Q9WUD2 (TRPV2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transient receptor potential cation channel subfamily V member 2
Short name=TrpV2

Alternative name(s):
Osm-9-like TRP channel 2
Short name=OTRPC2
Stretch-activated channel 2B
Vanilloid receptor-like protein 1
Short name=VRL-1

Gene names

Name:	Trpv2
Synonyms:	Sac2b, Vrl1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	761 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Ref.1 Ref.7
Subunit structure	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. Ref.6 Ref.7
Subcellular location	Cell membrane; Multi-pass membrane protein. Cytoplasm By similarity. Melanosome By similarity. Note: Translocates from the cytoplasm to the plasma membrane upon ligand stimulation By similarity. Ref.5 Ref.6 Ref.7
Tissue specificity	Ubiquitously expressed. Expressed in dorsal root ganglia, trigeminal ganglia, spinal chord (Lissauer's tract, dorsal horn and dorsal columns) (at protein level). Ref.1 Ref.7
Post-translational modification	N-glycosylated. Ref.5 Phosphorylated by PKA. Ref.7
Sequence similarities	Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV2 sub-subfamily. [View classification] Contains 6 ANK repeats.
Sequence caution	The sequence BAA93435.1 differs from that shown. Reason: Frameshift at position 758.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Cytoplasm Membrane
Domain	ANK repeat Repeat Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Calcium channel Ion channel
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of axon extension Inferred from electronic annotation. Source: Compara positive regulation of calcium ion import Inferred from electronic annotation. Source: Compara response to heat Inferred from direct assay Ref.1. Source: RGD
Cellular_component	axonal growth cone Inferred from electronic annotation. Source: Compara cell body Inferred from electronic annotation. Source: Compara cell surface Inferred from electronic annotation. Source: Compara endomembrane system Inferred from direct assay Ref.6. Source: UniProtKB growth cone membrane Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	calcium channel activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 761

761

Transient receptor potential cation channel subfamily V member 2

PRO_0000215344

Regions

Topological domain

1 – 392

392

Cytoplasmic Potential

Transmembrane

393 – 413

21

Helical; Potential

Topological domain

414 – 433

20

Extracellular Potential

Transmembrane

434 – 454

21

Helical; Potential

Topological domain

455 – 460

6

Cytoplasmic Potential

Transmembrane

461 – 481

21

Helical; Potential

Topological domain

482 – 495

14

Extracellular Potential

Transmembrane

496 – 516

21

Helical; Potential

Topological domain

517 – 537

21

Cytoplasmic Potential

Transmembrane

538 – 558

21

Helical; Potential

Intramembrane

573 – 609

37

Pore-forming; Potential

Transmembrane

622 – 642

21

Helical; Potential

Topological domain

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

Region

1 – 390

390

Required for interaction with SLC50A1

Amino acid modifications

Modified residue

15

1

Phosphoserine By similarity

Modified residue

47

1

Phosphoserine By similarity

Modified residue

760

1

Phosphoserine By similarity

Glycosylation

571

1

N-linked (GlcNAc...) Potential

Glycosylation

572

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

151

1

L → P Ref.1

Sequence conflict

151

1

L → P Ref.4

Sequence conflict

158

1

T → I in AAH89215. Ref.4

Sequence conflict

713

1

A → V in AAH89215. Ref.4

Secondary structure

1

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761

Helix Strand Turn

Details...

Helix

77 – 86

10

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

Turn

160 – 164

5

Helix

167 – 173

7

Helix

177 – 185

9

Helix

197 – 199

3

Beta strand

203 – 205

3

Helix

213 – 219

7

Helix

223 – 231

9

Beta strand

233 – 235

3

Helix

249 – 256

8

Helix

261 – 281

21

Helix

287 – 289

3

Helix

298 – 304

7

Helix

308 – 321

14

Sequences

	Sequence		Length	Mass (Da)
	Q9WUD2 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 8977CDE1D5351EC8	FASTA	761	86,706
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A capsaicin-receptor homologue with a high threshold for noxious heat." Caterina M.J., Rosen T.A., Tominaga M., Brake A.J., Julius D. Nature 398:436-441(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: Sprague-Dawley.
[2]	"Molecular cloning of a stretch activated channel from rat kidney." Ishibashi K. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	Suzuki M. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[5]	"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." Jahnel R., Bender O., Munter L.M., Dreger M., Gillen C., Hucho F. Eur. J. Biochem. 270:4264-4271(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[6]	"RGA protein associates with a TRPV ion channel during biosynthesis and trafficking." Barnhill J.C., Stokes A.J., Koblan-Huberson M., Shimoda L.M., Muraguchi A., Adra C.N., Turner H. J. Cell. Biochem. 91:808-820(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SLC50A1, SUBCELLULAR LOCATION.
[7]	"A TRPV2-PKA signaling module for transduction of physical stimuli in mast cells." Stokes A.J., Shimoda L.M., Koblan-Huberson M., Adra C.N., Turner H. J. Exp. Med. 200:137-147(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, PHOSPHORYLATION, INTERACTION WITH PRKAR2 AND ACBD3.
[8]	"Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel." Jin X., Touhey J., Gaudet R. J. Biol. Chem. 281:25006-25010(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 75-321, DOMAINS ANKYRIN REPEATS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF129113 mRNA. Translation: AAD26364.1.
AB029330 mRNA. Translation: BAA88637.1.
AB022332 mRNA. Translation: BAA93435.1. Frameshift.
BC089215 mRNA. Translation: AAH89215.1.

IPI

IPI00198821.

RefSeq

NP_001257726.1. NM_001270797.1.
NP_001257727.1. NM_001270798.1.
NP_058903.2. NM_017207.3.

UniGene

Rn.206528.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ETA	X-ray	2.20	A/B	75-321	[»]
2ETB	X-ray	1.65	A	75-321	[»]
2ETC	X-ray	3.10	A/B	62-326	[»]

ProteinModelPortal

Q9WUD2.

SMR

Q9WUD2. Positions 69-320.

ModBase

Search...

Proteomic databases

PaxDb

Q9WUD2.

PRIDE

Q9WUD2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000004248; ENSRNOP00000004248; ENSRNOG00000003104.

GeneID

29465.

KEGG

rno:29465.

UCSC

RGD:3965. rat.

Organism-specific databases

CTD

51393.

RGD

3965. Trpv2.

Phylogenomic databases

eggNOG

NOG281194.

GeneTree

ENSGT00550000074425.

HOGENOM

HOG000234630.

HOVERGEN

HBG054085.

InParanoid

Q9WUD2.

KO

K04971.

OrthoDB

EOG40ZQXF.

Gene expression databases

ArrayExpress

Q9WUD2.

Genevestigator

Q9WUD2.

GermOnline

ENSRNOG00000003104. Rattus norvegicus.

Family and domain databases

Gene3D

1.25.40.20. 1 hit.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
IPR024862. TRPV_channel.
[Graphical view]

PANTHER

PTHR10582. PTHR10582. 1 hit.
PTHR10582:SF3. PTHR10582:SF3. 1 hit.

Pfam

PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]

PRINTS

PR01768. TRPVRECEPTOR.

SMART

SM00248. ANK. 4 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

TIGRFAMs

TIGR00870. trp. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9WUD2.

ChEMBL

CHEMBL2863.

EvolutionaryTrace

Q9WUD2.

NextBio

609272.

Entry information

Entry name

TRPV2_RAT

Accession

Primary (citable) accession number: Q9WUD2
Secondary accession number(s): Q5FWT3, Q9JMI8, Q9QYH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	April 3, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program