Transient receptor potential cation channel subfamily V member 4

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Q9ERZ8 (TRPV4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	871 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity. Cell junction › adherens 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 process	Calcium transport Ion transport Transport
Cellular component	Cell junction Cell membrane Membrane
Domain	ANK repeat Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Calcium Calmodulin-binding Nucleotide-binding
Molecular function	Calcium channel Ion channel
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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: Compara cortical microtubule organization Inferred from direct assay PubMed 20657843. Source: BHF-UCL elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara hyperosmotic salinity response Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara vasopressin secretion Inferred from electronic annotation. Source: Compara
Cellular_component	cilium Inferred from electronic annotation. Source: Compara cortical actin cytoskeleton Inferred from direct assay PubMed 20657843. Source: BHF-UCL 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW lamellipodium Inferred from direct assay PubMed 20657843. Source: BHF-UCL ruffle membrane Inferred from direct assay PubMed 20657843. Source: BHF-UCL
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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 microtubule binding Inferred from direct assay PubMed 20657843. Source: BHF-UCL osmosensor activity Inferred from electronic annotation. Source: Compara protein kinase C binding Inferred from direct assay PubMed 20657843. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 871

871

Transient receptor potential cation channel subfamily V member 4

PRO_0000215349

Regions

Topological domain

1 – 465

465

Cytoplasmic Potential

Transmembrane

466 – 486

Helical; Potential

Topological domain

487 – 508

Extracellular Potential

Transmembrane

509 – 529

Helical; Potential

Topological domain

530 – 550

Cytoplasmic Potential

Transmembrane

551 – 571

Helical; Potential

Topological domain

572

Extracellular Potential

Transmembrane

573 – 593

Helical; Potential

Topological domain

594 – 616

Cytoplasmic Potential

Transmembrane

617 – 637

Helical; Potential

Intramembrane

648 – 678

Pore-forming; Probable

Transmembrane

691 – 711

Helical; Potential

Topological domain

712 – 871

160

Cytoplasmic Potential

Repeat

237 – 266

ANK 1

Repeat

284 – 313

ANK 2

Repeat

369 – 398

ANK 3

Region

812 – 831

Interaction with calmodulin By similarity

Sites

Binding site

192

ATP By similarity

Binding site

201

ATP By similarity

Binding site

239

ATP By similarity

Binding site

248

ATP By similarity

Amino acid modifications

Modified residue

824

Phosphoserine; by PKC and PKA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ERZ8 [UniParc].

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

FASTA

871

98,010

        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

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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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF263521 mRNA. Translation: AAG28027.1.
IPI	IPI00191593.
RefSeq	NP_076460.1. NM_023970.1.
UniGene	Rn.64508.
3D structure databases
ProteinModelPortal	Q9ERZ8.
SMR	Q9ERZ8. Positions 149-393.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000001586.
Protein family/group databases
TCDB	1.A.4.2.5. transient receptor potential Ca2+ channel (TRP-CC) family.
PTM databases
PhosphoSite	Q9ERZ8.
Proteomic databases
PaxDb	Q9ERZ8.
PRIDE	Q9ERZ8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000001586; ENSRNOP00000001586; ENSRNOG00000001195.
GeneID	66026.
KEGG	rno:66026.
UCSC	RGD:69337. rat.
Organism-specific databases
CTD	59341.
RGD	69337. Trpv4.
Phylogenomic databases
eggNOG	NOG278734.
GeneTree	ENSGT00550000074425.
HOGENOM	HOG000234630.
HOVERGEN	HBG054085.
InParanoid	Q9ERZ8.
KO	K04973.
OMA	EDPGKSE.
OrthoDB	EOG4JQ3WW.
Gene expression databases
Genevestigator	Q9ERZ8.
GermOnline	ENSRNOG00000001195. Rattus norvegicus.
Family and domain databases
Gene3D	1.25.40.20. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR005821. Ion_trans_dom. IPR004729. TRP_channel. IPR008347. TRPV1-4_channel. IPR008348. TRPV4_channel. IPR024862. TRPV_channel. [Graphical view]
PANTHER	PTHR10582. PTHR10582. 1 hit. PTHR10582:SF4. PTHR10582:SF4. 1 hit.
Pfam	PF00023. Ank. 1 hit. PF00520. Ion_trans. 1 hit. [Graphical view]
PRINTS	PR01768. TRPVRECEPTOR. PR01769. VRL2RECEPTOR.
SMART	SM00248. ANK. 3 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
TIGRFAMs	TIGR00870. trp. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9ERZ8.
ChEMBL	CHEMBL2775.
NextBio	614333.

Entry information

Entry name

TRPV4_RAT

Accession

Primary (citable) accession number: Q9ERZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents