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Q9Y5S1 (TRPV2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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
Gene names
Name:TRPV2
Synonyms:VRL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Protein existenceEvidence 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 IGF-I, PDGF and 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. Ref.1

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 By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cytoplasm By similarity. Melanosome. Note: Translocates from the cytoplasm to the plasma membrane upon ligand stimulation By similarity. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.8

Post-translational modification

N-glycosylated By similarity.

Phosphorylated by PKA By similarity.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV2 sub-subfamily. [View classification]

Contains 6 ANK repeats.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainANK repeat
Repeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Traceable author statement. Source: Reactome

ion transmembrane transport

Traceable author statement. Source: Reactome

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion import

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

response to temperature stimulus

Inferred from direct assay Ref.1. Source: MGI

sensory perception

Traceable author statement Ref.1. Source: ProtInc

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentaxonal growth cone

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

endomembrane system

Inferred from electronic annotation. Source: Ensembl

growth cone membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.1. Source: MGI

   Molecular_functioncalcium channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

cation channel activity

Inferred from direct assay Ref.1. Source: MGI

ion channel activity

Traceable author statement Ref.1. Source: ProtInc

ion transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 764764Transient receptor potential cation channel subfamily V member 2
PRO_0000215342

Regions

Topological domain1 – 390390Cytoplasmic Potential
Transmembrane391 – 41121Helical; Potential
Topological domain412 – 43423Extracellular Potential
Transmembrane435 – 45521Helical; Potential
Topological domain456 – 47116Cytoplasmic Potential
Transmembrane472 – 49221Helical; Potential
Topological domain4931Extracellular Potential
Transmembrane494 – 51421Helical; Potential
Topological domain515 – 53723Cytoplasmic Potential
Transmembrane538 – 55821Helical; Potential
Intramembrane572 – 60938Pore-forming; Potential
Transmembrane622 – 64221Helical; Potential
Topological domain643 – 764122Cytoplasmic Potential
Repeat72 – 11443ANK 1
Repeat115 – 16147ANK 2
Repeat162 – 20746ANK 3
Repeat208 – 24336ANK 4
Repeat244 – 29249ANK 5
Repeat293 – 31927ANK 6
Region1 – 388388Required for interaction with SLC50A1 By similarity

Amino acid modifications

Modified residue7631Phosphoserine By similarity
Glycosylation5701N-linked (GlcNAc...) Potential

Natural variations

Natural variant171G → A.
Corresponds to variant rs3813768 [ dbSNP | Ensembl ].
VAR_024678
Natural variant7641N → S.
Corresponds to variant rs8071215 [ dbSNP | Ensembl ].
VAR_059838

Experimental info

Sequence conflict521P → S in AAD41724. Ref.2
Sequence conflict821A → V in AAD41724. Ref.2
Sequence conflict2001K → N in AAD41724. Ref.2
Sequence conflict4591V → L in AAD41724. Ref.2
Sequence conflict465 – 4662FI → YT in AAD41724. Ref.2
Sequence conflict477 – 4782QA → HS in AAD41724. Ref.2
Sequence conflict4851Q → L in AAD41724. Ref.2
Sequence conflict4911A → V in AAD41724. Ref.2
Sequence conflict535 – 5362LL → MV in AAD41724. Ref.2
Sequence conflict5401L → V in AAD41724. Ref.2

Secondary structure

....................................... 764
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5S1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A73E3696E70F91E9

FASTA76485,981
        10         20         30         40         50         60 
MTSPSSSPVF RLETLDGGQE DGSEADRGKL DFGSGLPPME SQFQGEDRKF APQIRVNLNY 

        70         80         90        100        110        120 
RKGTGASQPD PNRFDRDRLF NAVSRGVPED LAGLPEYLSK TSKYLTDSEY TEGSTGKTCL 

       130        140        150        160        170        180 
MKAVLNLKDG VNACILPLLQ IDRDSGNPQP LVNAQCTDDY YRGHSALHIA IEKRSLQCVK 

       190        200        210        220        230        240 
LLVENGANVH ARACGRFFQK GQGTCFYFGE LPLSLAACTK QWDVVSYLLE NPHQPASLQA 

       250        260        270        280        290        300 
TDSQGNTVLH ALVMISDNSA ENIALVTSMY DGLLQAGARL CPTVQLEDIR NLQDLTPLKL 

       310        320        330        340        350        360 
AAKEGKIEIF RHILQREFSG LSHLSRKFTE WCYGPVRVSL YDLASVDSCE ENSVLEIIAF 

       370        380        390        400        410        420 
HCKSPHRHRM VVLEPLNKLL QAKWDLLIPK FFLNFLCNLI YMFIFTAVAY HQPTLKKQAA 

       430        440        450        460        470        480 
PHLKAEVGNS MLLTGHILIL LGGIYLLVGQ LWYFWRRHVF IWISFIDSYF EILFLFQALL 

       490        500        510        520        530        540 
TVVSQVLCFL AIEWYLPLLV SALVLGWLNL LYYTRGFQHT GIYSVMIQKV ILRDLLRFLL 

       550        560        570        580        590        600 
IYLVFLFGFA VALVSLSQEA WRPEAPTGPN ATESVQPMEG QEDEGNGAQY RGILEASLEL 

       610        620        630        640        650        660 
FKFTIGMGEL AFQEQLHFRG MVLLLLLAYV LLTYILLLNM LIALMSETVN SVATDSWSIW 

       670        680        690        700        710        720 
KLQKAISVLE MENGYWWCRK KQRAGVMLTV GTKPDGSPDE RWCFRVEEVN WASWEQTLPT 

       730        740        750        760 
LCEDPSGAGV PRTLENPVLA SPPKEDEDGA SEENYVPVQL LQSN 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Lymphoblast.
[2]"Cloning and functional expression of VRL, a vanilloid receptor-like gene."
Garcia R.L., Delmas P., Cesare P., England S., Liapi A., Wood J.N.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoblast.
[3]Kelsell R.E.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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: Skin.
[8]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[9]"Crystal structure of the human TRPV2 channel ankyrin repeat domain."
McCleverty C.J., Koesema E., Patapoutian A., Lesley S.A., Kreusch A.
Protein Sci. 15:2201-2206(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 69-319, ANK REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF129112 mRNA. Translation: AAD26363.1.
AF103906 mRNA. Translation: AAD41724.1.
AJ487963 mRNA. Translation: CAD32310.1.
AK289705 mRNA. Translation: BAF82394.1.
AC093484 Genomic DNA. No translation available.
CH471222 Genomic DNA. Translation: EAX04508.1.
BC018926 mRNA. Translation: AAH18926.1.
BC051305 mRNA. Translation: AAH51305.1.
RefSeqNP_057197.2. NM_016113.4.
UniGeneHs.279746.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F37X-ray1.70A/B69-319[»]
ProteinModelPortalQ9Y5S1.
SMRQ9Y5S1. Positions 70-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119520. 1 interaction.
STRING9606.ENSP00000342222.

Chemistry

ChEMBLCHEMBL5051.
GuidetoPHARMACOLOGY508.

Protein family/group databases

TCDB1.A.4.2.8. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteQ9Y5S1.

Polymorphism databases

DMDM62901477.

Proteomic databases

PaxDbQ9Y5S1.
PRIDEQ9Y5S1.

Protocols and materials databases

DNASU51393.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338560; ENSP00000342222; ENSG00000187688.
GeneID51393.
KEGGhsa:51393.
UCSCuc002gpy.3. human.

Organism-specific databases

CTD51393.
GeneCardsGC17P016318.
HGNCHGNC:18082. TRPV2.
HPAHPA044993.
MIM606676. gene.
neXtProtNX_Q9Y5S1.
PharmGKBPA38292.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281194.
HOGENOMHOG000234630.
HOVERGENHBG054085.
InParanoidQ9Y5S1.
KOK04971.
OMASMLLLGH.
OrthoDBEOG7V49XW.
PhylomeDBQ9Y5S1.
TreeFamTF314711.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9Y5S1.
BgeeQ9Y5S1.
CleanExHS_TRPV2.
GenevestigatorQ9Y5S1.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR024862. TRPV.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERPTHR10582. PTHR10582. 1 hit.
PTHR10582:SF3. PTHR10582:SF3. 1 hit.
PfamPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01768. TRPVRECEPTOR.
SMARTSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y5S1.
GeneWikiTRPV2.
GenomeRNAi51393.
NextBio54925.
PROQ9Y5S1.
SOURCESearch...

Entry information

Entry nameTRPV2_HUMAN
AccessionPrimary (citable) accession number: Q9Y5S1
Secondary accession number(s): A6NML2, A8K0Z0, Q9Y670
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM