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Q9WTR1 (TRPV2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transient receptor potential cation channel subfamily V member 2

Short name=TrpV2
Alternative name(s):
Growth factor-regulated calcium channel
Short name=GRC
Osm-9-like TRP channel 2
Short name=OTRPC2
Gene names
Name:Trpv2
Synonyms:Grc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH. Ref.1 Ref.5

Subunit structure

Homotetramer Probable. Interacts with a cAMP-dependent protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and ACBD3. Interacts with SLC50A1; the interaction probably occurs intracellularly and depends on TRPV2 N-glycosylation By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Cytoplasm. Melanosome By similarity. Note: Translocates from the cytoplasm to the plasma membrane upon ligand stimulation. Ref.1 Ref.5

Tissue specificity

Abundantly expressed in spleen, placenta, skeleton muscle, lung and brain. Ref.1

Post-translational modification

N-glycosylated. Ref.1

Phosphorylated by PKA By similarity.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV2 sub-subfamily. [View classification]

Contains 6 ANK repeats.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainANK repeat
Repeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of axon extension

Inferred from mutant phenotype PubMed 20357111. Source: DFLAT

positive regulation of calcium ion import

Inferred from mutant phenotype PubMed 20357111. Source: DFLAT

response to heat

Inferred from electronic annotation. Source: Ensembl

response to temperature stimulus

Inferred from sequence orthology PubMed 10201375. Source: MGI

   Cellular_componentaxon

Inferred from direct assay PubMed 20357111. Source: DFLAT

axonal growth cone

Inferred from direct assay PubMed 20357111. Source: DFLAT

cell body

Inferred from direct assay PubMed 20357111. Source: DFLAT

cell surface

Inferred from direct assay PubMed 20357111. Source: DFLAT

endomembrane system

Inferred from electronic annotation. Source: Ensembl

growth cone membrane

Inferred from direct assay PubMed 20357111. Source: DFLAT

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay Ref.1. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functioncalcium channel activity

Inferred from direct assay Ref.1. Source: MGI

cation channel activity

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756Transient receptor potential cation channel subfamily V member 2
PRO_0000215343

Regions

Topological domain1 – 387387Cytoplasmic Potential
Transmembrane388 – 40821Helical; Potential
Topological domain409 – 42820Extracellular Potential
Transmembrane429 – 44921Helical; Potential
Topological domain450 – 4556Cytoplasmic Potential
Transmembrane456 – 47621Helical; Potential
Topological domain477 – 49014Extracellular Potential
Transmembrane491 – 51121Helical; Potential
Topological domain512 – 53221Cytoplasmic Potential
Transmembrane533 – 55321Helical; Potential
Intramembrane568 – 60437Pore-forming; Potential
Transmembrane617 – 63721Helical; Potential
Topological domain638 – 756119Cytoplasmic Potential
Repeat68 – 11043ANK 1
Repeat111 – 15747ANK 2
Repeat158 – 20346ANK 3
Repeat204 – 23936ANK 4
Repeat240 – 28849ANK 5
Repeat289 – 31527ANK 6
Region1 – 385385Required for interaction with SLC50A1 By similarity

Amino acid modifications

Modified residue151Phosphoserine Ref.6
Modified residue7551Phosphoserine Ref.6
Glycosylation5671N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict5651D → N in BAA78478. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9WTR1 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: C0E537AB2C86E1A8

FASTA75685,965
        10         20         30         40         50         60 
MTSASNPPAF RLETSDGDEE GSAEVNKGKN EPPPMESPFQ GEDRNFSPQI KVNLNYRKGL 

        70         80         90        100        110        120 
GPSQQDPNRF DRDRLFSVVS RGVPEELTGL LEYLRRTSKY LTDSAYTEGS TGKTCLMKAV 

       130        140        150        160        170        180 
LNLQDGVNAC ILPLLQIDRD SGNPQPLVNA QCTDEFYRGH SALHIAIEKR SLWCVKLLVE 

       190        200        210        220        230        240 
NGANVHIRAC GRFFQKHQGT CFYFGELPLS LAACTKQWDV VTYLLENPHQ PASLEATDSL 

       250        260        270        280        290        300 
GNTVLHALVM IADNSPENSA LVIHMYDSLL QMGARLCPTV QLEDICNHQG LTPLKLAAKE 

       310        320        330        340        350        360 
GKIEIFRHIL QREFSGLYQP LSRKFTEWCY GPVRVSLYDL SSVDSWEKNS VLEIIAFHCK 

       370        380        390        400        410        420 
SPHRHRMVVL EPLNKLLQEK WDRLIPRFFF NFACYLVYMI IFTIVAYHQP SLEQPAIPSS 

       430        440        450        460        470        480 
KATFGDSMLL LGHILILLGG IYLLLGQLWY FWRRRLFIWI SFMDSYFEIL FLVQALLTVL 

       490        500        510        520        530        540 
SQVLRFVETE WYLPLLVSSL VLGWLNLLYY TRGFQHTGIY SVMIQKVILR DLLRFLLVYL 

       550        560        570        580        590        600 
VFLFGFAVAL VSLSREARSP KAPEDSNTTV TEKPTLGQEE EPVPYGGILD ASLELFKFTI 

       610        620        630        640        650        660 
GMGELAFQEQ LRFRGVVLLL LLAYVLLTYV LLLNMLIALM SETVNSVATD SWSIWKLQKA 

       670        680        690        700        710        720 
ISVLEMENGY WWCRRKRHRA GRLLKVGTKG DGIPDERWCF RVEEVNWAAW EKTLPTLSED 

       730        740        750 
PSGAGITGYK KNPTSKPGKN SASEEDHLPL QVLQSH 

« Hide

References

« Hide 'large scale' references
[1]"Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I."
Kanzaki M., Zhang Y.-Q., Mashima H., Li L., Shibata H., Kojima I.
Nat. Cell Biol. 1:165-170(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
Strain: C57BL/6.
Tissue: Spleen.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"The neuropeptide head activator induces activation and translocation of the growth-factor-regulated Ca(2+)-permeable channel GRC."
Boels K., Glassmeier G., Herrmann D., Riedel I.B., Hampe W., Kojima I., Schwarz J.R., Schaller H.C.
J. Cell Sci. 114:3599-3606(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB021665 mRNA. Translation: BAA78478.1.
AK089004 mRNA. Translation: BAC40695.1.
AL596181 Genomic DNA. Translation: CAI24670.1.
BC005415 mRNA. Translation: AAH05415.1.
CCDSCCDS24827.1.
RefSeqNP_035836.2. NM_011706.2.
XP_006533228.1. XM_006533165.1.
UniGeneMm.288064.

3D structure databases

ProteinModelPortalQ9WTR1.
SMRQ9WTR1. Positions 70-676.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY508.

Protein family/group databases

TCDB1.A.4.2.4. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteQ9WTR1.

Proteomic databases

PaxDbQ9WTR1.
PRIDEQ9WTR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018651; ENSMUSP00000018651; ENSMUSG00000018507.
ENSMUST00000102643; ENSMUSP00000099703; ENSMUSG00000018507.
GeneID22368.
KEGGmmu:22368.
UCSCuc007jjh.1. mouse.

Organism-specific databases

CTD51393.
MGIMGI:1341836. Trpv2.

Phylogenomic databases

eggNOGNOG281194.
GeneTreeENSGT00550000074425.
HOGENOMHOG000234630.
HOVERGENHBG054085.
InParanoidQ9WTR1.
KOK04971.
OMALSQVLCF.
OrthoDBEOG7V49XW.
PhylomeDBQ9WTR1.
TreeFamTF314711.

Gene expression databases

BgeeQ9WTR1.
GenevestigatorQ9WTR1.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERPTHR10582:SF5. PTHR10582:SF5. 1 hit.
PfamPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01768. TRPVRECEPTOR.
SMARTSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302697.
PROQ9WTR1.
SOURCESearch...

Entry information

Entry nameTRPV2_MOUSE
AccessionPrimary (citable) accession number: Q9WTR1
Secondary accession number(s): Q99K71
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot