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Q9WTR1

- TRPV2_MOUSE

UniProt

Q9WTR1 - TRPV2_MOUSE

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Protein

Transient receptor potential cation channel subfamily V member 2

Gene

Trpv2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. calcium channel activity Source: MGI
  2. cation channel activity Source: MGI

GO - Biological processi

  1. positive regulation of axon extension Source: DFLAT
  2. positive regulation of calcium ion import Source: DFLAT
  3. response to heat Source: Ensembl
  4. response to temperature stimulus Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_227861. TRP channels.

Protein family/group databases

TCDBi1.A.4.2.4. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Trpv2
Synonyms:Grc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1341836. Trpv2.

Subcellular locationi

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

GO - Cellular componenti

  1. axon Source: DFLAT
  2. axonal growth cone Source: DFLAT
  3. cell body Source: DFLAT
  4. cell surface Source: DFLAT
  5. cytoplasm Source: UniProtKB-KW
  6. endomembrane system Source: Ensembl
  7. growth cone membrane Source: DFLAT
  8. integral component of membrane Source: UniProtKB-KW
  9. intracellular Source: MGI
  10. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 756756Transient receptor potential cation channel subfamily V member 2PRO_0000215343Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine1 Publication
Glycosylationi567 – 5671N-linked (GlcNAc...)Sequence Analysis
Modified residuei755 – 7551Phosphoserine1 Publication

Post-translational modificationi

N-glycosylated.1 Publication
Phosphorylated by PKA.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9WTR1.
PaxDbiQ9WTR1.
PRIDEiQ9WTR1.

PTM databases

PhosphoSiteiQ9WTR1.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9WTR1.
GenevestigatoriQ9WTR1.

Interactioni

Subunit structurei

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).By similarityCurated

Structurei

3D structure databases

ProteinModelPortaliQ9WTR1.
SMRiQ9WTR1. Positions 70-676.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 387387CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini409 – 42820ExtracellularSequence AnalysisAdd
BLAST
Topological domaini450 – 4556CytoplasmicSequence Analysis
Topological domaini477 – 49014ExtracellularSequence AnalysisAdd
BLAST
Topological domaini512 – 53221CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini638 – 756119CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei568 – 60437Pore-formingSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Transmembranei429 – 44921HelicalSequence AnalysisAdd
BLAST
Transmembranei456 – 47621HelicalSequence AnalysisAdd
BLAST
Transmembranei491 – 51121HelicalSequence AnalysisAdd
BLAST
Transmembranei533 – 55321HelicalSequence AnalysisAdd
BLAST
Transmembranei617 – 63721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati68 – 11043ANK 1Add
BLAST
Repeati111 – 15747ANK 2Add
BLAST
Repeati158 – 20346ANK 3Add
BLAST
Repeati204 – 23936ANK 4Add
BLAST
Repeati240 – 28849ANK 5Add
BLAST
Repeati289 – 31527ANK 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 385385Required for interaction with SLC50A1By similarityAdd
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG281194.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9WTR1.
KOiK04971.
OMAiLSQVLCF.
OrthoDBiEOG7V49XW.
PhylomeDBiQ9WTR1.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERiPTHR10582:SF5. PTHR10582:SF5. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WTR1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSASNPPAF RLETSDGDEE GSAEVNKGKN EPPPMESPFQ GEDRNFSPQI
60 70 80 90 100
KVNLNYRKGL GPSQQDPNRF DRDRLFSVVS RGVPEELTGL LEYLRRTSKY
110 120 130 140 150
LTDSAYTEGS TGKTCLMKAV LNLQDGVNAC ILPLLQIDRD SGNPQPLVNA
160 170 180 190 200
QCTDEFYRGH SALHIAIEKR SLWCVKLLVE NGANVHIRAC GRFFQKHQGT
210 220 230 240 250
CFYFGELPLS LAACTKQWDV VTYLLENPHQ PASLEATDSL GNTVLHALVM
260 270 280 290 300
IADNSPENSA LVIHMYDSLL QMGARLCPTV QLEDICNHQG LTPLKLAAKE
310 320 330 340 350
GKIEIFRHIL QREFSGLYQP LSRKFTEWCY GPVRVSLYDL SSVDSWEKNS
360 370 380 390 400
VLEIIAFHCK SPHRHRMVVL EPLNKLLQEK WDRLIPRFFF NFACYLVYMI
410 420 430 440 450
IFTIVAYHQP SLEQPAIPSS KATFGDSMLL LGHILILLGG IYLLLGQLWY
460 470 480 490 500
FWRRRLFIWI SFMDSYFEIL FLVQALLTVL SQVLRFVETE WYLPLLVSSL
510 520 530 540 550
VLGWLNLLYY TRGFQHTGIY SVMIQKVILR DLLRFLLVYL VFLFGFAVAL
560 570 580 590 600
VSLSREARSP KAPEDSNTTV TEKPTLGQEE EPVPYGGILD ASLELFKFTI
610 620 630 640 650
GMGELAFQEQ LRFRGVVLLL LLAYVLLTYV LLLNMLIALM SETVNSVATD
660 670 680 690 700
SWSIWKLQKA ISVLEMENGY WWCRRKRHRA GRLLKVGTKG DGIPDERWCF
710 720 730 740 750
RVEEVNWAAW EKTLPTLSED PSGAGITGYK KNPTSKPGKN SASEEDHLPL

QVLQSH
Length:756
Mass (Da):85,965
Last modified:April 26, 2005 - v2
Checksum:iC0E537AB2C86E1A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti565 – 5651D → N in BAA78478. (PubMed:10559903)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB021665 mRNA. Translation: BAA78478.1.
AK089004 mRNA. Translation: BAC40695.1.
AL596181 Genomic DNA. Translation: CAI24670.1.
BC005415 mRNA. Translation: AAH05415.1.
CCDSiCCDS24827.1.
RefSeqiNP_035836.2. NM_011706.2.
XP_006533228.1. XM_006533165.1.
UniGeneiMm.288064.

Genome annotation databases

EnsembliENSMUST00000018651; ENSMUSP00000018651; ENSMUSG00000018507.
ENSMUST00000102643; ENSMUSP00000099703; ENSMUSG00000018507.
GeneIDi22368.
KEGGimmu:22368.
UCSCiuc007jjh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB021665 mRNA. Translation: BAA78478.1 .
AK089004 mRNA. Translation: BAC40695.1 .
AL596181 Genomic DNA. Translation: CAI24670.1 .
BC005415 mRNA. Translation: AAH05415.1 .
CCDSi CCDS24827.1.
RefSeqi NP_035836.2. NM_011706.2.
XP_006533228.1. XM_006533165.1.
UniGenei Mm.288064.

3D structure databases

ProteinModelPortali Q9WTR1.
SMRi Q9WTR1. Positions 70-676.
ModBasei Search...
MobiDBi Search...

Chemistry

GuidetoPHARMACOLOGYi 508.

Protein family/group databases

TCDBi 1.A.4.2.4. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSitei Q9WTR1.

Proteomic databases

MaxQBi Q9WTR1.
PaxDbi Q9WTR1.
PRIDEi Q9WTR1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018651 ; ENSMUSP00000018651 ; ENSMUSG00000018507 .
ENSMUST00000102643 ; ENSMUSP00000099703 ; ENSMUSG00000018507 .
GeneIDi 22368.
KEGGi mmu:22368.
UCSCi uc007jjh.1. mouse.

Organism-specific databases

CTDi 51393.
MGIi MGI:1341836. Trpv2.

Phylogenomic databases

eggNOGi NOG281194.
GeneTreei ENSGT00550000074425.
HOGENOMi HOG000234630.
HOVERGENi HBG054085.
InParanoidi Q9WTR1.
KOi K04971.
OMAi LSQVLCF.
OrthoDBi EOG7V49XW.
PhylomeDBi Q9WTR1.
TreeFami TF314711.

Enzyme and pathway databases

Reactomei REACT_227861. TRP channels.

Miscellaneous databases

NextBioi 302697.
PROi Q9WTR1.
SOURCEi Search...

Gene expression databases

Bgeei Q9WTR1.
Genevestigatori Q9WTR1.

Family and domain databases

Gene3Di 1.25.40.20. 2 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view ]
PANTHERi PTHR10582:SF5. PTHR10582:SF5. 1 hit.
Pfami PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
PRINTSi PR01768. TRPVRECEPTOR.
SMARTi SM00248. ANK. 4 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
TIGRFAMsi TIGR00870. trp. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].

Entry informationi

Entry nameiTRPV2_MOUSE
AccessioniPrimary (citable) accession number: Q9WTR1
Secondary accession number(s): Q99K71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: October 29, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3