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 25-MAY-2022, entry version 165.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 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 project:
RT 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 derived
RT cell line F-11 and biochemical analysis of VRL-1 after heterologous
RT 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., Muraguchi A.,
RA Adra C.N., Turner H.;
RT "RGA protein associates with a TRPV ion channel during biosynthesis and
RT 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 mast
RT cells.";
RL J. Exp. Med. 200:137-147(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-82 AND SER-760, AND
RP 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., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT 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 neuropeptide/head
CC activator. May transduce physical stimuli in mast cells. Activated by
CC temperatures higher than 52 degrees Celsius; is not activated by
CC vanilloids and acidic pH (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10201375, 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 Q9WUD2; Q9WUD2: Trpv2; NbExp=3; IntAct=EBI-11689641, EBI-11689641;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. Note=Translocates
CC from the cytoplasm to the plasma membrane upon ligand stimulation.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in dorsal root
CC ganglia, trigeminal ganglia, spinal cord (Lissauer's tract, dorsal horn
CC and dorsal columns) (at protein level). {ECO:0000269|PubMed:10201375,
CC 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. TrpV
CC subfamily. TRPV2 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA93435.1; Type=Frameshift; Evidence={ECO:0000305};
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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 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 PDB; 6BO4; EM; 4.00 A; A/B/C/D=72-726.
DR PDB; 6BO5; EM; 3.60 A; A/B/C/D=72-726.
DR PDB; 6U84; EM; 3.70 A; A/B/C/D=1-761.
DR PDB; 6U86; EM; 4.00 A; A/B/C/D=1-761.
DR PDB; 6U88; EM; 3.20 A; A/B/C/D=1-761.
DR PDB; 6U8A; EM; 3.40 A; A/B/C/D=1-761.
DR PDB; 6WKN; EM; 3.46 A; A/B/C/D=1-761.
DR PDBsum; 2ETA; -.
DR PDBsum; 2ETB; -.
DR PDBsum; 2ETC; -.
DR PDBsum; 5HI9; -.
DR PDBsum; 6BO4; -.
DR PDBsum; 6BO5; -.
DR PDBsum; 6U84; -.
DR PDBsum; 6U86; -.
DR PDBsum; 6U88; -.
DR PDBsum; 6U8A; -.
DR PDBsum; 6WKN; -.
DR AlphaFoldDB; Q9WUD2; -.
DR SMR; Q9WUD2; -.
DR DIP; DIP-60657N; -.
DR IntAct; Q9WUD2; 3.
DR MINT; Q9WUD2; -.
DR STRING; 10116.ENSRNOP00000004248; -.
DR BindingDB; Q9WUD2; -.
DR ChEMBL; CHEMBL2863; -.
DR DrugCentral; Q9WUD2; -.
DR GuidetoPHARMACOLOGY; 508; -.
DR GlyGen; Q9WUD2; 2 sites.
DR iPTMnet; Q9WUD2; -.
DR PhosphoSitePlus; Q9WUD2; -.
DR SwissPalm; Q9WUD2; -.
DR jPOST; 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 InParanoid; Q9WUD2; -.
DR OrthoDB; 693004at2759; -.
DR PhylomeDB; Q9WUD2; -.
DR TreeFam; TF314711; -.
DR Reactome; R-RNO-3295583; TRP channels.
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: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: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; 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:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0009408; P:response to heat; IDA:RGD.
DR GO; GO:0009266; P:response to temperature stimulus; ISO:RGD.
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 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Cytoplasm; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..761
FT /note="Transient receptor potential cation channel
FT subfamily V member 2"
FT /id="PRO_0000215344"
FT TOPO_DOM 1..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 573..609
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..761
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 73..115
FT /note="ANK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16809337"
FT REPEAT 116..162
FT /note="ANK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16809337"
FT REPEAT 163..208
FT /note="ANK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16809337"
FT REPEAT 209..244
FT /note="ANK 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16809337"
FT REPEAT 245..293
FT /note="ANK 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16809337"
FT REPEAT 294..320
FT /note="ANK 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:16809337"
FT REGION 1..390
FT /note="Required for interaction with SLC50A1"
FT /evidence="ECO:0000269|PubMed:14991772"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTR1"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTR1"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 151
FT /note="L -> P (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="T -> I (in Ref. 4; AAH89215)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="A -> V (in Ref. 4; AAH89215)"
FT /evidence="ECO:0000305"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 95..102
FT /evidence="ECO:0007829|PDB:2ETB"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:6U8A"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2ETB"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2ETB"
FT TURN 160..164
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2ETB"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:2ETB"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:2ETA"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6U8A"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 261..281
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 308..321
FT /evidence="ECO:0007829|PDB:2ETB"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:6WKN"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:6U88"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 378..412
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 430..458
FT /evidence="ECO:0007829|PDB:6U88"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 472..491
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 497..511
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 512..518
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 520..558
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:6U8A"
FT HELIX 593..605
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:6U8A"
FT HELIX 619..650
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 657..671
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:6U88"
FT STRAND 700..710
FT /evidence="ECO:0007829|PDB:6U88"
FT HELIX 712..717
FT /evidence="ECO:0007829|PDB:6U8A"
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
