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Transient receptor potential cation channel subfamily M member 4 (Calcium-activated non-selective cation channel 1) (Long transient receptor potential channel 4) (LTrpC-4) (LTrpC4) (MLS2s) (Melastatin-like 2)

 TRPM4_RAT               Reviewed;        1208 AA.
Q9ESQ5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 2.
22-NOV-2017, entry version 111.
RecName: Full=Transient receptor potential cation channel subfamily M member 4;
AltName: Full=Calcium-activated non-selective cation channel 1;
AltName: Full=Long transient receptor potential channel 4;
Short=LTrpC-4;
Short=LTrpC4;
AltName: Full=MLS2s;
AltName: Full=Melastatin-like 2;
Name=Trpm4; Synonyms=Ltrpc4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
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.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=19945433; DOI=10.1016/j.bbrc.2009.11.142;
Yoo J.C., Yarishkin O.V., Hwang E.M., Kim E., Kim D.G., Park N.,
Hong S.G., Park J.Y.;
"Cloning and characterization of rat transient receptor potential-
melastatin 4 (TRPM4).";
Biochem. Biophys. Res. Commun. 391:806-811(2010).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 717-1208.
TISSUE=Brain;
Ohki G., Ishibashi K., Suzuki M.;
"Cloning of novel Ca-permeable channels.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION.
PubMed=15030426; DOI=10.1046/j.1540-8167.2004.03477.x;
Guinamard R., Chatelier A., Lenfant J., Bois P.;
"Activation of the Ca(2+)-activated nonselective cation channel by
diacylglycerol analogues in rat cardiomyocytes.";
J. Cardiovasc. Electrophysiol. 15:342-348(2004).
[5]
FUNCTION.
PubMed=16966582; DOI=10.1161/01.HYP.0000237864.65019.a5;
Guinamard R., Demion M., Magaud C., Potreau D., Bois P.;
"Functional expression of the TRPM4 cationic current in ventricular
cardiomyocytes from spontaneously hypertensive rats.";
Hypertension 48:587-594(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Calcium-activated non selective (CAN) cation channel
that mediates membrane depolarization. While it is activated by
increase in intracellular Ca(2+), 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 Ca(2+) 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 Ca(2+) 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).
{ECO:0000250, ECO:0000269|PubMed:16966582,
ECO:0000269|PubMed:19945433}.
-!- ENZYME REGULATION: Gating is voltage-dependent and repressed by
decavanadate. Calmodulin-binding confers the Ca(2+) sensitivity.
ATP is able to restore Ca(2+) sensitivity after desensitization.
Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly
enhances activity, by increasing the channel's Ca(2+) 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).
{ECO:0000250}.
-!- SUBUNIT: Homomultimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Multi-pass
membrane protein. Endoplasmic reticulum. Golgi apparatus.
-!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum. Golgi
apparatus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms may exist.;
Name=1; Synonyms=TRPM4b;
IsoId=Q9ESQ5-1; Sequence=Displayed;
Name=2; Synonyms=TRPM4a;
IsoId=Q9ESQ5-2; Sequence=VSP_040337;
Note=Probably non-functional.;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:19945433}.
-!- PTM: Sumoylated. Desumoylated by SENP1 (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylation by PKC leads to increase the sensitivity to
Ca(2+). {ECO:0000269|PubMed:15030426}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
LTrpC subfamily. TRPM4 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15808.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AABR03000917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR03004552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB040807; BAB15808.1; ALT_SEQ; mRNA.
RefSeq; NP_001129701.1; NM_001136229.1. [Q9ESQ5-1]
UniGene; Rn.205004; -.
STRING; 10116.ENSRNOP00000041387; -.
iPTMnet; Q9ESQ5; -.
PhosphoSitePlus; Q9ESQ5; -.
PaxDb; Q9ESQ5; -.
PRIDE; Q9ESQ5; -.
GeneID; 171143; -.
KEGG; rno:171143; -.
UCSC; RGD:620244; rat. [Q9ESQ5-1]
CTD; 54795; -.
RGD; 620244; Trpm4.
eggNOG; KOG3614; Eukaryota.
eggNOG; ENOG410XR5B; LUCA.
HOGENOM; HOG000236350; -.
HOVERGEN; HBG108337; -.
InParanoid; Q9ESQ5; -.
KO; K04979; -.
OrthoDB; EOG091G017C; -.
PhylomeDB; Q9ESQ5; -.
TreeFam; TF314204; -.
PRO; PR:Q9ESQ5; -.
Proteomes; UP000002494; Unplaced.
Genevisible; Q9ESQ5; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0034706; C:sodium channel complex; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; ISO:RGD.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0006816; P:calcium ion transport; ISO:RGD.
GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISO:RGD.
GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:RGD.
GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:RGD.
GO; GO:0030502; P:negative regulation of bone mineralization; IMP:RGD.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
GO; GO:1904179; P:positive regulation of adipose tissue development; IMP:RGD.
GO; GO:1903949; P:positive regulation of atrial cardiac muscle cell action potential; IMP:RGD.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:RGD.
GO; GO:0010460; P:positive regulation of heart rate; IMP:RGD.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
GO; GO:1904199; P:positive regulation of regulation of vascular smooth muscle cell membrane depolarization; IMP:RGD.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
GO; GO:0002724; P:regulation of T cell cytokine production; ISS:UniProtKB.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:RGD.
GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR029581; TRPM4.
PANTHER; PTHR13800:SF6; PTHR13800:SF6; 1.
Pfam; PF00520; Ion_trans; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; ATP-binding; Calcium;
Calmodulin-binding; Cell membrane; Coiled coil; Complete proteome;
Endoplasmic reticulum; Golgi apparatus; Immunity; Ion channel;
Ion transport; Membrane; Nucleotide-binding; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation.
CHAIN 1 1208 Transient receptor potential cation
channel subfamily M member 4.
/FTId=PRO_0000259531.
TOPO_DOM 1 687 Cytoplasmic. {ECO:0000255}.
TRANSMEM 688 708 Helical. {ECO:0000255}.
TOPO_DOM 709 776 Extracellular. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TOPO_DOM 798 798 Cytoplasmic. {ECO:0000255}.
TRANSMEM 799 819 Helical. {ECO:0000255}.
TOPO_DOM 820 886 Extracellular. {ECO:0000255}.
TRANSMEM 887 907 Helical. {ECO:0000255}.
TOPO_DOM 908 924 Cytoplasmic. {ECO:0000255}.
TRANSMEM 925 945 Helical. {ECO:0000255}.
TOPO_DOM 946 959 Extracellular. {ECO:0000255}.
INTRAMEM 960 987 Pore-forming. {ECO:0000255}.
TOPO_DOM 988 1013 Extracellular. {ECO:0000255}.
TRANSMEM 1014 1034 Helical. {ECO:0000255}.
TOPO_DOM 1035 1208 Cytoplasmic. {ECO:0000255}.
REGION 1070 1170 Calmodulin-binding. {ECO:0000250}.
REGION 1130 1135 Mediates modulation by decavanadate and
PIP2-binding. {ECO:0000250}.
COILED 1128 1180 {ECO:0000255}.
MOTIF 975 980 Selectivity filter. {ECO:0000250}.
MOD_RES 527 527 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 538 538 Phosphoserine.
{ECO:0000250|UniProtKB:Q7TN37}.
MOD_RES 1139 1139 Phosphoserine; by PKC. {ECO:0000250}.
MOD_RES 1146 1146 Phosphoserine; by PKC. {ECO:0000250}.
VAR_SEQ 1 186 Missing (in isoform 2).
{ECO:0000303|PubMed:19945433}.
/FTId=VSP_040337.
SEQUENCE 1208 AA; 135341 MW; 324CEC9A6B9F7EA6 CRC64;
MVGQEKEQSW IPKIFRKKVC TTFIVDLHDD AGGTLCQCGQ PRDAHPSVAV EDAFGAAVVT
EWNSDEHTTE KPTDAYGDLD FTYSGRKSSN FLRLSDRTDP ATVYSLVTRS WGFRAPNLVV
SVLGGSEGPV LQTWLQDLLR RGLVRAAQST GAWIVTGGLH TGIGRHVGVA VRDHQTASTG
GSKVVAMGVA PWGVVRNRDM LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT
YGRMGGENRF RLRFESYVAQ QKTGVGGTGI DIPVLLLLIE GDEKMLKRIE DATQAQLPCL
LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA QVERIMTRKE
LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL AVAWNRVDIA QSELFRGDIQ
WRSFHLEASL MDALLNDRPE FVRLLISHGL SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ
ASHASSSKSP PANGAAELRP PNVGQVLRTL LGETCAPRYP ARNTRHSLLG QDHRENDSLL
MDWANMQQDA SFEQAPWSDL LIWALLLNRA QMAIYFWEKG SNSVASALGA CLLLRVMARL
EWEAEEAARR KDLAAKFESM SVDLFGECYH NSEYRAARLL LRRCPLWGEA TCLQLAMQAD
ARAFFAQDGV QSLLTQKWWG EMDSTNPIWA LLLTFFCPPL IYTNLILFRK SEEEPTQKDL
DFDMDSSMNG AGPLGPAEPS AKVALERRRR RRPGHTLCCG GCSKRWSYFW GAPVTAFLGN
VVSYLLFLLL FAHVLLVDFQ PTKPGVFELL LYFWAFTLLC EELRQGLGGG WGTLANGGPG
PGKAPLRHRL HLYLLDTWNQ CDLLALTCFL LGVGCRLTPG LFDLGRTVLC LDFMIFTLRL
LHIFTVNKQL GPKIVIVSKM MKDVFFFLFF LCVWLVAYGV ATEGILRPQD RSLPSILRRV
FYRPYLQIFG QIPQEEMDVA LMNPSNCSAE RGSWAHPEGP VAGSCVSQYA NWLVVLLLIV
FLLVANILLL NLLIAMFSYT FNKVHGNSDL YWKAQRYSLI REFHSRPALA PPLIIISHLR
LLFKWLRRCH RTNLPASPVF EHFRVCLSKE AERTLLTWES VHKENFLLAQ ARDKRDSDSE
RLKRTSQKVD TALKQLGQIR EYDRRLRGLE REVQHCSRVL TWMAEALSHS ALLPPGGPPP
PSPTGSKD


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