.
{ECO:0000250|UniProtKB:A0A1D5PXA5}.
MOD_RES 110 110 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9EPK8}.
MOD_RES 253 253 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9EPK8}.
MOD_RES 805 805 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9EPK8}.
MOD_RES 824 824 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPK8}.
VAR_SEQ 28 61 Missing (in isoform 5).
{ECO:0000303|PubMed:16293632}.
/FTId=VSP_026614.
VAR_SEQ 239 285 Missing (in isoform 4 and isoform 6).
{ECO:0000303|PubMed:16293632}.
/FTId=VSP_026615.
VAR_SEQ 385 444 Missing (in isoform 2 and isoform 6).
{ECO:0000303|PubMed:16293632,
ECO:0000303|Ref.6}.
/FTId=VSP_013436.
VAR_SEQ 844 871 PLDSMGNPRCDGHQQGYPRKWRTDDAPL -> RHLCRVRRK
R (in isoform 3).
{ECO:0000303|PubMed:12692122}.
/FTId=VSP_013437.
VARIANT 19 19 P -> S (associated with lower sodium
concentrations in serum; shows diminished
response to hypotonic stress relative to
wild-type; dbSNP:rs3742030).
/FTId=VAR_052391.
VARIANT 89 89 T -> I (in MTD; lethal form;
dbSNP:rs397514473).
{ECO:0000269|PubMed:20425821}.
/FTId=VAR_064517.
VARIANT 97 97 P -> R (in HMN8; loss of function
mutation; dbSNP:rs876661124).
{ECO:0000269|PubMed:22526352}.
/FTId=VAR_067989.
VARIANT 183 183 E -> K (found in a patient with
spondyloepiphyseal dysplasia Maroteaux
type; decreased protein stability;
increased ATP-binding;
dbSNP:rs387906324).
{ECO:0000269|PubMed:20503319,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064518.
VARIANT 197 197 K -> R (in MTD; lethal form; decreased
protein stability; reduced ATP-binding;
dbSNP:rs387906903).
{ECO:0000269|PubMed:20425821,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064519.
VARIANT 199 199 L -> F (in MTD; decreased protein
stability; dbSNP:rs515726167).
{ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064520.
VARIANT 232 232 R -> C (in HMN8 and CMT2C; does not
affect channel localization to plasma
membrane; results in increased agonist-
induced channel activity and increased
basal intracellular calcium
concentration; decreases ATP-binding; no
effect on protein stability; decreases
binding to membranes enriched in
phosphatidylinositol-2,4-bisphosphate;
causes increased cell death;
dbSNP:rs387906904).
{ECO:0000269|PubMed:21288981,
ECO:0000269|PubMed:22526352,
ECO:0000269|PubMed:22702953,
ECO:0000269|PubMed:25256292}.
/FTId=VAR_067990.
VARIANT 269 269 R -> C (in CMT2C; increased agonist-
induced channel activity; causes
increased cell death; no effect on
protein stability and ATP-binding;
dbSNP:rs267607146).
{ECO:0000269|PubMed:20037586,
ECO:0000269|PubMed:21288981,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_063528.
VARIANT 269 269 R -> H (in HMN8 and CMT2C; increased
agonist-induced channel activity and
increased basal intracellular calcium
concentration; slightly decreased protein
stability and ATP-binding; decreases
binding to membranes enriched in
phosphatidylinositol-2,4-bisphosphate;
causes increased cell death;
dbSNP:rs267607144).
{ECO:0000269|PubMed:20037586,
ECO:0000269|PubMed:20037587,
ECO:0000269|PubMed:20037588,
ECO:0000269|PubMed:21288981,
ECO:0000269|PubMed:22702953,
ECO:0000269|PubMed:25256292}.
/FTId=VAR_063529.
VARIANT 270 270 G -> V (in FDAB; poorly expressed on the
cell surface; mutant channels show a
significantly reduced response to
agonists; dbSNP:rs387907220).
{ECO:0000269|PubMed:21964574}.
/FTId=VAR_068498.
VARIANT 271 271 R -> P (in FDAB; poorly expressed on the
cell surface; mutant channels show a
significantly reduced response to
agonists; dbSNP:rs387907219).
{ECO:0000269|PubMed:21964574}.
/FTId=VAR_068499.
VARIANT 273 273 F -> L (in FDAB; poorly expressed on the
cell surface; mutant channels show a
significantly reduced response to
agonists; dbSNP:rs515726170).
{ECO:0000269|PubMed:21964574}.
/FTId=VAR_068500.
VARIANT 278 278 E -> K (in SMDK; slightly increased ATP-
binding; slightly decreased protein
stability; dbSNP:rs267607148).
{ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064521.
VARIANT 295 295 T -> A (in MTD; impairs protein folding
or stability; dbSNP:rs515726171).
{ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064522.
VARIANT 315 315 R -> W (in CMT2C; increased basal and
agonist-induced channel activity,
decreased protein stability; decreased
ATP-binding; decreases binding to
membranes enriched in
phosphatidylinositol-2,4-bisphosphate;
causes increased cell death;
dbSNP:rs267607143).
{ECO:0000269|PubMed:20037588,
ECO:0000269|PubMed:21115951,
ECO:0000269|PubMed:22702953,
ECO:0000269|PubMed:25256292}.
/FTId=VAR_063541.
VARIANT 316 316 R -> C (in CMT2C and SPSMA; decreased
protein stability; decreased ATP-binding;
dbSNP:rs267607145).
{ECO:0000269|PubMed:20037587,
ECO:0000269|PubMed:20037588}.
/FTId=VAR_063530.
VARIANT 316 316 R -> H (in CMT2C; does not affect channel
localization to plasma membrane; results
in increased agonist-induced channel
activity and increased basal
intracellular calcium concentration;
decreases protein stability; causes
increased cell death; dbSNP:rs387906905).
{ECO:0000269|PubMed:21288981,
ECO:0000269|PubMed:25256292}.
/FTId=VAR_067991.
VARIANT 331 331 I -> F (in MTD; decreased protein
stability; no effect on ATP-binding;
dbSNP:rs121912636).
{ECO:0000269|PubMed:19232556,
ECO:0000269|PubMed:20425821,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_062331.
VARIANT 331 331 I -> T (in MTD; no effect on protein
stability; no effect on ATP-binding;
dbSNP:rs515726172).
{ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064523.
VARIANT 333 336 Missing (in SMDK).
/FTId=VAR_067992.
VARIANT 333 333 D -> G (in SMDK; decreased protein
stability; no effect on ATP-binding;
dbSNP:rs121912634).
{ECO:0000269|PubMed:19232556,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_062332.
VARIANT 342 342 V -> F (in MTD; decreased protein
stability; decreased ATP-binding;
dbSNP:rs515726152).
{ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:22702953}.
/FTId=VAR_064524.
VARIANT 471 471 Missing (in MTD; lethal form).
{ECO:0000269|PubMed:20425821,
ECO:0000269|PubMed:20577006}.
/FTId=VAR_064525.
VARIANT 542 542 S -> Y (in CMT2C; dbSNP:rs387906902).
{ECO:0000269|PubMed:21115951}.
/FTId=VAR_067993.
VARIANT 592 592 F -> L (in MTD; dbSNP:rs515726158).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064526.
VARIANT 594 594 R -> H (in SMDK and PSTD;
dbSNP:rs77975504).
{ECO:0000269|PubMed:19232556,
ECO:0000269|PubMed:20503319,
ECO:0000269|PubMed:20577006}.
/FTId=VAR_062333.
VARIANT 596 596 L -> P (in SMDK; dbSNP:rs515726159).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064527.
VARIANT 600 600 G -> W (in SMDK; dbSNP:rs515726160).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064528.
VARIANT 602 602 Y -> C (found in a patient with
spondyloepiphyseal dysplasia Maroteaux
type; dbSNP:rs267607150).
{ECO:0000269|PubMed:20503319}.
/FTId=VAR_064529.
VARIANT 604 604 I -> M (in MTD; lethal form;
dbSNP:rs515726161).
{ECO:0000269|PubMed:20425821}.
/FTId=VAR_064530.
VARIANT 616 616 R -> Q (in BCYM3; results in a gain of
function and a constitutive activation of
the channel; dbSNP:rs121912632).
{ECO:0000269|PubMed:18587396}.
/FTId=VAR_054805.
VARIANT 617 617 F -> L (in MTD; dbSNP:rs515726162).
{ECO:0000269|PubMed:20425821}.
/FTId=VAR_064531.
VARIANT 618 618 L -> P (in MTD; dbSNP:rs515726163).
{ECO:0000269|PubMed:20425821,
ECO:0000269|Ref.6}.
/FTId=VAR_064532.
VARIANT 620 620 V -> I (in BCYM3; results in a gain of
function and a constitutive activation of
the channel; dbSNP:rs121912633).
{ECO:0000269|PubMed:18587396}.
/FTId=VAR_054806.
VARIANT 625 625 M -> I (in SMDK; dbSNP:rs515726164).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064533.
VARIANT 709 709 L -> M (in SMDK; dbSNP:rs116571438).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064534.
VARIANT 716 716 A -> S (in SMDK; dbSNP:rs121912635).
{ECO:0000269|PubMed:19232556}.
/FTId=VAR_062334.
VARIANT 775 775 R -> K (in MTD).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064535.
VARIANT 777 777 C -> Y (in SMDK; dbSNP:rs515726165).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064536.
VARIANT 797 797 E -> K (in MTD and SMDK; also found in a
patient with spondyloepiphyseal dysplasia
Maroteaux type; dbSNP:rs267607149).
{ECO:0000269|PubMed:20425821,
ECO:0000269|PubMed:20503319,
ECO:0000269|PubMed:20577006}.
/FTId=VAR_064537.
VARIANT 799 799 P -> A (in MTD; dbSNP:rs267607147).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064538.
VARIANT 799 799 P -> L (in MTD; also found in a patient
with spondyloepiphyseal dysplasia
Maroteaux type; dbSNP:rs121912637).
{ECO:0000269|PubMed:19232556,
ECO:0000269|PubMed:20425821,
ECO:0000269|PubMed:20503319,
ECO:0000269|PubMed:20577006,
ECO:0000269|PubMed:26249260}.
/FTId=VAR_062335.
VARIANT 799 799 P -> R (in MTD; dbSNP:rs121912637).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064539.
VARIANT 799 799 P -> S (in MTD; dbSNP:rs267607147).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064540.
MUTAGEN 231 231 F->C: Decreased ATP-binding.
{ECO:0000269|PubMed:22702953}.
MUTAGEN 251 251 K->E: No effect on channel activity. No
effect on interaction with membranes
enriched in phosphatidylinositol-2,4-
bisphosphate.
{ECO:0000269|PubMed:25256292}.
MUTAGEN 296 296 N->D: Loss of interaction with membranes
enriched in phosphatidylinositol-2,4-
bisphosphate; when associated with P-299.
{ECO:0000269|PubMed:25256292}.
MUTAGEN 299 299 H->P: Strongly decreased interaction with
membranes enriched in
phosphatidylinositol-2,4-bisphosphate.
Loss of interaction with membranes
enriched in phosphatidylinositol-2,4-
bisphosphate; when associated with D-296.
{ECO:0000269|PubMed:25256292}.
MUTAGEN 344 344 K->E: No effect on channel activity. No
effect on interaction with membranes
enriched in phosphatidylinositol-2,4-
bisphosphate.
{ECO:0000269|PubMed:25256292}.
MUTAGEN 816 821 RLRRDR->ELEEDE: Loss of calmodulin
binding; when associated with A-828.
MUTAGEN 821 824 RWSS->AASA: Loss of calmodulin binding.
MUTAGEN 822 822 W->A: Loss of Ca(2+) dependent current
potentiation.
MUTAGEN 828 828 R->A: Loss of calmodulin binding; when
associated with 816-ELEEDE-821.
{ECO:0000269|PubMed:12724311}.
CONFLICT 385 385 I -> V (in Ref. 1; AAG28029).
{ECO:0000305}.
CONFLICT 452 452 V -> A (in Ref. 6; BAC06573).
{ECO:0000305}.
CONFLICT 781 781 D -> N (in Ref. 1; AAG28029).
{ECO:0000305}.
CONFLICT 820 820 D -> T (in Ref. 4; BAB69040).
{ECO:0000305}.
CONFLICT 861 861 P -> T (in Ref. 6; BAC06573).
{ECO:0000305}.
CONFLICT 867 867 D -> E (in Ref. 2; AAG16127).
{ECO:0000305}.
HELIX 151 159 {ECO:0000244|PDB:4DX1}.
HELIX 164 166 {ECO:0000244|PDB:4DX1}.
HELIX 169 175 {ECO:0000244|PDB:4DX1}.
HELIX 183 185 {ECO:0000244|PDB:4DX1}.
STRAND 188 190 {ECO:0000244|PDB:4DX1}.
HELIX 194 200 {ECO:0000244|PDB:4DX1}.
HELIX 209 220 {ECO:0000244|PDB:4DX1}.
HELIX 223 228 {ECO:0000244|PDB:4DX1}.
STRAND 234 239 {ECO:0000244|PDB:4DX1}.
HELIX 241 247 {ECO:0000244|PDB:4DX1}.
HELIX 251 260 {ECO:0000244|PDB:4DX1}.
HELIX 271 273 {ECO:0000244|PDB:4DX2}.
TURN 276 279 {ECO:0000244|PDB:4DX1}.
HELIX 288 294 {ECO:0000244|PDB:4DX1}.
HELIX 298 306 {ECO:0000244|PDB:4DX1}.
HELIX 324 331 {ECO:0000244|PDB:4DX1}.
HELIX 336 356 {ECO:0000244|PDB:4DX1}.
STRAND 357 360 {ECO:0000244|PDB:4DX1}.
HELIX 362 364 {ECO:0000244|PDB:4DX2}.
HELIX 373 379 {ECO:0000244|PDB:4DX1}.
HELIX 383 395 {ECO:0000244|PDB:4DX1}.
SEQUENCE 871 AA; 98281 MW; C62056B86C5A6FB6 CRC64;
MADSSEGPRA GPGEVAELPG DESGTPGGEA FPLSSLANLF EGEDGSLSPS PADASRPAGP
GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHSSDN
KRWRKKIIEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL PFLLTHKKRL
TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT
ALHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCARLFPDS
NLEAVLNNDG LSPLMMAAKT GKIGIFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD
LSSLDTCGEE ASVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC
AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLFT GVLFFFTNIK DLFMKKCPGV
NSLFIDGSFQ LLYFIYSVLV IVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVSLLNPCA NMKVCNEDQT NCTVPTYPSC
RDSETFSTFL LDLFKLTIGM GDLEMLSSTK YPVVFIILLV TYIILTFVLL LNMLIALMGE
TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV
DEVNWSHWNQ NLGIINEDPG KNETYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSNPDE
VVVPLDSMGN PRCDGHQQGY PRKWRTDDAP L


Related products :

Catalog number Product name Quantity
EIAAB44125 Osm-9-like TRP channel 4,OTRPC4,Rat,Rattus norvegicus,Transient receptor potential cation channel subfamily V member 4,TrpV4,Trpv4,Vanilloid receptor-related osmotically-activated channel,Vroac,VR-OAC
EIAAB44124 Homo sapiens,Human,Osm-9-like TRP channel 4,OTRPC4,Transient receptor potential cation channel subfamily V member 4,Transient receptor potential protein 12,TRP12,TrpV4,TRPV4,Vanilloid receptor-like ch
EIAAB44123 Mouse,Mus musculus,Osm-9-like TRP channel 4,OTRPC4,Transient receptor potential cation channel subfamily V member 4,Transient receptor potential protein 12,TRP12,Trp12,TrpV4,Trpv4,Vanilloid receptor-l
EIAAB44113 Capsaicin receptor,Osm-9-like TRP channel 1,OTRPC1,Rat,Rattus norvegicus,Transient receptor potential cation channel subfamily V member 1,TrpV1,Trpv1,Vanilloid receptor 1,Vanilloid receptor type 1-lik
EIAAB44120 Osm-9-like TRP channel 2,OTRPC2,Rat,Rattus norvegicus,Sac2b,Stretch-activated channel 2B,Transient receptor potential cation channel subfamily V member 2,TrpV2,Trpv2,Vanilloid receptor-like protein 1,
EIAAB44119 Homo sapiens,Human,Osm-9-like TRP channel 2,OTRPC2,Transient receptor potential cation channel subfamily V member 2,TrpV2,TRPV2,Vanilloid receptor-like protein 1,VRL,VRL-1
18-783-75531 RABBIT ANTI Trpv2 (N-TERMINAL) - TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL. SUBFAMILY V. MEMBER 2; TrpV2; osm-9-like TRP channel 2; OTRPC2; Vanilloid receptor-like protein 1; VRL-1 Polyclonal 0.05 mg
EIAAB44117 Capsaicin receptor,Homo sapiens,Human,Osm-9-like TRP channel 1,OTRPC1,Transient receptor potential cation channel subfamily V member 1,TrpV1,TRPV1,Vanilloid receptor 1,VR1
EIAAB44114 Mouse,Mus musculus,Osm-9-like TRP channel 1,OTRPC1,Transient receptor potential cation channel subfamily V member 1,TrpV1,Trpv1,Vanilloid receptor 1
EIAAB44115 Oryctolagus cuniculus,Osm-9-like TRP channel 1,OTRPC1,Rabbit,Transient receptor potential cation channel subfamily V member 1,TrpV1,Trpv1,Vanilloid receptor 1
EIAAB44104 Chak,Channel-kinase 1,Long transient receptor potential channel 7,LTrpC7,Ltrpc7,LTrpC-7,Mouse,Mus musculus,Transient receptor potential cation channel subfamily M member 7,Transient receptor potential
EIAAB44103 Long transient receptor potential channel 7,LTrpC7,LTrpC-7,Rat,Rattus norvegicus,Transient receptor potential cation channel subfamily M member 7,Transient receptor potential-phospholipase C-interacti
EIAAB44095 Calcium-activated non-selective cation channel 1,Long transient receptor potential channel 4,LTrpC4,Ltrpc4,LTrpC-4,Mouse,Mus musculus,Transient receptor potential cation channel subfamily M member 4,T
EIAAB44099 Long transient receptor potential channel 5,LTrpC5,Ltrpc5,LTrpC-5,MLSN1- and TRP-related gene 1 protein,Mouse,Mtr1,Mus musculus,Transient receptor potential cation channel subfamily M member 5,Trpm5
EIAAB44098 Homo sapiens,Human,Long transient receptor potential channel 5,LTrpC5,LTRPC5,LTrpC-5,MLSN1- and TRP-related gene 1 protein,MTR1,Transient receptor potential cation channel subfamily M member 5,TRPM5
EIAAB44106 Homo sapiens,Human,Long transient receptor potential channel 6,LTrpC6,LTRPC6,LTrpC-6,Transient receptor potential cation channel subfamily M member 8,Transient receptor potential p8,TRPM8,TRPP8,Trp-p8
18-001-30066 Transient receptor potential cation channel subfamily M member 8 - Transient receptor potential-p8; Trp-p8; Long transient receptor potential channel 6; LTrpC6 Polyclonal 0.1 mg
EIAAB44121 Homo sapiens,Human,Transient receptor potential cation channel subfamily V member 3,TrpV3,TRPV3,Vanilloid receptor-like 3,VRL-3
EIAAB44105 Long transient receptor potential channel 6,LTrpC6,Ltrpc6,LTrpC-6,Mouse,Mus musculus,Transient receptor potential cation channel subfamily M member 8,Transient receptor potential p8,Trpm8,Trpp8,Trp-p8
EIAAB44092 Long transient receptor potential channel 2,LTrpC2,Ltrpc2,LTrpC-2,Mouse,Mus musculus,Transient receptor potential cation channel subfamily M member 2,Transient receptor potential channel 7,TrpC7,Trpc7
EIAAB44116 Canis familiaris,Canis lupus familiaris,Dog,Osm-9-like TRP channel 1,OTRPC1,Transient receptor potential cation channel subfamily V member 1,TrpV1,TRPV1,Vanilloid receptor 1
EIAAB44102 CHAK1,Channel-kinase 1,Homo sapiens,Human,Long transient receptor potential channel 7,LTrpC7,LTRPC7,LTrpC-7,Transient receptor potential cation channel subfamily M member 7,TRPM7
EIAAB44096 Calcium-activated non-selective cation channel 1,Homo sapiens,hTRPM4,Human,Long transient receptor potential channel 4,LTrpC4,LTRPC4,LTrpC-4,Melastatin-4,Transient receptor potential cation channel su
EIAAB44100 Channel kinase 2,Melastatin-related TRP cation channel 6,Mouse,Mus musculus,Transient receptor potential cation channel subfamily M member 6,Trpm6
EIAAB44101 CHAK2,Channel kinase 2,Homo sapiens,Human,Melastatin-related TRP cation channel 6,Transient receptor potential cation channel subfamily M member 6,TRPM6


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur