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Transient receptor potential cation channel subfamily V member 2 (TrpV2) (Osm-9-like TRP channel 2) (OTRPC2) (Stretch-activated channel 2B) (Vanilloid receptor-like protein 1) (VRL-1)

 TRPV2_RAT               Reviewed;         761 AA.
Q9WUD2; Q5FWT3; Q9JMI8; Q9QYH8;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
12-SEP-2018, entry version 147.
RecName: Full=Transient receptor potential cation channel subfamily V member 2;
Short=TrpV2;
AltName: Full=Osm-9-like TRP channel 2;
Short=OTRPC2;
AltName: Full=Stretch-activated channel 2B;
AltName: Full=Vanilloid receptor-like protein 1;
Short=VRL-1;
Name=Trpv2; Synonyms=Sac2b, Vrl1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=10201375; DOI=10.1038/18906;
Caterina M.J., Rosen T.A., Tominaga M., Brake A.J., Julius D.;
"A capsaicin-receptor homologue with a high threshold for noxious
heat.";
Nature 398:436-441(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Ishibashi K.;
"Molecular cloning of a stretch activated channel from rat kidney.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Suzuki M.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=14622291; DOI=10.1046/j.1432-1033.2003.03811.x;
Jahnel R., Bender O., Munter L.M., Dreger M., Gillen C., Hucho F.;
"Dual expression of mouse and rat VRL-1 in the dorsal root ganglion
derived cell line F-11 and biochemical analysis of VRL-1 after
heterologous expression.";
Eur. J. Biochem. 270:4264-4271(2003).
[6]
INTERACTION WITH SLC50A1, AND SUBCELLULAR LOCATION.
PubMed=14991772; DOI=10.1002/jcb.10775;
Barnhill J.C., Stokes A.J., Koblan-Huberson M., Shimoda L.M.,
Muraguchi A., Adra C.N., Turner H.;
"RGA protein associates with a TRPV ion channel during biosynthesis
and trafficking.";
J. Cell. Biochem. 91:808-820(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT,
PHOSPHORYLATION, AND INTERACTION WITH PRKAR2 AND ACBD3.
PubMed=15249591; DOI=10.1084/jem.20032082;
Stokes A.J., Shimoda L.M., Koblan-Huberson M., Adra C.N., Turner H.;
"A TRPV2-PKA signaling module for transduction of physical stimuli in
mast cells.";
J. Exp. Med. 200:137-147(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-82 AND SER-760,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[9]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 75-321, AND ANK REPEATS.
PubMed=16809337; DOI=10.1074/jbc.C600153200;
Jin X., Touhey J., Gaudet R.;
"Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion
channel.";
J. Biol. Chem. 281:25006-25010(2006).
-!- FUNCTION: Calcium-permeable, non-selective cation channel with an
outward rectification. Seems to be regulated, at least in part, by
growth factors, like IGF1, PDGF and morphogenetic
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 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:10201375,
ECO:0000269|PubMed:15249591}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:14991772, ECO:0000269|PubMed:15249591,
ECO:0000305}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-11689641, EBI-11689641;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}.
Note=Translocates from the cytoplasm to the plasma membrane upon
ligand stimulation. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in dorsal
root ganglia, trigeminal ganglia, spinal chord (Lissauer's tract,
dorsal horn and dorsal columns) (at protein level).
{ECO:0000269|PubMed:10201375, ECO:0000269|PubMed:15249591}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:14622291}.
-!- PTM: Phosphorylated by PKA. {ECO:0000269|PubMed:15249591}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV2 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA93435.1; Type=Frameshift; Positions=758; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF129113; AAD26364.1; -; mRNA.
EMBL; AB029330; BAA88637.1; -; mRNA.
EMBL; AB022332; BAA93435.1; ALT_FRAME; mRNA.
EMBL; BC089215; AAH89215.1; -; mRNA.
RefSeq; NP_001257726.1; NM_001270797.1.
RefSeq; NP_001257727.1; NM_001270798.1.
RefSeq; NP_058903.2; NM_017207.3.
UniGene; Rn.206528; -.
PDB; 2ETA; X-ray; 2.20 A; A/B=75-321.
PDB; 2ETB; X-ray; 1.65 A; A=75-321.
PDB; 2ETC; X-ray; 3.10 A; A/B=62-326.
PDB; 5HI9; EM; 4.40 A; A/B/C/D=1-761.
PDBsum; 2ETA; -.
PDBsum; 2ETB; -.
PDBsum; 2ETC; -.
PDBsum; 5HI9; -.
ProteinModelPortal; Q9WUD2; -.
SMR; Q9WUD2; -.
DIP; DIP-60657N; -.
IntAct; Q9WUD2; 1.
STRING; 10116.ENSRNOP00000004248; -.
BindingDB; Q9WUD2; -.
ChEMBL; CHEMBL2863; -.
GuidetoPHARMACOLOGY; 508; -.
iPTMnet; Q9WUD2; -.
PhosphoSitePlus; Q9WUD2; -.
SwissPalm; Q9WUD2; -.
PaxDb; Q9WUD2; -.
PRIDE; Q9WUD2; -.
GeneID; 29465; -.
KEGG; rno:29465; -.
UCSC; RGD:3965; rat.
CTD; 51393; -.
RGD; 3965; Trpv2.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
HOGENOM; HOG000234630; -.
HOVERGEN; HBG054085; -.
InParanoid; Q9WUD2; -.
KO; K04971; -.
PhylomeDB; Q9WUD2; -.
TreeFam; TF314711; -.
EvolutionaryTrace; Q9WUD2; -.
PRO; PR:Q9WUD2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0030027; C:lamellipodium; IDA:RGD.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
GO; GO:0009408; P:response to heat; IDA:RGD.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR024862; TRPV.
InterPro; IPR008347; TRPV1-4_channel.
InterPro; IPR024865; TRPV2_channel.
PANTHER; PTHR10582; PTHR10582; 1.
PANTHER; PTHR10582:SF5; PTHR10582:SF5; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01768; TRPVRECEPTOR.
SMART; SM00248; ANK; 4.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
1: Evidence at protein level;
3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
Cell membrane; Complete proteome; Cytoplasm; Glycoprotein;
Ion channel; Ion transport; Membrane; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 761 Transient receptor potential cation
channel subfamily V member 2.
/FTId=PRO_0000215344.
TOPO_DOM 1 392 Cytoplasmic. {ECO:0000255}.
TRANSMEM 393 413 Helical. {ECO:0000255}.
TOPO_DOM 414 433 Extracellular. {ECO:0000255}.
TRANSMEM 434 454 Helical. {ECO:0000255}.
TOPO_DOM 455 460 Cytoplasmic. {ECO:0000255}.
TRANSMEM 461 481 Helical. {ECO:0000255}.
TOPO_DOM 482 495 Extracellular. {ECO:0000255}.
TRANSMEM 496 516 Helical. {ECO:0000255}.
TOPO_DOM 517 537 Cytoplasmic. {ECO:0000255}.
TRANSMEM 538 558 Helical. {ECO:0000255}.
INTRAMEM 573 609 Pore-forming. {ECO:0000255}.
TRANSMEM 622 642 Helical. {ECO:0000255}.
TOPO_DOM 643 761 Cytoplasmic. {ECO:0000255}.
REPEAT 73 115 ANK 1. {ECO:0000255|PROSITE-
ProRule:PRU00023,
ECO:0000269|PubMed:16809337}.
REPEAT 116 162 ANK 2. {ECO:0000255|PROSITE-
ProRule:PRU00023,
ECO:0000269|PubMed:16809337}.
REPEAT 163 208 ANK 3. {ECO:0000255|PROSITE-
ProRule:PRU00023,
ECO:0000269|PubMed:16809337}.
REPEAT 209 244 ANK 4. {ECO:0000255|PROSITE-
ProRule:PRU00023,
ECO:0000269|PubMed:16809337}.
REPEAT 245 293 ANK 5. {ECO:0000255|PROSITE-
ProRule:PRU00023,
ECO:0000269|PubMed:16809337}.
REPEAT 294 320 ANK 6. {ECO:0000255|PROSITE-
ProRule:PRU00023,
ECO:0000269|PubMed:16809337}.
REGION 1 390 Required for interaction with SLC50A1.
{ECO:0000269|PubMed:14991772}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WTR1}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WTR1}.
MOD_RES 760 760 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 151 151 L -> P (in Ref. 1 and 4). {ECO:0000305}.
CONFLICT 158 158 T -> I (in Ref. 4; AAH89215).
{ECO:0000305}.
CONFLICT 713 713 A -> V (in Ref. 4; AAH89215).
{ECO:0000305}.
HELIX 77 86 {ECO:0000244|PDB:2ETB}.
HELIX 89 92 {ECO:0000244|PDB:2ETB}.
HELIX 95 102 {ECO:0000244|PDB:2ETB}.
HELIX 109 111 {ECO:0000244|PDB:2ETB}.
TURN 114 116 {ECO:0000244|PDB:2ETB}.
HELIX 120 126 {ECO:0000244|PDB:2ETB}.
HELIX 136 145 {ECO:0000244|PDB:2ETB}.
HELIX 152 154 {ECO:0000244|PDB:2ETB}.
TURN 160 164 {ECO:0000244|PDB:2ETB}.
HELIX 167 173 {ECO:0000244|PDB:2ETB}.
HELIX 177 185 {ECO:0000244|PDB:2ETB}.
HELIX 197 199 {ECO:0000244|PDB:2ETB}.
STRAND 203 205 {ECO:0000244|PDB:2ETB}.
HELIX 213 219 {ECO:0000244|PDB:2ETB}.
HELIX 223 231 {ECO:0000244|PDB:2ETB}.
STRAND 233 235 {ECO:0000244|PDB:2ETA}.
HELIX 249 256 {ECO:0000244|PDB:2ETB}.
HELIX 261 281 {ECO:0000244|PDB:2ETB}.
HELIX 287 289 {ECO:0000244|PDB:2ETB}.
HELIX 298 304 {ECO:0000244|PDB:2ETB}.
HELIX 308 321 {ECO:0000244|PDB:2ETB}.
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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