Transient receptor potential cation channel subfamily V member 4

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Reviewed, UniProtKB/Swiss-Prot Q9EPK8 (TRPV4_MOUSE)

Last modified February 9, 2010. Version 69. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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-like channel 2
    Vanilloid receptor-like protein 2
    Vanilloid receptor-related osmotically-activated channel
      Short name=VR-OAC
    Transient receptor potential protein 12
      Short name=TRP12

Gene names

Name:	Trpv4
Synonyms:	Trp12, Vrl2, Vroac

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	871 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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. Ref.2
Subunit structure	Interacts with calmodulin By similarity. Interacts with Map7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES. Ref.8 Ref.9
Subcellular location	Membrane; Multi-pass membrane protein Probable.
Tissue specificity	Expressed heart, liver, kidney and testis. In the central nervous system, expressed in the lamina terminalis (arched vascular organ and neurons of the subfornical organ), median preoptic area, ventral hippocampal commissure, and ependymal cells of the choroid plexus. In the cochlea, expressed in both inner and outer hair cells, and in marginal cells of the cochlear stria vascularis. Expressed in large neurons of the trigeminal ganglion. In the kidney cortex, strongly expressed by epithelial cells of tubules and much weaker in glomeruli. Ref.2 Ref.1 Ref.3 Ref.4
Sequence similarities	Belongs to the transient receptor family. TrpV subfamily. Contains 3 ANK repeats.
Sequence caution	The sequence AAG28028.1 differs from that shown. Reason: Frameshift at positions 47, 50, 53, 72 and 73.

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Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Membrane
Domain	ANK repeat Repeat Transmembrane
Ligand	Calcium Calmodulin-binding
Molecular function	Calcium channel Ionic channel
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	calcium ion transport Inferred from electronic annotation. Source: UniProtKB-KW hyperosmotic salinity response Inferred from mutant phenotype. Source: MGI osmosensory signaling pathway Ref.3 Inferred from direct assay. Source: MGI regulation of response to osmotic stress Inferred from mutant phenotype. Source: MGI transmembrane transport Inferred from electronic annotation. Source: InterPro vasopressin secretion Inferred from mutant phenotype. Source: MGI
Cellular component	cilium Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.8 Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	calcium channel activity Ref.3 Ref.8 Inferred from direct assay. Source: MGI calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Inferred from sequence or structural similarity. Source: UniProtKB osmosensor activity Ref.3 Inferred from direct assay. Source: MGI
Complete GO annotation...

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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_0000215348

Regions

Topological domain

1 – 465

465

Cytoplasmic Potential

Transmembrane

466 – 486

Potential

Topological domain

487 – 508

Extracellular Potential

Transmembrane

509 – 529

Potential

Topological domain

530 – 550

Cytoplasmic Potential

Transmembrane

551 – 571

Potential

Topological domain

572

Extracellular Potential

Transmembrane

573 – 593

Potential

Topological domain

594 – 616

Cytoplasmic Potential

Transmembrane

617 – 637

Potential

Topological domain

638 – 690

Pore forming Probable

Transmembrane

691 – 711

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

Amino acid modifications

Modified residue

253

Phosphotyrosine; by LYN Probable

Experimental info

Mutagenesis

253

Y → F: Abolishes hypotonicity-dependent channel activity. Ref.9

Mutagenesis

672

D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682. Ref.7

Mutagenesis

675

K → A: No effect on channel pore properties. Ref.7

Mutagenesis

680

M → A: Impairs Ca(2+) permeation. Ref.7

Mutagenesis

682

D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672. Ref.7

Sequence conflict

G → S in AAG28028. Ref.1

Sequence conflict

L → R Ref.3

Sequence conflict

L → R Ref.5

Sequence conflict

137

A → T in BAA83731. Ref.4

Sequence conflict

210 – 211

IP → LQ in BAA83731. Ref.4

Sequence conflict

477

S → P in AAG28028. Ref.1

Sequence conflict

784

N → S in BAA83731. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9EPK8-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5BAC6E33F89CEA05
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FASTA

871

98,027

        10         20         30         40         50         60 
MADPGDGPRA APGEVAEPPG 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 SFLLTHKKRL 

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

       250        260        270        280        290        300 
SLHIAIERRC 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 LAGEVITLFT GVLFFFTSIK DLFTKKCPGV 

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

       610        620        630        640        650        660 
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS NCTVPTYPAC 

       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 SHTVGRLRRD RWSSVVPRVV ELNKNSSADE 

       850        860        870 
VVVPLDNLGN PNCDGHQQGY APKWRTDDAP L

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References

	« Hide 'large scale' referencesShow 'large scale' 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: 11081638] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Hypothalamus.
[2]	"Trp12, a novel Trp related protein from kidney." Wissenbach U., Boedding M., Freichel M., Flockerzi V. FEBS Lett. 485:127-134(2000) [PubMed: 11094154] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Kidney.
[3]	"OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity." Strotmann R., Harteneck C., Nunnenmacher K., Schultz G., Plant T.D. Nat. Cell Biol. 2:695-702(2000) [PubMed: 11025659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: 129/SvEv.
[4]	"Impaired pressure sensation in mice lacking TRPV4." Suzuki M., Mizuno A., Kodaira K., Imai M. J. Biol. Chem. 278:22664-22668(2003) [PubMed: 12692122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Kidney.
[5]	"Cloning of mouse and human vanilloid receptor-like protein 2 (VRL-2)." Derst C., Schafer M.K. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[6]	"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].
[7]	"Molecular determinants of permeation through the cation channel TRPV4." Voets T., Prenen J., Vriens J., Watanabe H., Janssens A., Wissenbach U., Bodding M., Droogmans G., Nilius B. J. Biol. Chem. 277:33704-33710(2002) [PubMed: 12093812] [Abstract] Cited for: CHARACTERIZATION OF CHANNEL PORE, MUTAGENESIS OF ASP-672; LYS-675; MET-680 AND ASP-682.
[8]	"Microtubule-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4)." Suzuki M., Hirao A., Mizuno A. J. Biol. Chem. 278:51448-51453(2003) [PubMed: 14517216] [Abstract] Cited for: INTERACTION WITH MAP7.
[9]	"Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress." Xu H., Zhao H., Tian W., Yoshida K., Roullet J.B., Cohen D.M. J. Biol. Chem. 278:11520-11527(2003) [PubMed: 12538589] [Abstract] Cited for: INTERACTION WITH LYN; SRC; FYN; HCK; LCK AND YES, PHOSPHORYLATION AT TYR-253, MUTAGENESIS OF TYR-253.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF263522 mRNA. Translation: AAG28028.1. Frameshift. AJ296078 mRNA. Translation: CAC20703.1. AF208026 mRNA. Translation: AAG17543.1. AB021875 mRNA. Translation: BAA83731.2. AF279672 mRNA. Translation: AAK69486.1. Different initiation. BC127052 mRNA. Translation: AAI27053.1.
IPI	IPI00112949.
RefSeq	NP_071300.2.
UniGene	Mm.266450
3D structure databases
SMR	Q9EPK8. Positions 149-393.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9EPK8.
PTM databases
PhosphoSite	Q9EPK8.
Proteomic databases
PRIDE	Q9EPK8.
Genome annotation databases
Ensembl	ENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158; Mus musculus. [Genome view] ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158; Mus musculus. [Genome view]
GeneID	63873.
KEGG	mmu:63873.
Organism-specific databases
CTD	63873.
MGI	MGI:1926945. Trpv4.
Phylogenomic databases
HOGENOM	HBG446456.
HOVERGEN	Q9EPK8.
InParanoid	Q9EPK8.
OMA	ESTLYES.
OrthoDB	EOG9SR0FX.
PhylomeDB	Q9EPK8.
Gene expression databases
ArrayExpress	Q9EPK8.
Bgee	Q9EPK8.
Genevestigator	Q9EPK8.
GermOnline	ENSMUSG00000014158. Mus musculus.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR005821. Ion_trans. IPR004729. TRP_channel. IPR008347. Vanilpoid_rcpt. IPR008348. Vanilpoid_rcpt_2. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 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]
TIGRFAMs	TIGR00870. trp. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	319803.
SOURCE	Search...

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Entry information

Entry name

TRPV4_MOUSE

Accession

Primary (citable) accession number: Q9EPK8
Secondary accession number(s): A0JNY0

Q9ES76

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents