TRPV2_MOUSE
ID TRPV2_MOUSE Reviewed; 756 AA.
AC Q9WTR1; Q99K71;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 2;
DE Short=TrpV2;
DE AltName: Full=Growth factor-regulated calcium channel;
DE Short=GRC;
DE AltName: Full=Osm-9-like TRP channel 2;
DE Short=OTRPC2;
GN Name=Trpv2; Synonyms=Grc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=10559903; DOI=10.1038/11086;
RA Kanzaki M., Zhang Y.-Q., Mashima H., Li L., Shibata H., Kojima I.;
RT "Translocation of a calcium-permeable cation channel induced by insulin-
RT like growth factor-I.";
RL Nat. Cell Biol. 1:165-170(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11707512; DOI=10.1242/jcs.114.20.3599;
RA Boels K., Glassmeier G., Herrmann D., Riedel I.B., Hampe W., Kojima I.,
RA Schwarz J.R., Schaller H.C.;
RT "The neuropeptide head activator induces activation and translocation of
RT the growth-factor-regulated Ca(2+)-permeable channel GRC.";
RL J. Cell Sci. 114:3599-3606(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-755, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-743, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-permeable, non-selective cation channel with an
CC outward rectification. Seems to be regulated, at least in part, by IGF-
CC I, PDGF and neuropeptide head activator. May transduce physical stimuli
CC in mast cells. Activated by temperatures higher than 52 degrees
CC Celsius; is not activated by vanilloids and acidic pH.
CC {ECO:0000269|PubMed:10559903, ECO:0000269|PubMed:11707512}.
CC -!- SUBUNIT: Homotetramer (Probable). Interacts with a cAMP-dependent
CC protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and
CC ACBD3. Interacts with SLC50A1; the interaction probably occurs
CC intracellularly and depends on TRPV2 N-glycosylation (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasm. Melanosome {ECO:0000250}. Note=Translocates from the
CC cytoplasm to the plasma membrane upon ligand stimulation.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in spleen, placenta, skeleton
CC muscle, lung and brain. {ECO:0000269|PubMed:10559903}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:10559903}.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AB021665; BAA78478.1; -; mRNA.
DR EMBL; AK089004; BAC40695.1; -; mRNA.
DR EMBL; AL596181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005415; AAH05415.1; -; mRNA.
DR CCDS; CCDS24827.1; -.
DR RefSeq; NP_035836.2; NM_011706.2.
DR RefSeq; XP_006533228.1; XM_006533165.2.
DR RefSeq; XP_011247273.1; XM_011248971.1.
DR AlphaFoldDB; Q9WTR1; -.
DR SMR; Q9WTR1; -.
DR BioGRID; 204537; 1.
DR IntAct; Q9WTR1; 2.
DR MINT; Q9WTR1; -.
DR STRING; 10090.ENSMUSP00000018651; -.
DR BindingDB; Q9WTR1; -.
DR ChEMBL; CHEMBL4523498; -.
DR GuidetoPHARMACOLOGY; 508; -.
DR TCDB; 1.A.4.2.4; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q9WTR1; 1 site.
DR iPTMnet; Q9WTR1; -.
DR PhosphoSitePlus; Q9WTR1; -.
DR SwissPalm; Q9WTR1; -.
DR EPD; Q9WTR1; -.
DR jPOST; Q9WTR1; -.
DR MaxQB; Q9WTR1; -.
DR PaxDb; Q9WTR1; -.
DR PeptideAtlas; Q9WTR1; -.
DR PRIDE; Q9WTR1; -.
DR ProteomicsDB; 258986; -.
DR Antibodypedia; 13247; 307 antibodies from 36 providers.
DR DNASU; 22368; -.
DR Ensembl; ENSMUST00000018651; ENSMUSP00000018651; ENSMUSG00000018507.
DR Ensembl; ENSMUST00000102643; ENSMUSP00000099703; ENSMUSG00000018507.
DR GeneID; 22368; -.
DR KEGG; mmu:22368; -.
DR UCSC; uc007jjh.1; mouse.
DR CTD; 51393; -.
DR MGI; MGI:1341836; Trpv2.
DR VEuPathDB; HostDB:ENSMUSG00000018507; -.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000158512; -.
DR HOGENOM; CLU_012795_1_1_1; -.
DR InParanoid; Q9WTR1; -.
DR OMA; TNACILP; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q9WTR1; -.
DR TreeFam; TF314711; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 22368; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q9WTR1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WTR1; protein.
DR Bgee; ENSMUSG00000018507; Expressed in placenta labyrinth and 149 other tissues.
DR Genevisible; Q9WTR1; MM.
DR GO; GO:0030424; C:axon; IDA:DFLAT.
DR GO; GO:0044295; C:axonal growth cone; IDA:DFLAT.
DR GO; GO:0044297; C:cell body; IDA:DFLAT.
DR GO; GO:0009986; C:cell surface; IDA:DFLAT.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; ISO:MGI.
DR GO; GO:0032584; C:growth cone membrane; IDA:DFLAT.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:DFLAT.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IMP:DFLAT.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR GO; GO:0009266; P:response to temperature stimulus; ISO:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR024862; TRPV.
DR InterPro; IPR008347; TrpV1-4.
DR InterPro; IPR024865; TrpV2.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR PANTHER; PTHR10582:SF5; PTHR10582:SF5; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01768; TRPVRECEPTOR.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cytoplasm; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..756
FT /note="Transient receptor potential cation channel
FT subfamily V member 2"
FT /id="PRO_0000215343"
FT TOPO_DOM 1..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 568..604
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 638..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 68..110
FT /note="ANK 1"
FT REPEAT 111..157
FT /note="ANK 2"
FT REPEAT 158..203
FT /note="ANK 3"
FT REPEAT 204..239
FT /note="ANK 4"
FT REPEAT 240..288
FT /note="ANK 5"
FT REPEAT 289..315
FT /note="ANK 6"
FT REGION 1..385
FT /note="Required for interaction with SLC50A1"
FT /evidence="ECO:0000250"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUD2"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 565
FT /note="D -> N (in Ref. 1; BAA78478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 756 AA; 85965 MW; C0E537AB2C86E1A8 CRC64;
MTSASNPPAF RLETSDGDEE GSAEVNKGKN EPPPMESPFQ GEDRNFSPQI KVNLNYRKGL
GPSQQDPNRF DRDRLFSVVS RGVPEELTGL LEYLRRTSKY LTDSAYTEGS TGKTCLMKAV
LNLQDGVNAC ILPLLQIDRD SGNPQPLVNA QCTDEFYRGH SALHIAIEKR SLWCVKLLVE
NGANVHIRAC GRFFQKHQGT CFYFGELPLS LAACTKQWDV VTYLLENPHQ PASLEATDSL
GNTVLHALVM IADNSPENSA LVIHMYDSLL QMGARLCPTV QLEDICNHQG LTPLKLAAKE
GKIEIFRHIL QREFSGLYQP LSRKFTEWCY GPVRVSLYDL SSVDSWEKNS VLEIIAFHCK
SPHRHRMVVL EPLNKLLQEK WDRLIPRFFF NFACYLVYMI IFTIVAYHQP SLEQPAIPSS
KATFGDSMLL LGHILILLGG IYLLLGQLWY FWRRRLFIWI SFMDSYFEIL FLVQALLTVL
SQVLRFVETE WYLPLLVSSL VLGWLNLLYY TRGFQHTGIY SVMIQKVILR DLLRFLLVYL
VFLFGFAVAL VSLSREARSP KAPEDSNTTV TEKPTLGQEE EPVPYGGILD ASLELFKFTI
GMGELAFQEQ LRFRGVVLLL LLAYVLLTYV LLLNMLIALM SETVNSVATD SWSIWKLQKA
ISVLEMENGY WWCRRKRHRA GRLLKVGTKG DGIPDERWCF RVEEVNWAAW EKTLPTLSED
PSGAGITGYK KNPTSKPGKN SASEEDHLPL QVLQSH
