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Q9ERZ8 (TRPV4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transient receptor potential cation channel subfamily V member 4

Short name=TrpV4
Alternative name(s):
Osm-9-like TRP channel 4
Short name=OTRPC4
Vanilloid receptor-related osmotically-activated channel
Short name=VR-OAC
Gene names
Name:Trpv4
Synonyms:Vroac
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length871 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Non-selective calcium permeant cation channel probably involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by low pH, citrate and phorbol esters. Increase of intracellular Ca2+ potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism. Acts as a regulator of intracellular Ca2+ in synoviocytes. Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 By similarity. Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers By similarity. Ref.1

Subunit structure

Interacts with calmodulin. Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES. Interacts with CTNNB1. The TRPV4 and CTNNB1 complex can interact with CDH1 By similarity. Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1 By similarity. Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain). Ref.2

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity. Cell junctionadherens junction By similarity. Note: Assembly of the putative homotetramer occurs primarily in the endoplasmic reticulum By similarity.

Tissue specificity

Expressed lung, spleen, kidney, testis, fat, and at very low levels in trigeminal ganglia. Ref.1

Post-translational modification

Phosphorylation results in enhancement of its channel function By similarity.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily. [View classification]

Contains 3 ANK repeats.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
   DomainANK repeat
Repeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Calmodulin-binding
Nucleotide-binding
   Molecular functionCalcium channel
Ion channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

actin filament organization

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

calcium ion import

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

cell-cell junction assembly

Inferred from sequence or structural similarity. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular hypotonic response

Inferred from electronic annotation. Source: Ensembl

cellular response to heat

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to osmotic stress

Inferred from sequence or structural similarity. Source: UniProtKB

cortical microtubule organization

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

hyperosmotic salinity response

Inferred from electronic annotation. Source: Ensembl

hypotonic response

Inferred from direct assay Ref.1. Source: RGD

microtubule polymerization

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

negative regulation of neuron projection development

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

osmosensory signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Inferred from direct assay PubMed 20650893. Source: RGD

positive regulation of microtubule depolymerization

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

regulation of response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

vasopressin secretion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentadherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 20650893. Source: RGD

cilium

Inferred from electronic annotation. Source: Ensembl

cortical actin cytoskeleton

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

cytoplasmic vesicle

Inferred from direct assay PubMed 20650893. Source: RGD

filopodium

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

focal adhesion

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

growth cone

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle membrane

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

actin binding

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

actin filament binding

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

alpha-tubulin binding

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

beta-tubulin binding

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

calcium channel activity

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

calmodulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

cation channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule binding

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

osmosensor activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 20650893. Source: RGD

protein kinase C binding

Inferred from direct assay PubMed 20657843. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 871871Transient receptor potential cation channel subfamily V member 4
PRO_0000215349

Regions

Topological domain1 – 465465Cytoplasmic Potential
Transmembrane466 – 48621Helical; Potential
Topological domain487 – 50822Extracellular Potential
Transmembrane509 – 52921Helical; Potential
Topological domain530 – 55021Cytoplasmic Potential
Transmembrane551 – 57121Helical; Potential
Topological domain5721Extracellular Potential
Transmembrane573 – 59321Helical; Potential
Topological domain594 – 61623Cytoplasmic Potential
Transmembrane617 – 63721Helical; Potential
Intramembrane648 – 67831Pore-forming; Probable
Transmembrane691 – 71121Helical; Potential
Topological domain712 – 871160Cytoplasmic Potential
Repeat237 – 26630ANK 1
Repeat284 – 31330ANK 2
Repeat369 – 39830ANK 3
Region812 – 83120Interaction with calmodulin By similarity

Sites

Binding site1921ATP By similarity
Binding site2011ATP By similarity
Binding site2391ATP By similarity
Binding site2481ATP By similarity

Amino acid modifications

Modified residue8241Phosphoserine; by PKC and PKA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ERZ8 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5D50684DA08C354B

FASTA87198,010
        10         20         30         40         50         60 
MADPGDGPRA APGDVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS PVDASRPAGP 

        70         80         90        100        110        120 
GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK KAPMDSLFDY GTYRHHPSDN 

       130        140        150        160        170        180 
KRWRRKVVEK QPQSPKAPAP QPPPILKVFN RPILFDIVSR GSTADLDGLL SYLLTHKKRL 

       190        200        210        220        230        240 
TDEEFREPST GKTCLPKALL NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT 

       250        260        270        280        290        300 
ALHIAIERRC KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 

       310        320        330        340        350        360 
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL LKCSRLFPDS 

       370        380        390        400        410        420 
NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR HLSRKFKDWA YGPVYSSLYD 

       430        440        450        460        470        480 
LSSLDTCGEE VSVLEILVYN SKIENRHEML AVEPINELLR DKWRKFGAVS FYINVVSYLC 

       490        500        510        520        530        540 
AMVIFTLTAY YQPLEGTPPY PYRTTVDYLR LAGEVITLLT GVLFFFTSIK DLFMKKCPGV 

       550        560        570        580        590        600 
NSLFVDGSFQ LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 

       610        620        630        640        650        660 
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCNEDQS NCTVPSYPAC 

       670        680        690        700        710        720 
RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV TYIILTFVLL LNMLIALMGE 

       730        740        750        760        770        780 
TVGQVSKESK HIWKLQWATT ILDIERSFPV FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV 

       790        800        810        820        830        840 
DEVNWSHWNQ NLGIINEDPG KSEIYQYYGF SHTMGRLRRD RWSSVVPRVV ELNKNSGTDE 

       850        860        870 
VVVPLDNLGN PNCDGHQQGY APKWRAEDAP L 

« Hide

References

[1]"Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor."
Liedtke W.B., Choe Y., Marti-Renom M.A., Bell A.M., Denis C.S., Sali A., Hudspeth A.J., Friedman J.M., Heller S.
Cell 103:525-535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"PACSINs bind to the TRPV4 cation channel. PACSIN 3 modulates the subcellular localization of TRPV4."
Cuajungco M.P., Grimm C., Oshima K., D'hoedt D., Nilius B., Mensenkamp A.R., Bindels R.J., Plomann M., Heller S.
J. Biol. Chem. 281:18753-18762(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF263521 mRNA. Translation: AAG28027.1.
RefSeqNP_076460.1. NM_023970.1.
XP_006249528.1. XM_006249466.1.
UniGeneRn.64508.

3D structure databases

ProteinModelPortalQ9ERZ8.
SMRQ9ERZ8. Positions 149-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249353. 3 interactions.
DIPDIP-59600N.
STRING10116.ENSRNOP00000001586.

Chemistry

BindingDBQ9ERZ8.
ChEMBLCHEMBL2775.
GuidetoPHARMACOLOGY510.

Protein family/group databases

TCDB1.A.4.2.5. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteQ9ERZ8.

Proteomic databases

PaxDbQ9ERZ8.
PRIDEQ9ERZ8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001586; ENSRNOP00000001586; ENSRNOG00000001195.
GeneID66026.
KEGGrno:66026.
UCSCRGD:69337. rat.

Organism-specific databases

CTD59341.
RGD69337. Trpv4.

Phylogenomic databases

eggNOGNOG278734.
GeneTreeENSGT00550000074425.
HOGENOMHOG000234630.
HOVERGENHBG054085.
InParanoidQ9ERZ8.
KOK04973.
OMAEDQTNCT.
OrthoDBEOG70S74P.
PhylomeDBQ9ERZ8.
TreeFamTF314711.

Gene expression databases

GenevestigatorQ9ERZ8.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR008348. TRPV4_channel.
[Graphical view]
PANTHERPTHR10582:SF4. PTHR10582:SF4. 1 hit.
PfamPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01768. TRPVRECEPTOR.
PR01769. VRL2RECEPTOR.
SMARTSM00248. ANK. 3 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

NextBio614333.
PROQ9ERZ8.

Entry information

Entry nameTRPV4_RAT
AccessionPrimary (citable) accession number: Q9ERZ8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families