Reviewed, UniProtKB/Swiss-Prot Q9Y5S1 (TRPV2_HUMAN)

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
    Vanilloid receptor-like protein 1
      Short name=VRL-1

Gene names

Name:	TRPV2
Synonyms:	VRL

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	764 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 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 RGA 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 family. TrpV subfamily. Contains 6 ANK repeats.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat Transmembrane
Ligand	Calcium
Molecular function	Calcium channel Ionic channel
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW sensory perception Ref.1 Traceable author statement. Source: ProtInc
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium channel activity Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding 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 – 764

764

Transient receptor potential cation channel subfamily V member 2

PRO_0000215342

Regions

Topological domain

1 – 390

390

Cytoplasmic Potential

Transmembrane

391 – 411

21

Potential

Topological domain

412 – 434

23

Extracellular Potential

Transmembrane

435 – 455

21

Potential

Topological domain

456 – 471

16

Cytoplasmic Potential

Transmembrane

472 – 492

21

Potential

Topological domain

493

1

Extracellular Potential

Transmembrane

494 – 514

21

Potential

Topological domain

515 – 537

23

Cytoplasmic Potential

Transmembrane

538 – 558

21

Potential

Topological domain

559 – 621

63

Pore forming Potential

Transmembrane

622 – 642

21

Potential

Topological domain

643 – 764

122

Cytoplasmic Potential

Repeat

72 – 114

43

ANK 1

Repeat

115 – 161

47

ANK 2

Repeat

162 – 207

46

ANK 3

Repeat

208 – 243

36

ANK 4

Repeat

244 – 292

49

ANK 5

Repeat

293 – 319

27

ANK 6

Amino acid modifications

Modified residue

523

1

Phosphotyrosine Ref.9

Modified residue

524

1

Phosphoserine Ref.9

Modified residue

763

1

Phosphoserine By similarity

Glycosylation

570

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

17

1

G → A: dbSNP rs3813768.

VAR_024678

Natural variant

764

1

N → S: dbSNP rs8071215.

VAR_059838

Experimental info

Sequence conflict

52

1

P → S in AAD41724. Ref.2

Sequence conflict

82

1

A → V in AAD41724. Ref.2

Sequence conflict

200

1

K → N in AAD41724. Ref.2

Sequence conflict

459

1

V → L in AAD41724. Ref.2

Sequence conflict

465 – 466

2

FI → YT in AAD41724. Ref.2

Sequence conflict

477 – 478

2

QA → HS in AAD41724. Ref.2

Sequence conflict

485

1

Q → L in AAD41724. Ref.2

Sequence conflict

491

1

A → V in AAD41724. Ref.2

Sequence conflict

535 – 536

2

LL → MV in AAD41724. Ref.2

Sequence conflict

540

1

L → V in AAD41724. Ref.2

Secondary structure

1

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764

Helix Strand Turn

Details...

Helix

76 – 84

9

Helix

88 – 91

4

Helix

94 – 101

8

Helix

108 – 110

3

Turn

113 – 115

3

Helix

119 – 125

7

Helix

135 – 145

11

Helix

151 – 153

3

Turn

159 – 163

5

Helix

166 – 172

7

Helix

176 – 184

9

Helix

196 – 198

3

Helix

212 – 218

7

Helix

222 – 230

9

Helix

248 – 255

8

Helix

260 – 280

21

Helix

286 – 288

3

Helix

297 – 303

7

Helix

307 – 315

9

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5S1-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: A73E3696E70F91E9	FASTA	764	85,981
	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

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: 10201375] [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. , 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: 14702039] [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. , 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: 16625196] [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. , 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: 15489334] [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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-523 AND SER-524, MASS SPECTROMETRY.
[10]	"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: 16882997] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 69-319, DOMAINS ANKYRIN 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.

IPI

IPI00183666.

RefSeq

NP_057197.2.

UniGene

Hs.279746

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F37	X-ray	1.70	A/B	69-319	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

Q9Y5S1.

Protein family/group databases

TCDB

1.A.4.2.8. transient receptor potential Ca2+ channel (TRP-CC) family.

PTM databases

PhosphoSite

Q9Y5S1.

Proteomic databases

PRIDE

Q9Y5S1.

Genome annotation databases

Ensembl

ENST00000338560; ENSP00000342222; ENSG00000187688; Homo sapiens. [Genome view]

GeneID

51393.

KEGG

hsa:51393.

UCSC

uc002gpy.1. human.

Organism-specific databases

CTD

51393.

GeneCards

GC17P016259.

H-InvDB

HIX0013570.
HIX0059753.

HGNC

HGNC:18082. TRPV2.

MIM

606676. gene.

PharmGKB

PA38292.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04475.

HOGENOM

HBG446456.

HOVERGEN

Q9Y5S1.

InParanoid

Q9Y5S1.

OMA

IQKVILR.

OrthoDB

EOG9SR0FX.

Gene expression databases

ArrayExpress

Q9Y5S1.

Bgee

Q9Y5S1.

CleanEx

HS_TRPV2.

Genevestigator

Q9Y5S1.

GermOnline

ENSG00000187688. Homo sapiens.

Family and domain databases

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR004729. TRP_channel.
IPR008347. Vanilpoid_rcpt.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.

Pfam

PF00023. Ank. 1 hit.
[Graphical view]

PRINTS

PR01768. TRPVRECEPTOR.

SMART

SM00248. ANK. 4 hits.
[Graphical view]

TIGRFAMs

TIGR00870. trp. 1 hit.

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

54925.

SOURCE

Search...

Entry information

Entry name

TRPV2_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.