LOCUS NP_001257727 761 aa linear ROD 03-SEP-2023
DEFINITION transient receptor potential cation channel subfamily V member 2
[Rattus norvegicus].
ACCESSION NP_001257727
VERSION NP_001257727.1
DBSOURCE REFSEQ: accession NM_001270798.1
KEYWORDS RefSeq.
SOURCE Rattus norvegicus (Norway rat)
ORGANISM Rattus norvegicus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
REFERENCE 1 (residues 1 to 761)
AUTHORS Shigemi S, Sato T, Sakamoto M, Yajima T, Honda T, Tsumaki H,
Deguchi T, Ichikawa H, Fukunaga T and Mizoguchi I.
TITLE The role of TRPV2 as a regulator on the osteoclast differentiation
during orthodontic tooth movement in rats
JOURNAL Sci Rep 13 (1), 13718 (2023)
PUBMED 37608122
REMARK GeneRIF: The role of TRPV2 as a regulator on the osteoclast
differentiation during orthodontic tooth movement in rats.
Publication Status: Online-Only
REFERENCE 2 (residues 1 to 761)
AUTHORS Zhang L, Simonsen C, Zimova L, Wang K, Moparthi L, Gaudet R, Ekoff
M, Nilsson G, Hellmich UA, Vlachova V, Gourdon P and Zygmunt PM.
TITLE Cannabinoid non-cannabidiol site modulation of TRPV2 structure and
function
JOURNAL Nat Commun 13 (1), 7483 (2022)
PUBMED 36470868
REMARK GeneRIF: Cannabinoid non-cannabidiol site modulation of TRPV2
structure and function.
Publication Status: Online-Only
REFERENCE 3 (residues 1 to 761)
AUTHORS O'Hare M, Esquiva G, McGahon MK, Hombrebueno JMR, Augustine J,
Canning P, Edgar KS, Barabas P, Friedel T, Cincola P, Henry J,
Mayne K, Ferrin H, Stitt AW, Lyons TJ, Brazil DP, Grieve DJ,
McGeown JG and Curtis TM.
TITLE Loss of TRPV2-mediated blood flow autoregulation recapitulates
diabetic retinopathy in rats
JOURNAL JCI Insight 7 (18), e155128 (2022)
PUBMED 36134661
REMARK GeneRIF: Loss of TRPV2-mediated blood flow autoregulation
recapitulates diabetic retinopathy in rats.
Publication Status: Online-Only
REFERENCE 4 (residues 1 to 761)
AUTHORS Mo X, Pang P, Wang Y, Jiang D, Zhang M, Li Y, Wang P, Geng Q, Xie
C, Du HN, Zhong B, Li D and Yao J.
TITLE Tyrosine phosphorylation tunes chemical and thermal sensitivity of
TRPV2 ion channel
JOURNAL Elife 11, e78301 (2022)
PUBMED 35686730
REMARK GeneRIF: Tyrosine phosphorylation tunes chemical and thermal
sensitivity of TRPV2 ion channel.
Publication Status: Online-Only
REFERENCE 5 (residues 1 to 761)
AUTHORS Chen L, Chen Y, Ding W, Zhan T, Zhu J, Zhang L, Wang H, Shen B and
Wang Y.
TITLE Oxidative Stress-Induced TRPV2 Expression Increase Is Involved in
Diabetic Cataracts and Apoptosis of Lens Epithelial Cells in a
High-Glucose Environment
JOURNAL Cells 11 (7), 1196 (2022)
PUBMED 35406761
REMARK GeneRIF: Oxidative Stress-Induced TRPV2 Expression Increase Is
Involved in Diabetic Cataracts and Apoptosis of Lens Epithelial
Cells in a High-Glucose Environment.
Publication Status: Online-Only
REFERENCE 6 (residues 1 to 761)
AUTHORS Zahner MR, Li DP, Chen SR and Pan HL.
TITLE Cardiac vanilloid receptor 1-expressing afferent nerves and their
role in the cardiogenic sympathetic reflex in rats
JOURNAL J Physiol 551 (Pt 2), 515-523 (2003)
PUBMED 12829722
REMARK GeneRIF: the heart is innervated by VR1-expressing afferent nerves
and these afferent nerves are essential for the cardiogenic
sympathoexcitatory reflex during myocardial ischaemia
REFERENCE 7 (residues 1 to 761)
AUTHORS Jung J, Lee SY, Hwang SW, Cho H, Shin J, Kang YS, Kim S and Oh U.
TITLE Agonist recognition sites in the cytosolic tails of vanilloid
receptor 1
JOURNAL J Biol Chem 277 (46), 44448-44454 (2002)
PUBMED 12228246
REMARK GeneRIF: key amino acids, Arg-114 and Glu-761, in the N- and
C-cytosolic tails, respectively, that determine ligand binding were
determined in VRL1
REFERENCE 8 (residues 1 to 761)
AUTHORS Suzuki M, Ohki G, Mochizuki T, Somlo S, Ishibashi K and Imai M.
TITLE Opening of ligand-gated cation channel families by calpain
inhibitors
JOURNAL FEBS Lett 517 (1-3), 219-224 (2002)
PUBMED 12062441
REFERENCE 9 (residues 1 to 761)
AUTHORS Kanzaki M, Zhang YQ, Mashima H, Li L, Shibata H and Kojima I.
TITLE Translocation of a calcium-permeable cation channel induced by
insulin-like growth factor-I
JOURNAL Nat Cell Biol 1 (3), 165-170 (1999)
PUBMED 10559903
REFERENCE 10 (residues 1 to 761)
AUTHORS Caterina MJ, Rosen TA, Tominaga M, Brake AJ and Julius D.
TITLE A capsaicin-receptor homologue with a high threshold for noxious
heat
JOURNAL Nature 398 (6726), 436-441 (1999)
PUBMED 10201375
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
JACYVU010000220.1 and BC089215.1.
Transcript Variant: This variant (3) differs in the 5' UTR compared
to variant 1. All three variants encode the same protein.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: AB029330.1 [ECO:0000332]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..761
/organism="Rattus norvegicus"
/strain="BN"
/db_xref="taxon:10116"
/chromosome="10"
/map="10q23"
Protein 1..761
/product="transient receptor potential cation channel
subfamily V member 2"
/note="VRL-1; OTRPC2; osm-9-like TRP channel 2;
stretch-activated channel 2B; vanilloid receptor-like
protein 1"
/calculated_mol_wt=86599
Region 1..390
/region_name="Required for interaction with SLC50A1.
/evidence=ECO:0000269|PubMed:14991772"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Region 1..49
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 6
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 15
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9WTR1; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
Region 56..75
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Region 71..710
/region_name="TRPV2"
/note="Transient Receptor Potential channel, Vanilloid
subfamily (TRPV), type 2; cd22197"
/db_xref="CDD:411981"
Site 82
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site order(126..127,173..174,206..207,332..338,388,408,
411..412,414,502..503,505..506,509..510,512..513,525,
528..529,532,539,542..543,546,549..551,553..554,556..558,
560..563,598..599,601..602,621..623,626..627,630,636,
638..642,644..645,706,708..710)
/site_type="other"
/note="tetramer interface [polypeptide binding]"
/db_xref="CDD:411981"
Region 164..194
/region_name="ANK repeat"
/note="ANK repeat [structural motif]"
/db_xref="CDD:293786"
Site order(165,169..170,173..175,177..178,182,185,194,209,211,
215..216,219..221,223..224,228,231,243,245,247,251..252,
255..257,268..269,273,276)
/site_type="other"
/note="oligomer interface [polypeptide binding]"
/db_xref="CDD:293786"
Region 209..243
/region_name="ANK repeat"
/note="ANK repeat [structural motif]"
/db_xref="CDD:293786"
Region 245..279
/region_name="ANK repeat"
/note="ANK repeat [structural motif]"
/db_xref="CDD:293786"
Site 393..413
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 434..454
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 461..481
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site order(471..472,475,478,503,506..507,510..511,513..514,517,
526..527,529..530,533..534,537..538,541,663)
/site_type="other"
/note="toxin binding site [chemical binding]"
/db_xref="CDD:411981"
Site 496..516
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 538..558
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Region 564..587
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 571
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 572
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 622..642
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Region 720..761
/region_name="Disordered.
/evidence=ECO:0000256|SAM:MobiDB-lite"
/note="propagated from UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 748
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:Q9WTR1; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
Site 760
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (Q9WUD2.2)"
CDS 1..761
/gene="Trpv2"
/gene_synonym="Vrl1"
/coded_by="NM_001270798.1:327..2612"
/db_xref="GeneID:29465"
/db_xref="RGD:3965"
ORIGIN
1 mtsassppaf rletsdgdee gnaevnkgkq epppmespfq redrnsspqi kvnlnfikrp
61 pkntsapsqq epdrfdrdrl fsvvsrgvpe eltglleylr wnskyltdsa ytegstgktc
121 lmkavlnlqd gvnacimpll qidkdsgnpk plvnaqcide fyqghsalhi aiekrslqcv
181 kllvengadv hlracgrffq khqgtcfyfg elplslaact kqwdvvtyll enphqpasle
241 atdslgntvl halvmiadns pensalvihm ydgllqmgar lcptvqleei snhqgltplk
301 laakegkiei frhilqrefs gpyqplsrkf tewcygpvrv slydlssvds weknsvleii
361 afhckspnrh rmvvleplnk llqekwdrlv srfffnfacy lvymfiftvv ayhqpsldqp
421 aipsskatfg esmlllghil illggiylll gqlwyfwrrr lfiwisfmds yfeilfllqa
481 lltvlsqvlr fmetewylpl lvlslvlgwl nllyytrgfq htgiysvmiq kvilrdllrf
541 llvylvflfg favalvslsr earspkaped nnstvteqpt vgqeeepapy rsildaslel
601 fkftigmgel afqeqlrfrg vvlllllayv lltyvlllnm lialmsetvn hvadnswsiw
661 klqkaisvle mengywwcrr kkhregrllk vgtrgdgtpd erwcfrveev nwvawektlp
721 tlsedpsgpg itgnkknpts kpgknsasee dhlplqvlqs p
//