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Protein

Transient receptor potential cation channel subfamily V member 2

Gene

Trpv2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

  • negative regulation of cell proliferation Source: RGD
  • response to heat Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
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 namesi
Name:Trpv2
Synonyms:Sac2b, Vrl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3965. Trpv2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 392392CytoplasmicSequence analysisAdd
BLAST
Transmembranei393 – 41321HelicalSequence analysisAdd
BLAST
Topological domaini414 – 43320ExtracellularSequence analysisAdd
BLAST
Transmembranei434 – 45421HelicalSequence analysisAdd
BLAST
Topological domaini455 – 4606CytoplasmicSequence analysis
Transmembranei461 – 48121HelicalSequence analysisAdd
BLAST
Topological domaini482 – 49514ExtracellularSequence analysisAdd
BLAST
Transmembranei496 – 51621HelicalSequence analysisAdd
BLAST
Topological domaini517 – 53721CytoplasmicSequence analysisAdd
BLAST
Transmembranei538 – 55821HelicalSequence analysisAdd
BLAST
Intramembranei573 – 60937Pore-formingSequence analysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence analysisAdd
BLAST
Topological domaini643 – 761119CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • endomembrane system Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • lamellipodium Source: RGD
  • melanosome Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2096684.
GuidetoPHARMACOLOGYi508.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 761761Transient receptor potential cation channel subfamily V member 2PRO_0000215344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei82 – 821PhosphoserineCombined sources
Glycosylationi571 – 5711N-linked (GlcNAc...)Sequence analysis
Glycosylationi572 – 5721N-linked (GlcNAc...)Sequence analysis
Modified residuei748 – 7481PhosphoserineBy similarity
Modified residuei760 – 7601PhosphoserineCombined sources

Post-translational modificationi

N-glycosylated.1 Publication
Phosphorylated by PKA.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9WUD2.
PRIDEiQ9WUD2.

PTM databases

iPTMnetiQ9WUD2.
SwissPalmiQ9WUD2.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed in dorsal root ganglia, trigeminal ganglia, spinal chord (Lissauer's tract, dorsal horn and dorsal columns) (at protein level).2 Publications

Interactioni

Subunit structurei

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.Curated2 Publications

Protein-protein interaction databases

DIPiDIP-60657N.
STRINGi10116.ENSRNOP00000004248.

Chemistry

BindingDBiQ9WUD2.

Structurei

Secondary structure

1
761
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi77 – 8610Combined sources
Helixi89 – 924Combined sources
Helixi95 – 1028Combined sources
Helixi109 – 1113Combined sources
Turni114 – 1163Combined sources
Helixi120 – 1267Combined sources
Helixi136 – 14510Combined sources
Helixi152 – 1543Combined sources
Turni160 – 1645Combined sources
Helixi167 – 1737Combined sources
Helixi177 – 1859Combined sources
Helixi197 – 1993Combined sources
Beta strandi203 – 2053Combined sources
Helixi213 – 2197Combined sources
Helixi223 – 2319Combined sources
Beta strandi233 – 2353Combined sources
Helixi249 – 2568Combined sources
Helixi261 – 28121Combined sources
Helixi287 – 2893Combined sources
Helixi298 – 3047Combined sources
Helixi308 – 32114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ETAX-ray2.20A/B75-321[»]
2ETBX-ray1.65A75-321[»]
2ETCX-ray3.10A/B62-326[»]
5HI9electron microscopy4.40A/B/C/D1-761[»]
ProteinModelPortaliQ9WUD2.
SMRiQ9WUD2. Positions 69-320.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WUD2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati73 – 11543ANK 1PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati116 – 16247ANK 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati163 – 20846ANK 3PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati209 – 24436ANK 4PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati245 – 29349ANK 5PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati294 – 32027ANK 6PROSITE-ProRule annotation1 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 390390Required for interaction with SLC50A1Add
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9WUD2.
KOiK04971.
OrthoDBiEOG7V49XW.
PhylomeDBiQ9WUD2.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERiPTHR10582:SF5. PTHR10582:SF5. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WUD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSASSPPAF RLETSDGDEE GNAEVNKGKQ EPPPMESPFQ REDRNSSPQI
60 70 80 90 100
KVNLNFIKRP PKNTSAPSQQ EPDRFDRDRL FSVVSRGVPE ELTGLLEYLR
110 120 130 140 150
WNSKYLTDSA YTEGSTGKTC LMKAVLNLQD GVNACIMPLL QIDKDSGNPK
160 170 180 190 200
LLVNAQCTDE FYQGHSALHI AIEKRSLQCV KLLVENGADV HLRACGRFFQ
210 220 230 240 250
KHQGTCFYFG ELPLSLAACT KQWDVVTYLL ENPHQPASLE ATDSLGNTVL
260 270 280 290 300
HALVMIADNS PENSALVIHM YDGLLQMGAR LCPTVQLEEI SNHQGLTPLK
310 320 330 340 350
LAAKEGKIEI FRHILQREFS GPYQPLSRKF TEWCYGPVRV SLYDLSSVDS
360 370 380 390 400
WEKNSVLEII AFHCKSPNRH RMVVLEPLNK LLQEKWDRLV SRFFFNFACY
410 420 430 440 450
LVYMFIFTVV AYHQPSLDQP AIPSSKATFG ESMLLLGHIL ILLGGIYLLL
460 470 480 490 500
GQLWYFWRRR LFIWISFMDS YFEILFLLQA LLTVLSQVLR FMETEWYLPL
510 520 530 540 550
LVLSLVLGWL NLLYYTRGFQ HTGIYSVMIQ KVILRDLLRF LLVYLVFLFG
560 570 580 590 600
FAVALVSLSR EARSPKAPED NNSTVTEQPT VGQEEEPAPY RSILDASLEL
610 620 630 640 650
FKFTIGMGEL AFQEQLRFRG VVLLLLLAYV LLTYVLLLNM LIALMSETVN
660 670 680 690 700
HVADNSWSIW KLQKAISVLE MENGYWWCRR KKHREGRLLK VGTRGDGTPD
710 720 730 740 750
ERWCFRVEEV NWAAWEKTLP TLSEDPSGPG ITGNKKNPTS KPGKNSASEE
760
DHLPLQVLQS P
Length:761
Mass (Da):86,706
Last modified:April 26, 2005 - v2
Checksum:i8977CDE1D5351EC8
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511L → P (PubMed:10201375).Curated
Sequence conflicti151 – 1511L → P (PubMed:15489334).Curated
Sequence conflicti158 – 1581T → I in AAH89215 (PubMed:15489334).Curated
Sequence conflicti713 – 7131A → V in AAH89215 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129113 mRNA. Translation: AAD26364.1.
AB029330 mRNA. Translation: BAA88637.1.
AB022332 mRNA. Translation: BAA93435.1. Frameshift.
BC089215 mRNA. Translation: AAH89215.1.
RefSeqiNP_001257726.1. NM_001270797.1.
NP_001257727.1. NM_001270798.1.
NP_058903.2. NM_017207.3.
UniGeneiRn.206528.

Genome annotation databases

GeneIDi29465.
KEGGirno:29465.
UCSCiRGD:3965. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129113 mRNA. Translation: AAD26364.1.
AB029330 mRNA. Translation: BAA88637.1.
AB022332 mRNA. Translation: BAA93435.1. Frameshift.
BC089215 mRNA. Translation: AAH89215.1.
RefSeqiNP_001257726.1. NM_001270797.1.
NP_001257727.1. NM_001270798.1.
NP_058903.2. NM_017207.3.
UniGeneiRn.206528.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ETAX-ray2.20A/B75-321[»]
2ETBX-ray1.65A75-321[»]
2ETCX-ray3.10A/B62-326[»]
5HI9electron microscopy4.40A/B/C/D1-761[»]
ProteinModelPortaliQ9WUD2.
SMRiQ9WUD2. Positions 69-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60657N.
STRINGi10116.ENSRNOP00000004248.

Chemistry

BindingDBiQ9WUD2.
ChEMBLiCHEMBL2096684.
GuidetoPHARMACOLOGYi508.

PTM databases

iPTMnetiQ9WUD2.
SwissPalmiQ9WUD2.

Proteomic databases

PaxDbiQ9WUD2.
PRIDEiQ9WUD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29465.
KEGGirno:29465.
UCSCiRGD:3965. rat.

Organism-specific databases

CTDi51393.
RGDi3965. Trpv2.

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9WUD2.
KOiK04971.
OrthoDBiEOG7V49XW.
PhylomeDBiQ9WUD2.
TreeFamiTF314711.

Miscellaneous databases

EvolutionaryTraceiQ9WUD2.
PROiQ9WUD2.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERiPTHR10582:SF5. PTHR10582:SF5. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-82 AND SER-760, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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, ANK REPEATS.

Entry informationi

Entry nameiTRPV2_RAT
AccessioniPrimary (citable) accession number: Q9WUD2
Secondary accession number(s): Q5FWT3, Q9JMI8, Q9QYH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: June 8, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.