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Q9ESQ5

- TRPM4_RAT

UniProt

Q9ESQ5 - TRPM4_RAT

Protein

Transient receptor potential cation channel subfamily M member 4

Gene

Trpm4

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
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    Functioni

    Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca2+, it is impermeable to it. Mediates transport of monovalent cations (Na+ > K+ > Cs+ > Li+), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca2+ oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca2+ overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. Essential for the migration but not the maturation of dendritic cells By similarity.By similarity

    Enzyme regulationi

    Gating is voltage-dependent and repressed by decavanadate. Calmodulin-binding confers the Ca2+ sensitivity. ATP is able to restore Ca2+ sensitivity after desensitization. Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances activity, by increasing the channel's Ca2+ sensitivity and shifting its voltage dependence of activation towards negative potentials. Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole derivative (BTP2) By similarity.By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium activated cation channel activity Source: UniProtKB
    3. calcium channel activity Source: Ensembl

    GO - Biological processi

    1. dendritic cell chemotaxis Source: UniProtKB
    2. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    3. positive regulation of cell proliferation Source: UniProtKB
    4. protein sumoylation Source: UniProtKB
    5. regulation of T cell cytokine production Source: UniProtKB

    Keywords - Molecular functioni

    Ion channel

    Keywords - Biological processi

    Adaptive immunity, Immunity, Ion transport, Transport

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_198388. TRP channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transient receptor potential cation channel subfamily M member 4
    Alternative name(s):
    Calcium-activated non-selective cation channel 1
    Long transient receptor potential channel 4
    Short name:
    LTrpC-4
    Short name:
    LTrpC4
    MLS2s
    Melastatin-like 2
    Gene namesi
    Name:Trpm4
    Synonyms:Ltrpc4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi620244. Trpm4.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. Golgi apparatus Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12081208Transient receptor potential cation channel subfamily M member 4PRO_0000259531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1139 – 11391Phosphoserine; by PKCBy similarity
    Modified residuei1146 – 11461Phosphoserine; by PKCBy similarity

    Post-translational modificationi

    Sumoylated. Desumoylated by SENP1 By similarity.By similarity
    Phosphorylation by PKC leads to increase the sensitivity to Ca2+.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9ESQ5.
    PRIDEiQ9ESQ5.

    Expressioni

    Tissue specificityi

    Isoform 1 is highly expressed in the testis with a moderate expression in the brain, spleen and thymus. Isoform 2 is only expressed in the brain and spleen.1 Publication

    Gene expression databases

    GenevestigatoriQ9ESQ5.

    Interactioni

    Subunit structurei

    Homomultimer.By similarity

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 687687CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini709 – 77668ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini798 – 7981CytoplasmicSequence Analysis
    Topological domaini820 – 88667ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini908 – 92417CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini946 – 95914ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini988 – 101326ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1035 – 1208174CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei960 – 98728Pore-formingSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei688 – 70821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei777 – 79721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei799 – 81921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei887 – 90721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei925 – 94521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1014 – 103421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1070 – 1170101Calmodulin-bindingBy similarityAdd
    BLAST
    Regioni1130 – 11356Mediates modulation by decavanadate and PIP2-bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1128 – 118053Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi975 – 9806Selectivity filterBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG253824.
    GeneTreeiENSGT00650000093200.
    HOGENOMiHOG000236350.
    HOVERGENiHBG108337.
    InParanoidiQ9ESQ5.
    KOiK04979.
    OMAiRTWGFRA.
    OrthoDBiEOG725DH1.
    PhylomeDBiQ9ESQ5.
    TreeFamiTF314204.

    Family and domain databases

    InterProiIPR005821. Ion_trans_dom.
    IPR029581. TRPM4.
    [Graphical view]
    PANTHERiPTHR13800:SF6. PTHR13800:SF6. 1 hit.
    PfamiPF00520. Ion_trans. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms may exist.

    Isoform 1 (identifier: Q9ESQ5-1) [UniParc]FASTAAdd to Basket

    Also known as: TRPM4b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVGQEKEQSW IPKIFRKKVC TTFIVDLHDD AGGTLCQCGQ PRDAHPSVAV     50
    EDAFGAAVVT EWNSDEHTTE KPTDAYGDLD FTYSGRKSSN FLRLSDRTDP 100
    ATVYSLVTRS WGFRAPNLVV SVLGGSEGPV LQTWLQDLLR RGLVRAAQST 150
    GAWIVTGGLH TGIGRHVGVA VRDHQTASTG GSKVVAMGVA PWGVVRNRDM 200
    LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT YGRMGGENRF 250
    RLRFESYVAQ QKTGVGGTGI DIPVLLLLIE GDEKMLKRIE DATQAQLPCL 300
    LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA 350
    QVERIMTRKE LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL 400
    AVAWNRVDIA QSELFRGDIQ WRSFHLEASL MDALLNDRPE FVRLLISHGL 450
    SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ ASHASSSKSP PANGAAELRP 500
    PNVGQVLRTL LGETCAPRYP ARNTRHSLLG QDHRENDSLL MDWANMQQDA 550
    SFEQAPWSDL LIWALLLNRA QMAIYFWEKG SNSVASALGA CLLLRVMARL 600
    EWEAEEAARR KDLAAKFESM SVDLFGECYH NSEYRAARLL LRRCPLWGEA 650
    TCLQLAMQAD ARAFFAQDGV QSLLTQKWWG EMDSTNPIWA LLLTFFCPPL 700
    IYTNLILFRK SEEEPTQKDL DFDMDSSMNG AGPLGPAEPS AKVALERRRR 750
    RRPGHTLCCG GCSKRWSYFW GAPVTAFLGN VVSYLLFLLL FAHVLLVDFQ 800
    PTKPGVFELL LYFWAFTLLC EELRQGLGGG WGTLANGGPG PGKAPLRHRL 850
    HLYLLDTWNQ CDLLALTCFL LGVGCRLTPG LFDLGRTVLC LDFMIFTLRL 900
    LHIFTVNKQL GPKIVIVSKM MKDVFFFLFF LCVWLVAYGV ATEGILRPQD 950
    RSLPSILRRV FYRPYLQIFG QIPQEEMDVA LMNPSNCSAE RGSWAHPEGP 1000
    VAGSCVSQYA NWLVVLLLIV FLLVANILLL NLLIAMFSYT FNKVHGNSDL 1050
    YWKAQRYSLI REFHSRPALA PPLIIISHLR LLFKWLRRCH RTNLPASPVF 1100
    EHFRVCLSKE AERTLLTWES VHKENFLLAQ ARDKRDSDSE RLKRTSQKVD 1150
    TALKQLGQIR EYDRRLRGLE REVQHCSRVL TWMAEALSHS ALLPPGGPPP 1200
    PSPTGSKD 1208
    Length:1,208
    Mass (Da):135,341
    Last modified:October 31, 2006 - v2
    Checksum:i324CEC9A6B9F7EA6
    GO
    Isoform 2 (identifier: Q9ESQ5-2) [UniParc]FASTAAdd to Basket

    Also known as: TRPM4a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-186: Missing.

    Note: Probably non-functional.

    Show »
    Length:1,022
    Mass (Da):115,277
    Checksum:i68246240BDC5FECB
    GO

    Sequence cautioni

    The sequence BAB15808.1 differs from that shown. Reason: Chimeric cDNA.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 186186Missing in isoform 2. 1 PublicationVSP_040337Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03000917 Genomic DNA. No translation available.
    AABR03004552 Genomic DNA. No translation available.
    AB040807 mRNA. Translation: BAB15808.1. Sequence problems.
    RefSeqiNP_001129701.1. NM_001136229.1. [Q9ESQ5-1]
    UniGeneiRn.205004.

    Genome annotation databases

    EnsembliENSRNOT00000041513; ENSRNOP00000041387; ENSRNOG00000020714. [Q9ESQ5-1]
    GeneIDi171143.
    KEGGirno:171143.
    UCSCiRGD:620244. rat. [Q9ESQ5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03000917 Genomic DNA. No translation available.
    AABR03004552 Genomic DNA. No translation available.
    AB040807 mRNA. Translation: BAB15808.1 . Sequence problems.
    RefSeqi NP_001129701.1. NM_001136229.1. [Q9ESQ5-1 ]
    UniGenei Rn.205004.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9ESQ5.
    PRIDEi Q9ESQ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000041513 ; ENSRNOP00000041387 ; ENSRNOG00000020714 . [Q9ESQ5-1 ]
    GeneIDi 171143.
    KEGGi rno:171143.
    UCSCi RGD:620244. rat. [Q9ESQ5-1 ]

    Organism-specific databases

    CTDi 54795.
    RGDi 620244. Trpm4.

    Phylogenomic databases

    eggNOGi NOG253824.
    GeneTreei ENSGT00650000093200.
    HOGENOMi HOG000236350.
    HOVERGENi HBG108337.
    InParanoidi Q9ESQ5.
    KOi K04979.
    OMAi RTWGFRA.
    OrthoDBi EOG725DH1.
    PhylomeDBi Q9ESQ5.
    TreeFami TF314204.

    Enzyme and pathway databases

    Reactomei REACT_198388. TRP channels.

    Miscellaneous databases

    NextBioi 621940.

    Gene expression databases

    Genevestigatori Q9ESQ5.

    Family and domain databases

    InterProi IPR005821. Ion_trans_dom.
    IPR029581. TRPM4.
    [Graphical view ]
    PANTHERi PTHR13800:SF6. PTHR13800:SF6. 1 hit.
    Pfami PF00520. Ion_trans. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "Cloning and characterization of rat transient receptor potential-melastatin 4 (TRPM4)."
      Yoo J.C., Yarishkin O.V., Hwang E.M., Kim E., Kim D.G., Park N., Hong S.G., Park J.Y.
      Biochem. Biophys. Res. Commun. 391:806-811(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Cloning of novel Ca-permeable channels."
      Ohki G., Ishibashi K., Suzuki M.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 717-1208.
      Tissue: Brain.
    4. "Activation of the Ca(2+)-activated nonselective cation channel by diacylglycerol analogues in rat cardiomyocytes."
      Guinamard R., Chatelier A., Lenfant J., Bois P.
      J. Cardiovasc. Electrophysiol. 15:342-348(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    5. "Functional expression of the TRPM4 cationic current in ventricular cardiomyocytes from spontaneously hypertensive rats."
      Guinamard R., Demion M., Magaud C., Potreau D., Bois P.
      Hypertension 48:587-594(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiTRPM4_RAT
    AccessioniPrimary (citable) accession number: Q9ESQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 88 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3