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Q9ESQ5

- TRPM4_RAT

UniProt

Q9ESQ5 - TRPM4_RAT

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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

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. cardiac conduction Source: InterPro
  2. dendritic cell chemotaxis Source: UniProtKB
  3. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  4. positive regulation of cell proliferation Source: UniProtKB
  5. protein sumoylation Source: UniProtKB
  6. regulation of membrane potential Source: InterPro
  7. regulation of T cell cytokine production Source: UniProtKB
  8. vasoconstriction Source: InterPro
Complete GO annotation...

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
Complete GO annotation...

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

ExpressionAtlasiQ9ESQ5. baseline.
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.
GeneTreeiENSGT00760000119127.
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

        10         20         30         40         50
MVGQEKEQSW IPKIFRKKVC TTFIVDLHDD AGGTLCQCGQ PRDAHPSVAV
60 70 80 90 100
EDAFGAAVVT EWNSDEHTTE KPTDAYGDLD FTYSGRKSSN FLRLSDRTDP
110 120 130 140 150
ATVYSLVTRS WGFRAPNLVV SVLGGSEGPV LQTWLQDLLR RGLVRAAQST
160 170 180 190 200
GAWIVTGGLH TGIGRHVGVA VRDHQTASTG GSKVVAMGVA PWGVVRNRDM
210 220 230 240 250
LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT YGRMGGENRF
260 270 280 290 300
RLRFESYVAQ QKTGVGGTGI DIPVLLLLIE GDEKMLKRIE DATQAQLPCL
310 320 330 340 350
LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA
360 370 380 390 400
QVERIMTRKE LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL
410 420 430 440 450
AVAWNRVDIA QSELFRGDIQ WRSFHLEASL MDALLNDRPE FVRLLISHGL
460 470 480 490 500
SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ ASHASSSKSP PANGAAELRP
510 520 530 540 550
PNVGQVLRTL LGETCAPRYP ARNTRHSLLG QDHRENDSLL MDWANMQQDA
560 570 580 590 600
SFEQAPWSDL LIWALLLNRA QMAIYFWEKG SNSVASALGA CLLLRVMARL
610 620 630 640 650
EWEAEEAARR KDLAAKFESM SVDLFGECYH NSEYRAARLL LRRCPLWGEA
660 670 680 690 700
TCLQLAMQAD ARAFFAQDGV QSLLTQKWWG EMDSTNPIWA LLLTFFCPPL
710 720 730 740 750
IYTNLILFRK SEEEPTQKDL DFDMDSSMNG AGPLGPAEPS AKVALERRRR
760 770 780 790 800
RRPGHTLCCG GCSKRWSYFW GAPVTAFLGN VVSYLLFLLL FAHVLLVDFQ
810 820 830 840 850
PTKPGVFELL LYFWAFTLLC EELRQGLGGG WGTLANGGPG PGKAPLRHRL
860 870 880 890 900
HLYLLDTWNQ CDLLALTCFL LGVGCRLTPG LFDLGRTVLC LDFMIFTLRL
910 920 930 940 950
LHIFTVNKQL GPKIVIVSKM MKDVFFFLFF LCVWLVAYGV ATEGILRPQD
960 970 980 990 1000
RSLPSILRRV FYRPYLQIFG QIPQEEMDVA LMNPSNCSAE RGSWAHPEGP
1010 1020 1030 1040 1050
VAGSCVSQYA NWLVVLLLIV FLLVANILLL NLLIAMFSYT FNKVHGNSDL
1060 1070 1080 1090 1100
YWKAQRYSLI REFHSRPALA PPLIIISHLR LLFKWLRRCH RTNLPASPVF
1110 1120 1130 1140 1150
EHFRVCLSKE AERTLLTWES VHKENFLLAQ ARDKRDSDSE RLKRTSQKVD
1160 1170 1180 1190 1200
TALKQLGQIR EYDRRLRGLE REVQHCSRVL TWMAEALSHS ALLPPGGPPP

PSPTGSKD
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 ENSGT00760000119127.
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

ExpressionAtlasi Q9ESQ5. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 89 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