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Q9EPK8

- TRPV4_MOUSE

UniProt

Q9EPK8 - TRPV4_MOUSE

Protein

Transient receptor potential cation channel subfamily V member 4

Gene

Trpv4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    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 similarity3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei192 – 1921ATPBy similarity
    Binding sitei201 – 2011ATPBy similarity
    Binding sitei239 – 2391ATPBy similarity
    Binding sitei248 – 2481ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium channel activity Source: UniProtKB
    3. calmodulin binding Source: UniProtKB
    4. cation channel activity Source: UniProtKB
    5. osmosensor activity Source: MGI
    6. protein binding Source: UniProtKB
    7. protein kinase binding Source: BHF-UCL
    8. SH2 domain binding Source: BHF-UCL

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: Ensembl
    2. actin filament organization Source: Ensembl
    3. calcium ion import Source: BHF-UCL
    4. cell-cell junction assembly Source: UniProtKB
    5. cellular calcium ion homeostasis Source: UniProtKB
    6. cellular hypotonic response Source: BHF-UCL
    7. cellular response to heat Source: UniProtKB
    8. cellular response to osmotic stress Source: UniProtKB
    9. cortical microtubule organization Source: Ensembl
    10. hyperosmotic salinity response Source: MGI
    11. microtubule polymerization Source: Ensembl
    12. negative regulation of neuron projection development Source: Ensembl
    13. osmosensory signaling pathway Source: BHF-UCL
    14. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    15. positive regulation of microtubule depolymerization Source: Ensembl
    16. regulation of response to osmotic stress Source: MGI
    17. response to osmotic stress Source: MGI
    18. vasopressin secretion Source: MGI

    Keywords - Molecular functioni

    Calcium channel, Ion channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_227861. TRP channels.

    Names & Taxonomyi

    Protein namesi
    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
    Transient receptor potential protein 12
    Short name:
    TRP12
    Vanilloid receptor-like channel 2
    Vanilloid receptor-like protein 2
    Vanilloid receptor-related osmotically-activated channel
    Short name:
    VR-OAC
    Gene namesi
    Name:Trpv4
    Synonyms:Trp12, Vrl2, Vroac
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1926945. Trpv4.

    Subcellular locationi

    GO - Cellular componenti

    1. adherens junction Source: UniProtKB
    2. cell surface Source: Ensembl
    3. cilium Source: MGI
    4. cortical actin cytoskeleton Source: Ensembl
    5. cytoplasmic microtubule Source: Ensembl
    6. cytoplasmic vesicle Source: Ensembl
    7. filopodium Source: Ensembl
    8. focal adhesion Source: Ensembl
    9. growth cone Source: Ensembl
    10. integral component of membrane Source: UniProtKB-KW
    11. lamellipodium Source: Ensembl
    12. plasma membrane Source: UniProtKB
    13. ruffle membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice display impairment of the intercellular junction-dependent barrier function in the skin.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi142 – 1432PP → AL: Strongly reduced interaction with PACSIN3. 1 Publication
    Mutagenesisi253 – 2531Y → F: Abolishes hypotonicity-dependent channel activity. 2 Publications
    Mutagenesisi672 – 6721D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682. 2 Publications
    Mutagenesisi675 – 6751K → A: No effect on channel pore properties. 2 Publications
    Mutagenesisi680 – 6801M → A: Impairs Ca(2+) permeation. 2 Publications
    Mutagenesisi682 – 6821D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 871871Transient receptor potential cation channel subfamily V member 4PRO_0000215348Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei253 – 2531Phosphotyrosine; by LYN1 Publication
    Modified residuei824 – 8241Phosphoserine; by PKC and PKABy similarity

    Post-translational modificationi

    Phosphorylation results in enhancement of its channel function.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9EPK8.
    PRIDEiQ9EPK8.

    PTM databases

    PhosphoSiteiQ9EPK8.

    Expressioni

    Tissue specificityi

    Detected in liver, kidney, heart, brain cortex, cerebellum and brainstem (at protein level). Expressed in heart, lung, spleen, liver, kidney, brain, skeletal muscle 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.5 Publications

    Gene expression databases

    ArrayExpressiQ9EPK8.
    BgeeiQ9EPK8.
    GenevestigatoriQ9EPK8.

    Interactioni

    Subunit structurei

    Interacts with calmodulin By similarity. Interacts with CTNNB1. The TRPV4 and CTNNB1 complex can interact with CDH1. Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1 By similarity. Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES. Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain).By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UBCP0CG483EBI-7091763,EBI-3390054From a different organism.

    Protein-protein interaction databases

    DIPiDIP-44011N.
    IntActiQ9EPK8. 2 interactions.
    MINTiMINT-4050076.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EPK8.
    SMRiQ9EPK8. Positions 148-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 465465CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini487 – 50822ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini530 – 55021CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini572 – 5721ExtracellularSequence Analysis
    Topological domaini594 – 61623CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini712 – 871160CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei648 – 67831Pore-formingCuratedAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei466 – 48621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei509 – 52921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei551 – 57121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei573 – 59321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei617 – 63721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei691 – 71121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati237 – 26630ANK 1Add
    BLAST
    Repeati284 – 31330ANK 2Add
    BLAST
    Repeati369 – 39830ANK 3Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni812 – 83120Interaction with calmodulinBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 3 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG278734.
    GeneTreeiENSGT00550000074425.
    HOGENOMiHOG000234630.
    HOVERGENiHBG054085.
    InParanoidiA0JNY0.
    KOiK04973.
    OMAiEDQTNCT.
    OrthoDBiEOG70S74P.
    PhylomeDBiQ9EPK8.
    TreeFamiTF314711.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR008347. TRPV1-4_channel.
    IPR008348. TRPV4_channel.
    [Graphical view]
    PANTHERiPTHR10582:SF4. PTHR10582:SF4. 1 hit.
    PfamiPF12796. Ank_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view]
    PRINTSiPR01768. TRPVRECEPTOR.
    PR01769. VRL2RECEPTOR.
    SMARTiSM00248. ANK. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    TIGRFAMsiTIGR00870. trp. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9EPK8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADPGDGPRA APGEVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS    50
    PVDASRPAGP GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK 100
    KAPMDSLFDY GTYRHHPSDN KRWRRKVVEK QPQSPKAPAP QPPPILKVFN 150
    RPILFDIVSR GSTADLDGLL SFLLTHKKRL TDEEFREPST GKTCLPKALL 200
    NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT SLHIAIERRC 250
    KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI 300
    VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL 350
    LKCSRLFPDS NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR 400
    HLSRKFKDWA YGPVYSSLYD LSSLDTCGEE VSVLEILVYN SKIENRHEML 450
    AVEPINELLR DKWRKFGAVS FYINVVSYLC AMVIFTLTAY YQPLEGTPPY 500
    PYRTTVDYLR LAGEVITLFT GVLFFFTSIK DLFTKKCPGV NSLFVDGSFQ 550
    LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG 600
    TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS 650
    NCTVPTYPAC RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV 700
    TYIILTFVLL LNMLIALMGE TVGQVSKESK HIWKLQWATT ILDIERSFPV 750
    FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV DEVNWSHWNQ NLGIINEDPG 800
    KSEIYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSSADE VVVPLDNLGN 850
    PNCDGHQQGY APKWRTDDAP L 871
    Length:871
    Mass (Da):98,027
    Last modified:March 1, 2001 - v1
    Checksum:i5BAC6E33F89CEA05
    GO

    Sequence cautioni

    The sequence AAG28028.1 differs from that shown. Reason: Frameshift at positions 47, 50, 53, 72 and 73.
    The sequence AAK69486.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451G → S in AAG28028. (PubMed:11081638)Curated
    Sequence conflicti90 – 901L → R in AAG17543. (PubMed:11025659)Curated
    Sequence conflicti90 – 901L → R in AAK69486. 1 PublicationCurated
    Sequence conflicti137 – 1371A → T in BAA83731. (PubMed:12692122)Curated
    Sequence conflicti210 – 2112IP → LQ in BAA83731. (PubMed:12692122)Curated
    Sequence conflicti477 – 4771S → P in AAG28028. (PubMed:11081638)Curated
    Sequence conflicti784 – 7841N → S in BAA83731. (PubMed:12692122)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS19568.1.
    RefSeqiNP_071300.2. NM_022017.3.
    UniGeneiMm.266450.

    Genome annotation databases

    EnsembliENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158.
    ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158.
    GeneIDi63873.
    KEGGimmu:63873.
    UCSCiuc008yzu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS19568.1.
    RefSeqi NP_071300.2. NM_022017.3.
    UniGenei Mm.266450.

    3D structure databases

    ProteinModelPortali Q9EPK8.
    SMRi Q9EPK8. Positions 148-755.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-44011N.
    IntActi Q9EPK8. 2 interactions.
    MINTi MINT-4050076.

    Chemistry

    BindingDBi Q9EPK8.
    ChEMBLi CHEMBL6126.
    GuidetoPHARMACOLOGYi 510.

    PTM databases

    PhosphoSitei Q9EPK8.

    Proteomic databases

    PaxDbi Q9EPK8.
    PRIDEi Q9EPK8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000071968 ; ENSMUSP00000071859 ; ENSMUSG00000014158 .
    ENSMUST00000112225 ; ENSMUSP00000107844 ; ENSMUSG00000014158 .
    GeneIDi 63873.
    KEGGi mmu:63873.
    UCSCi uc008yzu.1. mouse.

    Organism-specific databases

    CTDi 59341.
    MGIi MGI:1926945. Trpv4.

    Phylogenomic databases

    eggNOGi NOG278734.
    GeneTreei ENSGT00550000074425.
    HOGENOMi HOG000234630.
    HOVERGENi HBG054085.
    InParanoidi A0JNY0.
    KOi K04973.
    OMAi EDQTNCT.
    OrthoDBi EOG70S74P.
    PhylomeDBi Q9EPK8.
    TreeFami TF314711.

    Enzyme and pathway databases

    Reactomei REACT_227861. TRP channels.

    Miscellaneous databases

    NextBioi 319803.
    PROi Q9EPK8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EPK8.
    Bgeei Q9EPK8.
    Genevestigatori Q9EPK8.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR008347. TRPV1-4_channel.
    IPR008348. TRPV4_channel.
    [Graphical view ]
    PANTHERi PTHR10582:SF4. PTHR10582:SF4. 1 hit.
    Pfami PF12796. Ank_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR01768. TRPVRECEPTOR.
    PR01769. VRL2RECEPTOR.
    SMARTi SM00248. ANK. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    TIGRFAMsi TIGR00870. trp. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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], TISSUE SPECIFICITY.
      Tissue: Hypothalamus.
    2. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYN; SRC; FYN; HCK; LCK AND YES, PHOSPHORYLATION AT TYR-253, MUTAGENESIS OF TYR-253.
    10. "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: SUBCELLULAR LOCATION, INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3, MUTAGENESIS OF 142-PRO-PRO-143, TISSUE SPECIFICITY.
    11. "Stimulus-specific modulation of the cation channel TRPV4 by PACSIN 3."
      D'hoedt D., Owsianik G., Prenen J., Cuajungco M.P., Grimm C., Heller S., Voets T., Nilius B.
      J. Biol. Chem. 283:6272-6280(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PACSIN3.
    12. "The TRPV4 channel contributes to intercellular junction formation in keratinocytes."
      Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.
      J. Biol. Chem. 285:18749-18758(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH CTNBB1 AND CDH1.

    Entry informationi

    Entry nameiTRPV4_MOUSE
    AccessioniPrimary (citable) accession number: Q9EPK8
    Secondary accession number(s): A0JNY0
    , Q91XR5, Q9EQZ4, Q9ERZ7, Q9ES76
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3