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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) (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.
25-OCT-2017, entry version 151.
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;
Short=VRL-2;
AltName: Full=Vanilloid receptor-related osmotically-activated channel;
Short=VR-OAC;
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), SUBCELLULAR
LOCATION, AND SELF-ASSOCIATION.
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, 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).
[18]
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 149-397 ALONE AND IN COMPLEX
WITH ATP.
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
VARIANTS CMT2C CYS-269 AND HIS-269.
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).
[28]
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).
[29]
VARIANTS FDAB VAL-270; PRO-271 AND LEU-273, AND CHARACTERIZATION OF
VARIANTS FDAB VAL-270; PRO-271 AND LEU-273.
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).
[30]
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).
[31]
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:18826956, PubMed:18695040). 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:18695040, ECO:0000269|PubMed:18826956,
ECO:0000269|PubMed:19759329, ECO:0000269|PubMed:26249260}.
-!- SUBUNIT: Homotetramer (Probable). Self-associates in a isoform-
specific manner (PubMed:16293632). Isoforms 1/A and 5/D but not
isoform 2/B, 4/C and 6/E can 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. 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.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane.
-!- 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;
Name=3; Synonyms=TRPV-SV;
IsoId=Q9HBA0-3; Sequence=VSP_013437;
Name=4; Synonyms=C;
IsoId=Q9HBA0-4; Sequence=VSP_026615;
Name=5; Synonyms=D;
IsoId=Q9HBA0-5; Sequence=VSP_026614;
Name=6; Synonyms=E;
IsoId=Q9HBA0-6; Sequence=VSP_026615, VSP_013436;
-!- TISSUE SPECIFICITY: Found in the synoviocytes from patients with
(RA) and without (CTR) rheumatoid arthritis (at protein level).
{ECO:0000269|PubMed:19759329}.
-!- 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}.
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: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}.
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. Nerve conduction velocities are normal or
slightly reduced. {ECO:0000269|PubMed:20037586,
ECO:0000269|PubMed:20037587, ECO:0000269|PubMed:20037588,
ECO:0000269|PubMed:21115951, ECO:0000269|PubMed:21288981}.
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}. 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}. 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}.
-----------------------------------------------------------------------
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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; MINT-4535111; -.
STRING; 9606.ENSP00000261740; -.
BindingDB; Q9HBA0; -.
ChEMBL; CHEMBL3119; -.
GuidetoPHARMACOLOGY; 510; -.
iPTMnet; Q9HBA0; -.
PhosphoSitePlus; Q9HBA0; -.
BioMuta; TRPV4; -.
DMDM; 62901470; -.
MaxQB; Q9HBA0; -.
PaxDb; Q9HBA0; -.
PeptideAtlas; Q9HBA0; -.
PRIDE; Q9HBA0; -.
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; 85169; Familial digital arthropathy-brachydactyly.
Orphanet; 2635; Metatropic dysplasia.
Orphanet; 2646; Parastremmatic dwarfism.
Orphanet; 263482; Spondyloepiphyseal dysplasia, Maroteaux type.
Orphanet; 93314; Spondylometaphyseal dysplasia, Kozlowski type.
PharmGKB; PA38293; -.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
GeneTree; ENSGT00550000074425; -.
HOVERGEN; HBG054085; -.
InParanoid; Q9HBA0; -.
KO; K04973; -.
OMA; KVCNEDQ; -.
OrthoDB; EOG091G016O; -.
PhylomeDB; Q9HBA0; -.
TreeFam; TF314711; -.
Reactome; R-HSA-3295583; TRP channels.
SignaLink; Q9HBA0; -.
SIGNOR; Q9HBA0; -.
GeneWiki; TRPV4; -.
GenomeRNAi; 59341; -.
PRO; PR:Q9HBA0; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111199; -.
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: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: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: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 from RNA polymerase II promoter; 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:2000507; P:positive regulation of energy homeostasis; IEA:Ensembl.
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; -; 2.
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;
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; Ion channel;
Ion transport; Membrane; 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 1 465 Cytoplasmic. {ECO:0000255}.
TRANSMEM 466 486 Helical. {ECO:0000255}.
TOPO_DOM 487 508 Extracellular. {ECO:0000255}.
TRANSMEM 509 529 Helical. {ECO:0000255}.
TOPO_DOM 530 550 Cytoplasmic. {ECO:0000255}.
TRANSMEM 551 571 Helical. {ECO:0000255}.
TOPO_DOM 572 572 Extracellular. {ECO:0000255}.
TRANSMEM 573 593 Helical. {ECO:0000255}.
TOPO_DOM 594 616 Cytoplasmic. {ECO:0000255}.
TRANSMEM 617 637 Helical. {ECO:0000255}.
INTRAMEM 648 678 Pore-forming. {ECO:0000305}.
TRANSMEM 691 711 Helical. {ECO:0000255}.
TOPO_DOM 712 871 Cytoplasmic. {ECO:0000255}.
REPEAT 237 266 ANK 1.
REPEAT 284 313 ANK 2.
REPEAT 369 398 ANK 3.
REGION 812 831 Interaction with calmodulin and ITPR3.
{ECO:0000269|PubMed:12724311,
ECO:0000269|PubMed:18826956}.
BINDING 192 192 ATP. {ECO:0000269|PubMed:22702953}.
BINDING 201 201 ATP. {ECO:0000269|PubMed:22702953}.
BINDING 239 239 ATP. {ECO:0000269|PubMed:22702953}.
BINDING 248 248 ATP. {ECO:0000269|PubMed:22702953}.
MOD_RES 110 110 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
concentraions 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; dbSNP:rs387906324).
{ECO:0000269|PubMed:20503319}.
/FTId=VAR_064518.
VARIANT 197 197 K -> R (in MTD; lethal form;
dbSNP:rs387906903).
{ECO:0000269|PubMed:20425821}.
/FTId=VAR_064519.
VARIANT 199 199 L -> F (in MTD; dbSNP:rs515726167).
{ECO:0000269|PubMed:20577006}.
/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; causes increased cell
death; dbSNP:rs387906904).
{ECO:0000269|PubMed:21288981,
ECO:0000269|PubMed:22526352}.
/FTId=VAR_067990.
VARIANT 269 269 R -> C (in CMT2C; dbSNP:rs267607146).
{ECO:0000269|PubMed:20037586,
ECO:0000269|PubMed:21288981}.
/FTId=VAR_063528.
VARIANT 269 269 R -> H (in HMN8 and CMT2C; increased
agonist-induced channel activity and
increased basal intracellular calcium
concentration; causes increased cell
death; dbSNP:rs267607144).
{ECO:0000269|PubMed:20037586,
ECO:0000269|PubMed:20037587,
ECO:0000269|PubMed:20037588,
ECO:0000269|PubMed:21288981}.
/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; dbSNP:rs267607148).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064521.
VARIANT 295 295 T -> A (in MTD; dbSNP:rs515726171).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064522.
VARIANT 315 315 R -> W (in CMT2C; dbSNP:rs267607143).
{ECO:0000269|PubMed:20037588,
ECO:0000269|PubMed:21115951}.
/FTId=VAR_063541.
VARIANT 316 316 R -> C (in CMT2C and SPSMA;
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;
causes increased cell death;
dbSNP:rs387906905).
{ECO:0000269|PubMed:21288981}.
/FTId=VAR_067991.
VARIANT 331 331 I -> F (in MTD; dbSNP:rs121912636).
{ECO:0000269|PubMed:19232556,
ECO:0000269|PubMed:20425821}.
/FTId=VAR_062331.
VARIANT 331 331 I -> T (in MTD; dbSNP:rs515726172).
{ECO:0000269|PubMed:20577006}.
/FTId=VAR_064523.
VARIANT 333 336 Missing (in SMDK).
/FTId=VAR_067992.
VARIANT 333 333 D -> G (in SMDK; dbSNP:rs121912634).
{ECO:0000269|PubMed:19232556}.
/FTId=VAR_062332.
VARIANT 342 342 V -> F (in MTD; dbSNP:rs515726152).
{ECO:0000269|PubMed:20577006}.
/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; this mutation 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; this mutation 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 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


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