GenomeNet

Database: UniProt
Entry: TRPV2_RAT
LinkDB: TRPV2_RAT
Original site: TRPV2_RAT 
ID   TRPV2_RAT               Reviewed;         761 AA.
AC   Q9WUD2; Q5FWT3; Q9JMI8; Q9QYH8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   22-NOV-2017, entry version 145.
DE   RecName: Full=Transient receptor potential cation channel subfamily V member 2;
DE            Short=TrpV2;
DE   AltName: Full=Osm-9-like TRP channel 2;
DE            Short=OTRPC2;
DE   AltName: Full=Stretch-activated channel 2B;
DE   AltName: Full=Vanilloid receptor-like protein 1;
DE            Short=VRL-1;
GN   Name=Trpv2; Synonyms=Sac2b, Vrl1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=10201375; DOI=10.1038/18906;
RA   Caterina M.J., Rosen T.A., Tominaga M., Brake A.J., Julius D.;
RT   "A capsaicin-receptor homologue with a high threshold for noxious
RT   heat.";
RL   Nature 398:436-441(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Ishibashi K.;
RT   "Molecular cloning of a stretch activated channel from rat kidney.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Suzuki M.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX   PubMed=14622291; DOI=10.1046/j.1432-1033.2003.03811.x;
RA   Jahnel R., Bender O., Munter L.M., Dreger M., Gillen C., Hucho F.;
RT   "Dual expression of mouse and rat VRL-1 in the dorsal root ganglion
RT   derived cell line F-11 and biochemical analysis of VRL-1 after
RT   heterologous expression.";
RL   Eur. J. Biochem. 270:4264-4271(2003).
RN   [6]
RP   INTERACTION WITH SLC50A1, AND SUBCELLULAR LOCATION.
RX   PubMed=14991772; DOI=10.1002/jcb.10775;
RA   Barnhill J.C., Stokes A.J., Koblan-Huberson M., Shimoda L.M.,
RA   Muraguchi A., Adra C.N., Turner H.;
RT   "RGA protein associates with a TRPV ion channel during biosynthesis
RT   and trafficking.";
RL   J. Cell. Biochem. 91:808-820(2004).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT,
RP   PHOSPHORYLATION, AND INTERACTION WITH PRKAR2 AND ACBD3.
RX   PubMed=15249591; DOI=10.1084/jem.20032082;
RA   Stokes A.J., Shimoda L.M., Koblan-Huberson M., Adra C.N., Turner H.;
RT   "A TRPV2-PKA signaling module for transduction of physical stimuli in
RT   mast cells.";
RL   J. Exp. Med. 200:137-147(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-82 AND SER-760,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 75-321, AND ANK REPEATS.
RX   PubMed=16809337; DOI=10.1074/jbc.C600153200;
RA   Jin X., Touhey J., Gaudet R.;
RT   "Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion
RT   channel.";
RL   J. Biol. Chem. 281:25006-25010(2006).
CC   -!- FUNCTION: Calcium-permeable, non-selective cation channel with an
CC       outward rectification. Seems to be regulated, at least in part, by
CC       growth factors, like IGF1, PDGF and morphogenetic
CC       neuropeptide/head activator. May transduce physical stimuli in
CC       mast cells. Activated by temperatures higher than 52 degrees
CC       Celsius; is not activated by vanilloids and acidic pH (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:10201375,
CC       ECO:0000269|PubMed:15249591}.
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.
CC       {ECO:0000269|PubMed:14991772, ECO:0000269|PubMed:15249591,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-11689641, EBI-11689641;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}.
CC       Note=Translocates from the cytoplasm to the plasma membrane upon
CC       ligand stimulation. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in dorsal
CC       root ganglia, trigeminal ganglia, spinal chord (Lissauer's tract,
CC       dorsal horn and dorsal columns) (at protein level).
CC       {ECO:0000269|PubMed:10201375, ECO:0000269|PubMed:15249591}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14622291}.
CC   -!- PTM: Phosphorylated by PKA. {ECO:0000269|PubMed:15249591}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       TrpV subfamily. TRPV2 sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA93435.1; Type=Frameshift; Positions=758; Evidence={ECO:0000305};
DR   EMBL; AF129113; AAD26364.1; -; mRNA.
DR   EMBL; AB029330; BAA88637.1; -; mRNA.
DR   EMBL; AB022332; BAA93435.1; ALT_FRAME; mRNA.
DR   EMBL; BC089215; AAH89215.1; -; mRNA.
DR   RefSeq; NP_001257726.1; NM_001270797.1.
DR   RefSeq; NP_001257727.1; NM_001270798.1.
DR   RefSeq; NP_058903.2; NM_017207.3.
DR   UniGene; Rn.206528; -.
DR   PDB; 2ETA; X-ray; 2.20 A; A/B=75-321.
DR   PDB; 2ETB; X-ray; 1.65 A; A=75-321.
DR   PDB; 2ETC; X-ray; 3.10 A; A/B=62-326.
DR   PDB; 5HI9; EM; 4.40 A; A/B/C/D=1-761.
DR   PDBsum; 2ETA; -.
DR   PDBsum; 2ETB; -.
DR   PDBsum; 2ETC; -.
DR   PDBsum; 5HI9; -.
DR   ProteinModelPortal; Q9WUD2; -.
DR   SMR; Q9WUD2; -.
DR   DIP; DIP-60657N; -.
DR   IntAct; Q9WUD2; 1.
DR   STRING; 10116.ENSRNOP00000004248; -.
DR   BindingDB; Q9WUD2; -.
DR   ChEMBL; CHEMBL2863; -.
DR   GuidetoPHARMACOLOGY; 508; -.
DR   iPTMnet; Q9WUD2; -.
DR   PhosphoSitePlus; Q9WUD2; -.
DR   SwissPalm; Q9WUD2; -.
DR   PaxDb; Q9WUD2; -.
DR   PRIDE; Q9WUD2; -.
DR   GeneID; 29465; -.
DR   KEGG; rno:29465; -.
DR   UCSC; RGD:3965; rat.
DR   CTD; 51393; -.
DR   RGD; 3965; Trpv2.
DR   eggNOG; KOG3676; Eukaryota.
DR   eggNOG; ENOG4110DG4; LUCA.
DR   HOGENOM; HOG000234630; -.
DR   HOVERGEN; HBG054085; -.
DR   InParanoid; Q9WUD2; -.
DR   KO; K04971; -.
DR   PhylomeDB; Q9WUD2; -.
DR   TreeFam; TF314711; -.
DR   EvolutionaryTrace; Q9WUD2; -.
DR   PRO; PR:Q9WUD2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0044295; C:axonal growth cone; ISO:RGD.
DR   GO; GO:0044297; C:cell body; ISO:RGD.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR   GO; GO:0032584; C:growth cone membrane; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005622; C:intracellular; ISO:RGD.
DR   GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005262; F:calcium channel activity; ISO:RGD.
DR   GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
DR   GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
DR   GO; GO:0009408; P:response to heat; IDA:RGD.
DR   GO; GO:0009266; P:response to temperature stimulus; ISO:RGD.
DR   CDD; cd00204; ANK; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR024862; TRPV.
DR   InterPro; IPR008347; TRPV1-4_channel.
DR   InterPro; IPR024865; TRPV2_channel.
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   TIGRFAMs; TIGR00870; trp; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW   Cell membrane; Complete proteome; Cytoplasm; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    761       Transient receptor potential cation
FT                                channel subfamily V member 2.
FT                                /FTId=PRO_0000215344.
FT   TOPO_DOM      1    392       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    393    413       Helical. {ECO:0000255}.
FT   TOPO_DOM    414    433       Extracellular. {ECO:0000255}.
FT   TRANSMEM    434    454       Helical. {ECO:0000255}.
FT   TOPO_DOM    455    460       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    461    481       Helical. {ECO:0000255}.
FT   TOPO_DOM    482    495       Extracellular. {ECO:0000255}.
FT   TRANSMEM    496    516       Helical. {ECO:0000255}.
FT   TOPO_DOM    517    537       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    538    558       Helical. {ECO:0000255}.
FT   INTRAMEM    573    609       Pore-forming. {ECO:0000255}.
FT   TRANSMEM    622    642       Helical. {ECO:0000255}.
FT   TOPO_DOM    643    761       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       73    115       ANK 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00023,
FT                                ECO:0000269|PubMed:16809337}.
FT   REPEAT      116    162       ANK 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00023,
FT                                ECO:0000269|PubMed:16809337}.
FT   REPEAT      163    208       ANK 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00023,
FT                                ECO:0000269|PubMed:16809337}.
FT   REPEAT      209    244       ANK 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00023,
FT                                ECO:0000269|PubMed:16809337}.
FT   REPEAT      245    293       ANK 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00023,
FT                                ECO:0000269|PubMed:16809337}.
FT   REPEAT      294    320       ANK 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00023,
FT                                ECO:0000269|PubMed:16809337}.
FT   REGION        1    390       Required for interaction with SLC50A1.
FT                                {ECO:0000269|PubMed:14991772}.
FT   MOD_RES       6      6       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES      15     15       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9WTR1}.
FT   MOD_RES      82     82       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     748    748       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9WTR1}.
FT   MOD_RES     760    760       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    572    572       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    151    151       L -> P (in Ref. 1 and 4). {ECO:0000305}.
FT   CONFLICT    158    158       T -> I (in Ref. 4; AAH89215).
FT                                {ECO:0000305}.
FT   CONFLICT    713    713       A -> V (in Ref. 4; AAH89215).
FT                                {ECO:0000305}.
FT   HELIX        77     86       {ECO:0000244|PDB:2ETB}.
FT   HELIX        89     92       {ECO:0000244|PDB:2ETB}.
FT   HELIX        95    102       {ECO:0000244|PDB:2ETB}.
FT   HELIX       109    111       {ECO:0000244|PDB:2ETB}.
FT   TURN        114    116       {ECO:0000244|PDB:2ETB}.
FT   HELIX       120    126       {ECO:0000244|PDB:2ETB}.
FT   HELIX       136    145       {ECO:0000244|PDB:2ETB}.
FT   HELIX       152    154       {ECO:0000244|PDB:2ETB}.
FT   TURN        160    164       {ECO:0000244|PDB:2ETB}.
FT   HELIX       167    173       {ECO:0000244|PDB:2ETB}.
FT   HELIX       177    185       {ECO:0000244|PDB:2ETB}.
FT   HELIX       197    199       {ECO:0000244|PDB:2ETB}.
FT   STRAND      203    205       {ECO:0000244|PDB:2ETB}.
FT   HELIX       213    219       {ECO:0000244|PDB:2ETB}.
FT   HELIX       223    231       {ECO:0000244|PDB:2ETB}.
FT   STRAND      233    235       {ECO:0000244|PDB:2ETA}.
FT   HELIX       249    256       {ECO:0000244|PDB:2ETB}.
FT   HELIX       261    281       {ECO:0000244|PDB:2ETB}.
FT   HELIX       287    289       {ECO:0000244|PDB:2ETB}.
FT   HELIX       298    304       {ECO:0000244|PDB:2ETB}.
FT   HELIX       308    321       {ECO:0000244|PDB:2ETB}.
SQ   SEQUENCE   761 AA;  86706 MW;  8977CDE1D5351EC8 CRC64;
     MTSASSPPAF RLETSDGDEE GNAEVNKGKQ EPPPMESPFQ REDRNSSPQI KVNLNFIKRP
     PKNTSAPSQQ EPDRFDRDRL FSVVSRGVPE ELTGLLEYLR WNSKYLTDSA YTEGSTGKTC
     LMKAVLNLQD GVNACIMPLL QIDKDSGNPK LLVNAQCTDE FYQGHSALHI AIEKRSLQCV
     KLLVENGADV HLRACGRFFQ KHQGTCFYFG ELPLSLAACT KQWDVVTYLL ENPHQPASLE
     ATDSLGNTVL HALVMIADNS PENSALVIHM YDGLLQMGAR LCPTVQLEEI SNHQGLTPLK
     LAAKEGKIEI FRHILQREFS GPYQPLSRKF TEWCYGPVRV SLYDLSSVDS WEKNSVLEII
     AFHCKSPNRH RMVVLEPLNK LLQEKWDRLV SRFFFNFACY LVYMFIFTVV AYHQPSLDQP
     AIPSSKATFG ESMLLLGHIL ILLGGIYLLL GQLWYFWRRR LFIWISFMDS YFEILFLLQA
     LLTVLSQVLR FMETEWYLPL LVLSLVLGWL NLLYYTRGFQ HTGIYSVMIQ KVILRDLLRF
     LLVYLVFLFG FAVALVSLSR EARSPKAPED NNSTVTEQPT VGQEEEPAPY RSILDASLEL
     FKFTIGMGEL AFQEQLRFRG VVLLLLLAYV LLTYVLLLNM LIALMSETVN HVADNSWSIW
     KLQKAISVLE MENGYWWCRR KKHREGRLLK VGTRGDGTPD ERWCFRVEEV NWAAWEKTLP
     TLSEDPSGPG ITGNKKNPTS KPGKNSASEE DHLPLQVLQS P
//
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