[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. STRAIN=Sprague-Dawley; DOI=10.1038/18906; PubMed=10201375 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1046/j.1432-1033.2003.03811.x; PubMed=14622291 [NCBI, ExPASy, EBI, Israel, Japan] 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 RGA. DOI=10.1002/jcb.10775; PubMed=14991772 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1084/jem.20032082; PubMed=15249591 [NCBI, ExPASy, EBI, Israel, Japan] 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]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 75-321, AND DOMAINS ANKYRIN REPEATS. DOI=10.1074/jbc.C600153200; PubMed=16809337 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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).
SUBUNIT: Homotetramer (Probable). Interacts with a cAMP-dependent protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and ACBD3. Interacts with RGA.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein (By similarity). Cytoplasm (By similarity). Melanosome (By similarity). Note=Translocates from the cytoplasm to the plasma membrane upon ligand stimulation (By similarity).
TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in dorsal root ganglia, trigeminal ganglia, spinal chord (Lissauer's tract, dorsal horn and dorsal columns) (at protein level).
PTM: N-glycosylated.
PTM: Phosphorylated by PKA.
SIMILARITY: Belongs to the transient receptor family. TrpV subfamily.
SIMILARITY: Contains 6 ANK repeats.
SEQUENCE CAUTION:
- Sequence=BAA93435.1; Type=Frameshift; Positions=758;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF129113; AAD26364.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB029330; BAA88637.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB022332; BAA93435.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089215; AAH89215.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00198821; -.

NP_058903.2; -.

3D structure databases

PDB

2ETA; X-ray; 2.20 A; A/B=75-321.	[ExPASy / RCSB / EBI]
2ETB; X-ray; 1.65 A; A=75-321.	[ExPASy / RCSB / EBI]
2ETC; X-ray; 3.10 A; A/B=62-326.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2ETA; -.
2ETB; -.
2ETC; -.

ModBase

Q9WUD2.

Organism-specific databases

RGD

3965; Trpv2.

Gene expression databases

ArrayExpress

Q9WUD2; -.

GermOnline

ENSRNOG00000003104; Rattus norvegicus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0042470;	Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005262;	Molecular function: calcium channel activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006816;	Biological process: calcium ion transport (inferred from electronic annotation from UniProtKB-KW).
GO:0009408;	Biological process: response to heat (inferred from direct assay from RGD).
QuickGo view.

Family and domain databases

InterPro

IPR002110; ANK.
IPR005821; Ion_trans.
IPR004729; TRP_channel.
IPR008347; Vanilpoid_rcpt.
Graphical view of domain structure.

Gene3D

G3DSA:1.25.40.20; ANK; 1.

Pfam

PF00023; Ank; 4.
PF00520; Ion_trans; 1.
Pfam graphical view of domain structure.

PRINTS

PR01768; TRPVRECEPTOR.

SMART

SM00248; ANK; 4.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00870; trp; 1.

PROSITE

PS50297; ANK_REP_REGION; 1.
PS50088; ANK_REPEAT; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000003104; Rattus norvegicus. [Contig view]

GeneID

29465; -.

KEGG

rno:29465; -.

Phylogenomic databases

HOVERGEN

Q9WUD2; -.

Other

609272; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane; Cytoplasm; Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein; Repeat; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 761`	`761`	`Transient receptor potential cation channel subfamily V member 2.`	`PRO_0000215344`
`TOPO_DOM`	`1 392`	`392`	`Cytoplasmic (Potential).`
`TRANSMEM`	`393 413`	`21`	`Potential.`
`TOPO_DOM`	`414 433`	`20`	`Extracellular (Potential).`
`TRANSMEM`	`434 454`	`21`	`Potential.`
`TOPO_DOM`	`455 460`	`6`	`Cytoplasmic (Potential).`
`TRANSMEM`	`461 481`	`21`	`Potential.`
`TOPO_DOM`	`482 495`	`14`	`Extracellular (Potential).`
`TRANSMEM`	`496 516`	`21`	`Potential.`
`TOPO_DOM`	`517 537`	`21`	`Cytoplasmic (Potential).`
`TRANSMEM`	`538 558`	`21`	`Potential.`
`TOPO_DOM`	`559 621`	`63`	`Pore forming (Potential).`
`TRANSMEM`	`622 642`	`21`	`Potential.`
`TOPO_DOM`	`643 761`	`119`	`Cytoplasmic (Potential).`
`REPEAT`	`73 115`	`43`	`ANK 1.`
`REPEAT`	`116 162`	`47`	`ANK 2.`
`REPEAT`	`163 208`	`46`	`ANK 3.`
`REPEAT`	`209 244`	`36`	`ANK 4.`
`REPEAT`	`245 293`	`49`	`ANK 5.`
`REPEAT`	`294 320`	`27`	`ANK 6.`
`MOD_RES`	`15 15`		`Phosphoserine (By similarity).`
`MOD_RES`	`47 47`		`Phosphoserine (By similarity).`
`MOD_RES`	`525 525`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`526 526`		`Phosphoserine (By similarity).`
`CARBOHYD`	`571 571`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`572 572`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`151 151`		`L -> P (in Ref. 1 and 4).`
`CONFLICT`	`158 158`		`T -> I (in Ref. 4; AAH89215).`
`CONFLICT`	`713 713`		`A -> V (in Ref. 4; AAH89215).`
`HELIX`	`77 85`	`9`
`HELIX`	`89 92`	`4`
`HELIX`	`95 102`	`8`
`HELIX`	`109 111`	`3`
`TURN`	`114 116`	`3`
`HELIX`	`120 126`	`7`
`HELIX`	`136 145`	`10`
`HELIX`	`152 154`	`3`
`STRAND`	`159 162`	`4`
`HELIX`	`167 173`	`7`
`HELIX`	`177 185`	`9`
`HELIX`	`197 199`	`3`
`HELIX`	`213 219`	`7`
`HELIX`	`223 231`	`9`
`STRAND`	`233 235`	`3`
`HELIX`	`249 256`	`8`
`HELIX`	`261 281`	`21`
`HELIX`	`287 289`	`3`
`HELIX`	`298 304`	`7`
`HELIX`	`308 318`	`11`

Sequence information

Length: 761 AA [This is the length of the unprocessed precursor]

Molecular weight: 86706 Da [This is the MW of the unprocessed precursor]

CRC64: 8977CDE1D5351EC8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTSASSPPAF RLETSDGDEE GNAEVNKGKQ EPPPMESPFQ REDRNSSPQI KVNLNFIKRP 

        70         80         90        100        110        120 
PKNTSAPSQQ EPDRFDRDRL FSVVSRGVPE ELTGLLEYLR WNSKYLTDSA YTEGSTGKTC 

       130        140        150        160        170        180 
LMKAVLNLQD GVNACIMPLL QIDKDSGNPK LLVNAQCTDE FYQGHSALHI AIEKRSLQCV 

       190        200        210        220        230        240 
KLLVENGADV HLRACGRFFQ KHQGTCFYFG ELPLSLAACT KQWDVVTYLL ENPHQPASLE 

       250        260        270        280        290        300 
ATDSLGNTVL HALVMIADNS PENSALVIHM YDGLLQMGAR LCPTVQLEEI SNHQGLTPLK 

       310        320        330        340        350        360 
LAAKEGKIEI FRHILQREFS GPYQPLSRKF TEWCYGPVRV SLYDLSSVDS WEKNSVLEII 

       370        380        390        400        410        420 
AFHCKSPNRH RMVVLEPLNK LLQEKWDRLV SRFFFNFACY LVYMFIFTVV AYHQPSLDQP 

       430        440        450        460        470        480 
AIPSSKATFG ESMLLLGHIL ILLGGIYLLL GQLWYFWRRR LFIWISFMDS YFEILFLLQA 

       490        500        510        520        530        540 
LLTVLSQVLR FMETEWYLPL LVLSLVLGWL NLLYYTRGFQ HTGIYSVMIQ KVILRDLLRF 

       550        560        570        580        590        600 
LLVYLVFLFG FAVALVSLSR EARSPKAPED NNSTVTEQPT VGQEEEPAPY RSILDASLEL 

       610        620        630        640        650        660 
FKFTIGMGEL AFQEQLRFRG VVLLLLLAYV LLTYVLLLNM LIALMSETVN HVADNSWSIW 

       670        680        690        700        710        720 
KLQKAISVLE MENGYWWCRR KKHREGRLLK VGTRGDGTPD ERWCFRVEEV NWAAWEKTLP 

       730        740        750        760 
TLSEDPSGPG ITGNKKNPTS KPGKNSASEE DHLPLQVLQS P

Q9WUD2 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools