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Reviewed, UniProtKB/Swiss-Prot Q9WUD2 (TRPV2_RAT)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
    Vanilloid receptor-like protein 1
      Short name=VRL-1
    Stretch-activated channel 2B
Gene names
Name: Trpv2
Synonyms: Sac2b, Vrl1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length761 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Subunit structure

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). Ref.1 Ref.7

Post-translational modification

N-glycosylated. Ref.5

Phosphorylated by PKA. Ref.7

Sequence similarities

Belongs to the transient receptor family. TrpV subfamily.

Contains 6 ANK repeats.

Sequence caution

The sequence BAA93435.1 differs from that shown. Reason: Frameshift at position 758.

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Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainANK repeat
Repeat
Transmembrane
   LigandCalcium
   Molecular functionCalcium channel
Ionic channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcalcium ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

response to heat Ref.1

Inferred from direct assay. Source: RGD

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 761761Transient receptor potential cation channel subfamily V member 2
PRO_0000215344

Regions

Topological domain1 – 392392Cytoplasmic Potential
Transmembrane393 – 41321 Potential
Topological domain414 – 43320Extracellular Potential
Transmembrane434 – 45421 Potential
Topological domain455 – 4606Cytoplasmic Potential
Transmembrane461 – 48121 Potential
Topological domain482 – 49514Extracellular Potential
Transmembrane496 – 51621 Potential
Topological domain517 – 53721Cytoplasmic Potential
Transmembrane538 – 55821 Potential
Topological domain559 – 62163Pore forming Potential
Transmembrane622 – 64221 Potential
Topological domain643 – 761119Cytoplasmic Potential
Repeat73 – 11543ANK 1
Repeat116 – 16247ANK 2
Repeat163 – 20846ANK 3
Repeat209 – 24436ANK 4
Repeat245 – 29349ANK 5
Repeat294 – 32027ANK 6

Amino acid modifications

Modified residue151Phosphoserine By similarity
Modified residue471Phosphoserine By similarity
Modified residue5251Phosphotyrosine By similarity
Modified residue5261Phosphoserine By similarity
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation5721N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1511L → P Ref.1
Sequence conflict1511L → P Ref.4
Sequence conflict1581T → I in AAH89215. Ref.4
Sequence conflict7131A → V in AAH89215. Ref.4

Secondary structure

1 ......................................... 761
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9WUD2-1 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 8977CDE1D5351EC8

FASTA76186,706
        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

« Hide

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References

« Hide '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: 10201375] [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: 15489334] [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: 14622291] [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: 14991772] [Abstract]
Cited for: INTERACTION WITH RGA.
[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: 15249591] [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: 16809337] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 75-321, DOMAINS ANKYRIN REPEATS.

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Cross-references

Sequence databases

AF129113 mRNA. Translation: AAD26364.1.
AB029330 mRNA. Translation: BAA88637.1.
AB022332 mRNA. Translation: BAA93435.1. Frameshift.
BC089215 mRNA. Translation: AAH89215.1.
IPIIPI00198821.
RefSeqNP_058903.2.
UniGeneRn.206528

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2ETAX-ray2.20A/B75-321[»]
2ETBX-ray1.65A75-321[»]
2ETCX-ray3.10A/B62-326[»]
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000003104. Rattus norvegicus. [Contig view]
GeneID29465.
KEGGrno:29465.

Organism-specific databases

RGD3965. Trpv2.

Phylogenomic databases

HOVERGENQ9WUD2.

Gene expression databases

ArrayExpressQ9WUD2.
GermOnlineENSRNOG00000003104. Rattus norvegicus.

Family and domain databases

InterProIPR002110. ANK.
IPR005821. Ion_trans.
IPR004729. TRP_channel.
IPR008347. Vanilpoid_rcpt.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 4 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01768. TRPVRECEPTOR.
SMARTSM00248. ANK. 4 hits.
[Graphical view]
TIGRFAMsTIGR00870. trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio609272.

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Entry information

Entry nameTRPV2_RAT
AccessionPrimary (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: June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents