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Transient receptor potential cation channel subfamily M member 4 (hTRPM4) (Calcium-activated non-selective cation channel 1) (Long transient receptor potential channel 4) (LTrpC-4) (LTrpC4) (Melastatin-4)

 TRPM4_HUMAN             Reviewed;        1214 AA.
Q8TD43; A2RU25; Q7Z5D9; Q96L84; Q9NXV1;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 125.
RecName: Full=Transient receptor potential cation channel subfamily M member 4;
Short=hTRPM4;
AltName: Full=Calcium-activated non-selective cation channel 1;
AltName: Full=Long transient receptor potential channel 4;
Short=LTrpC-4;
Short=LTrpC4;
AltName: Full=Melastatin-4;
Name=TRPM4; Synonyms=LTRPC4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=11535825; DOI=10.1073/pnas.191360198;
Xu X.-Z.S., Moebius F., Gill D.L., Montell C.;
"Regulation of melastatin, a TRP-related protein, through interaction
with a cytoplasmic isoform.";
Proc. Natl. Acad. Sci. U.S.A. 98:10692-10697(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=12015988; DOI=10.1016/S0092-8674(02)00719-5;
Launay P., Fleig A., Perraud A.-L., Scharenberg A.M., Penner R.,
Kinet J.-P.;
"TRPM4 is a Ca2+-activated nonselective cation channel mediating cell
membrane depolarization.";
Cell 109:397-407(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=12842017; DOI=10.1016/S0960-9822(03)00431-7;
Hofmann T., Chubanov V., Gudermann T., Montell C.;
"TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent
selective cation channel.";
Curr. Biol. 13:1153-1158(2003).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Prostate;
PubMed=12799367; DOI=10.1074/jbc.M305127200;
Nilius B., Prenen J., Droogmans G., Voets T., Vennekens R.,
Freichel M., Wissenbach U., Flockerzi V.;
"Voltage dependence of the Ca2+-activated cation channel TRPM4.";
J. Biol. Chem. 278:30813-30820(2003).
[5]
ERRATUM.
Nilius B., Prenen J., Droogmans G., Voets T., Vennekens R.,
Freichel M., Wissenbach U., Flockerzi V.;
J. Biol. Chem. 278:42728-42728(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15472118; DOI=10.1161/01.RES.0000147311.54833.03;
Earley S., Waldron B.J., Brayden J.E.;
"Critical role for transient receptor potential channel TRPM4 in
myogenic constriction of cerebral arteries.";
Circ. Res. 95:922-929(2004).
[9]
FUNCTION.
PubMed=15121803; DOI=10.1113/jphysiol.2004.063974;
Guinamard R., Chatelier A., Demion M., Potreau D., Patri S.,
Rahmati M., Bois P.;
"Functional characterization of a Ca(2+)-activated non-selective
cation channel in human atrial cardiomyocytes.";
J. Physiol. (Lond.) 558:75-83(2004).
[10]
ENZYME REGULATION.
PubMed=15331675; DOI=10.1113/jphysiol.2004.070839;
Nilius B., Prenen J., Janssens A., Voets T., Droogmans G.;
"Decavanadate modulates gating of TRPM4 cation channels.";
J. Physiol. (Lond.) 560:753-765(2004).
[11]
ATP-BINDING, AND ENZYME REGULATION.
PubMed=14758478; DOI=10.1007/s00424-003-1221-x;
Nilius B., Prenen J., Voets T., Droogmans G.;
"Intracellular nucleotides and polyamines inhibit the Ca2+-activated
cation channel TRPM4b.";
Pflugers Arch. 448:70-75(2004).
[12]
FUNCTION.
PubMed=15550671; DOI=10.1126/science.1098845;
Launay P., Cheng H., Srivatsan S., Penner R., Fleig A., Kinet J.-P.;
"TRPM4 regulates calcium oscillations after T cell activation.";
Science 306:1374-1377(2004).
[13]
PHOSPHORYLATION AT SER-1145 AND SER-1152, ATP-BINDING,
CALMODULIN-BINDING, AND MUTAGENESIS OF LEU-275; ILE-278; ASP-279;
GLY-324; GLY-325; ARG-327; SER-1145 AND SER-1152.
PubMed=15590641; DOI=10.1074/jbc.M411089200;
Nilius B., Prenen J., Tang J., Wang C., Owsianik G., Janssens A.,
Voets T., Zhu M.X.;
"Regulation of the Ca2+ sensitivity of the nonselective cation channel
TRPM4.";
J. Biol. Chem. 280:6423-6433(2005).
[14]
SELECTIVITY FILTER MOTIF, AND MUTAGENESIS OF GLN-977; GLU-981;
981-GLU--ALA-986; ASP-982 AND ASP-984.
PubMed=15845551; DOI=10.1074/jbc.M501686200;
Nilius B., Prenen J., Janssens A., Owsianik G., Wang C., Zhu M.X.,
Voets T.;
"The selectivity filter of the cation channel TRPM4.";
J. Biol. Chem. 280:22899-22906(2005).
[15]
ENZYME REGULATION, AND PIP2-BINDING.
PubMed=16186107; DOI=10.1074/jbc.M506965200;
Zhang Z., Okawa H., Wang Y., Liman E.R.;
"Phosphatidylinositol 4,5-bisphosphate rescues TRPM4 channels from
desensitization.";
J. Biol. Chem. 280:39185-39192(2005).
[16]
FUNCTION.
PubMed=16806463; DOI=10.1016/j.ceca.2006.04.032;
Cheng H., Beck A., Launay P., Gross S.A., Stokes A.J., Kinet J.-P.,
Fleig A., Penner R.;
"TRPM4 controls insulin secretion in pancreatic beta-cells.";
Cell Calcium 41:51-61(2007).
[17]
ENZYME REGULATION, PIP2-BINDING, AND MUTAGENESIS OF LYS-1059; ARG-1072
AND 1136-ARG--ARG-1141.
PubMed=16424899; DOI=10.1038/sj.emboj.7600963;
Nilius B., Mahieu F., Prenen J., Janssens A., Owsianik G.,
Vennekens R., Voets T.;
"The Ca2+-activated cation channel TRPM4 is regulated by
phosphatidylinositol 4,5-biphosphate.";
EMBO J. 25:467-478(2006).
[18]
TISSUE SPECIFICITY.
PubMed=16777713; DOI=10.1080/10799890600637506;
Fonfria E., Murdock P.R., Cusdin F.S., Benham C.D., Kelsell R.E.,
McNulty S.;
"Tissue distribution profiles of the human TRPM cation channel
family.";
J. Recept. Signal Transduct. 26:159-178(2006).
[19]
ENZYME REGULATION.
PubMed=16407466; DOI=10.1124/mol.105.021154;
Takezawa R., Cheng H., Beck A., Ishikawa J., Launay P., Kubota H.,
Kinet J.-P., Fleig A., Yamada T., Penner R.;
"A pyrazole derivative potently inhibits lymphocyte Ca2+ influx and
cytokine production by facilitating transient receptor potential
melastatin 4 channel activity.";
Mol. Pharmacol. 69:1413-1420(2006).
[20]
SUBCELLULAR LOCATION.
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).
[21]
FUNCTION.
PubMed=20625999; DOI=10.1002/jcp.22310;
Armisen R., Marcelain K., Simon F., Tapia J.C., Toro J., Quest A.F.,
Stutzin A.;
"TRPM4 enhances cell proliferation through up-regulation of the beta-
catenin signaling pathway.";
J. Cell. Physiol. 226:103-109(2011).
[22]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20656926; DOI=10.4049/jimmunol.1000880;
Weber K.S., Hildner K., Murphy K.M., Allen P.M.;
"Trpm4 differentially regulates Th1 and th2 function by altering
calcium signaling and NFAT localization.";
J. Immunol. 185:2836-2846(2010).
[23]
VARIANT PFHB1B LYS-7, CHARACTERIZATION OF VARIANT PFHB1B LYS-7,
SUMOYLATION, AND TISSUE SPECIFICITY.
PubMed=19726882; DOI=10.1172/JCI38292;
Kruse M., Schulze-Bahr E., Corfield V., Beckmann A., Stallmeyer B.,
Kurtbay G., Ohmert I., Schulze-Bahr E., Brink P., Pongs O.;
"Impaired endocytosis of the ion channel TRPM4 is associated with
human progressive familial heart block type I.";
J. Clin. Invest. 119:2737-2744(2009).
[24]
VARIANTS PFHB1B TRP-164; THR-432 AND ASP-844.
PubMed=20562447; DOI=10.1161/CIRCGENETICS.109.930867;
Liu H., El Zein L., Kruse M., Guinamard R., Beckmann A., Bozio A.,
Kurtbay G., Megarbane A., Ohmert I., Blaysat G., Villain E., Pongs O.,
Bouvagnet P.;
"Gain-of-function mutations in TRPM4 cause autosomal dominant isolated
cardiac conduction disease.";
Circ. Cardiovasc. Genet. 3:374-385(2010).
[25]
VARIANTS PFHB1B HIS-131; ARG-293; THR-432; SER-582; HIS-790; ASP-844;
ARG-914 AND SER-970, AND VARIANTS THR-101; CYS-103; HIS-252; LYS-487
DEL; ALA-561; ARG-854 AND LEU-1204.
PubMed=21887725; DOI=10.1002/humu.21599;
Stallmeyer B., Zumhagen S., Denjoy I., Duthoit G., Hebert J.L.,
Ferrer X., Maugenre S., Schmitz W., Kirchhefer U., Schulze-Bahr E.,
Guicheney P., Schulze-Bahr E.;
"Mutational spectrum in the Ca(2+) -activated cation channel gene
TRPM4 in patients with cardiac conductance disturbances.";
Hum. Mutat. 33:109-117(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. {ECO:0000269|PubMed:12015988,
ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:15121803,
ECO:0000269|PubMed:15472118, ECO:0000269|PubMed:15550671,
ECO:0000269|PubMed:16806463, ECO:0000269|PubMed:20625999,
ECO:0000269|PubMed:20656926}.
-!- 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).
{ECO:0000269|PubMed:14758478, ECO:0000269|PubMed:15331675,
ECO:0000269|PubMed:16186107, ECO:0000269|PubMed:16407466,
ECO:0000269|PubMed:16424899}.
-!- SUBUNIT: Homomultimer. {ECO:0000269|PubMed:12015988}.
-!- 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=3;
Name=1; Synonyms=TRPM4b;
IsoId=Q8TD43-1; Sequence=Displayed;
Name=2; Synonyms=TRPM4a;
IsoId=Q8TD43-2; Sequence=VSP_021442;
Name=3; Synonyms=TRPM4c;
IsoId=Q8TD43-3; Sequence=VSP_021443;
-!- TISSUE SPECIFICITY: Widely expressed with a high expression in
intestine and prostate. In brain, it is both expressed in whole
cerebral arteries and isolated vascular smooth muscle cells.
Prominently expressed in Purkinje fibers. Expressed at higher
levels in T-helper 2 (Th2) cells as compared to T-helper 1 (Th1)
cells. {ECO:0000269|PubMed:11535825, ECO:0000269|PubMed:12015988,
ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:15472118,
ECO:0000269|PubMed:16777713, ECO:0000269|PubMed:19726882,
ECO:0000269|PubMed:20656926}.
-!- PTM: Phosphorylation by PKC leads to increase the sensitivity to
Ca(2+). {ECO:0000269|PubMed:15590641}.
-!- PTM: Sumoylated. Desumoylated by SENP1.
{ECO:0000269|PubMed:19726882}.
-!- DISEASE: Progressive familial heart block 1B (PFHB1B)
[MIM:604559]: A cardiac bundle branch disorder characterized by
progressive alteration of cardiac conduction through the His-
Purkinje system, with a pattern of a right bundle-branch block
and/or left anterior hemiblock occurring individually or together.
It leads to complete atrio-ventricular block causing syncope and
sudden death. {ECO:0000269|PubMed:19726882,
ECO:0000269|PubMed:20562447, ECO:0000269|PubMed:21887725}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
LTrpC subfamily. TRPM4 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA90907.1; Type=Erroneous termination; Positions=1191; Note=Translated as Glu.; Evidence={ECO:0000305};
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EMBL; AY046396; AAL02142.1; -; mRNA.
EMBL; AF497623; AAM18083.1; -; mRNA.
EMBL; AY297044; AAP44473.1; -; mRNA.
EMBL; AY297045; AAP44474.1; -; mRNA.
EMBL; AY297046; AAP44475.1; -; mRNA.
EMBL; AJ575813; CAE05941.1; -; mRNA.
EMBL; AK000048; BAA90907.1; ALT_SEQ; mRNA.
EMBL; AK292862; BAF85551.1; -; mRNA.
EMBL; BC132727; AAI32728.1; -; mRNA.
CCDS; CCDS33073.1; -. [Q8TD43-1]
CCDS; CCDS56098.1; -. [Q8TD43-3]
RefSeq; NP_001182156.1; NM_001195227.1. [Q8TD43-3]
RefSeq; NP_001308212.1; NM_001321283.1. [Q8TD43-2]
RefSeq; NP_060106.2; NM_017636.3. [Q8TD43-1]
UniGene; Hs.467101; -.
ProteinModelPortal; Q8TD43; -.
BioGrid; 120154; 11.
IntAct; Q8TD43; 1.
STRING; 9606.ENSP00000252826; -.
ChEMBL; CHEMBL1628469; -.
GuidetoPHARMACOLOGY; 496; -.
TCDB; 1.A.4.5.4; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q8TD43; -.
PhosphoSitePlus; Q8TD43; -.
BioMuta; TRPM4; -.
DMDM; 74715868; -.
EPD; Q8TD43; -.
MaxQB; Q8TD43; -.
PaxDb; Q8TD43; -.
PeptideAtlas; Q8TD43; -.
PRIDE; Q8TD43; -.
Ensembl; ENST00000252826; ENSP00000252826; ENSG00000130529. [Q8TD43-1]
Ensembl; ENST00000427978; ENSP00000407492; ENSG00000130529. [Q8TD43-3]
GeneID; 54795; -.
KEGG; hsa:54795; -.
UCSC; uc002pmw.4; human. [Q8TD43-1]
CTD; 54795; -.
DisGeNET; 54795; -.
EuPathDB; HostDB:ENSG00000130529.15; -.
GeneCards; TRPM4; -.
HGNC; HGNC:17993; TRPM4.
HPA; HPA041169; -.
MalaCards; TRPM4; -.
MIM; 604559; phenotype.
MIM; 606936; gene.
neXtProt; NX_Q8TD43; -.
OpenTargets; ENSG00000130529; -.
Orphanet; 130; Brugada syndrome.
Orphanet; 871; Familial progressive cardiac conduction defect.
PharmGKB; PA38272; -.
eggNOG; KOG3614; Eukaryota.
eggNOG; ENOG410XR5B; LUCA.
GeneTree; ENSGT00760000119127; -.
HOGENOM; HOG000236350; -.
HOVERGEN; HBG108337; -.
InParanoid; Q8TD43; -.
KO; K04979; -.
OMA; GQAPWSD; -.
OrthoDB; EOG091G017C; -.
PhylomeDB; Q8TD43; -.
TreeFam; TF314204; -.
Reactome; R-HSA-3295583; TRP channels.
SIGNOR; Q8TD43; -.
GeneWiki; TRPM4; -.
GenomeRNAi; 54795; -.
PRO; PR:Q8TD43; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130529; -.
CleanEx; HS_TRPM4; -.
ExpressionAtlas; Q8TD43; baseline and differential.
Genevisible; Q8TD43; HS.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0034706; C:sodium channel complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005227; F:calcium activated cation channel activity; IDA:BHF-UCL.
GO; GO:0005262; F:calcium channel activity; IEA:Ensembl.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0005272; F:sodium channel activity; TAS:Reactome.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
GO; GO:0019722; P:calcium-mediated signaling; IDA:BHF-UCL.
GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
GO; GO:0086045; P:membrane depolarization during AV node cell action potential; IMP:BHF-UCL.
GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; IMP:BHF-UCL.
GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; IMP:BHF-UCL.
GO; GO:0030502; P:negative regulation of bone mineralization; ISS:BHF-UCL.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
GO; GO:1904179; P:positive regulation of adipose tissue development; ISS:BHF-UCL.
GO; GO:1903949; P:positive regulation of atrial cardiac muscle cell action potential; ISS:BHF-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:BHF-UCL.
GO; GO:0010460; P:positive regulation of heart rate; ISS:BHF-UCL.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:BHF-UCL.
GO; GO:1904199; P:positive regulation of regulation of vascular smooth muscle cell membrane depolarization; ISS:BHF-UCL.
GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:BHF-UCL.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
GO; GO:0002724; P:regulation of T cell cytokine production; IDA:UniProtKB.
GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; IMP:BHF-UCL.
GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:BHF-UCL.
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;
Disease mutation; Endoplasmic reticulum; Golgi apparatus; Immunity;
Ion channel; Ion transport; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 1214 Transient receptor potential cation
channel subfamily M member 4.
/FTId=PRO_0000259529.
TOPO_DOM 1 683 Cytoplasmic. {ECO:0000255}.
TRANSMEM 684 704 Helical. {ECO:0000255}.
TOPO_DOM 705 776 Extracellular. {ECO:0000255}.
TRANSMEM 777 797 Helical. {ECO:0000255}.
TOPO_DOM 798 868 Cytoplasmic. {ECO:0000255}.
TRANSMEM 869 889 Helical. {ECO:0000255}.
TOPO_DOM 890 892 Extracellular. {ECO:0000255}.
TRANSMEM 893 913 Helical. {ECO:0000255}.
TOPO_DOM 914 929 Cytoplasmic. {ECO:0000255}.
TRANSMEM 930 950 Helical. {ECO:0000255}.
TOPO_DOM 951 965 Extracellular. {ECO:0000255}.
INTRAMEM 966 993 Pore-forming. {ECO:0000255}.
TOPO_DOM 994 1019 Extracellular. {ECO:0000255}.
TRANSMEM 1020 1040 Helical. {ECO:0000255}.
TOPO_DOM 1041 1214 Cytoplasmic. {ECO:0000255}.
REGION 1076 1176 Calmodulin-binding.
REGION 1136 1141 Mediates modulation by decavanadate and
PIP2-binding.
COILED 1134 1187 {ECO:0000255}.
MOTIF 981 986 Selectivity filter.
MOD_RES 1145 1145 Phosphoserine; by PKC.
{ECO:0000305|PubMed:15590641}.
MOD_RES 1152 1152 Phosphoserine; by PKC.
{ECO:0000305|PubMed:15590641}.
VAR_SEQ 1 174 Missing (in isoform 2).
{ECO:0000303|PubMed:11535825,
ECO:0000303|PubMed:12842017}.
/FTId=VSP_021442.
VAR_SEQ 738 882 Missing (in isoform 3).
{ECO:0000303|PubMed:12842017}.
/FTId=VSP_021443.
VARIANT 7 7 E -> K (in PFHB1B; attenuated
desumoylation of TRPM4 resulting in
constitutive sumoylation of the channel
leading to impaired endocytosis and
elevated channel density at the cell
surface; dbSNP:rs267607142).
{ECO:0000269|PubMed:19726882}.
/FTId=VAR_064042.
VARIANT 101 101 A -> T (in dbSNP:rs113984787).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066761.
VARIANT 103 103 Y -> C (in dbSNP:rs144781529).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066762.
VARIANT 131 131 Q -> H (in PFHB1B; incomplete right
bundle-branch block; dbSNP:rs172146854).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066763.
VARIANT 164 164 R -> W (in PFHB1B; dbSNP:rs387907216).
{ECO:0000269|PubMed:20562447}.
/FTId=VAR_066764.
VARIANT 252 252 R -> H (in dbSNP:rs146564314).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066765.
VARIANT 293 293 Q -> R (in PFHB1B; right bundle-branch
block; dbSNP:rs172147855).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066766.
VARIANT 432 432 A -> T (in PFHB1B; atrioventricular
block; dbSNP:rs201907325).
{ECO:0000269|PubMed:20562447,
ECO:0000269|PubMed:21887725}.
/FTId=VAR_066767.
VARIANT 487 498 Missing.
/FTId=VAR_066768.
VARIANT 561 561 D -> A (in dbSNP:rs56355369).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066769.
VARIANT 582 582 G -> S (in PFHB1B; atrioventricular
block; dbSNP:rs172149856).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066770.
VARIANT 790 790 Y -> H (in PFHB1B; atrioventricular
block; dbSNP:rs172150857).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066771.
VARIANT 844 844 G -> D (in PFHB1B; right bundle-branch
block; dbSNP:rs200038418).
{ECO:0000269|PubMed:20562447,
ECO:0000269|PubMed:21887725}.
/FTId=VAR_066772.
VARIANT 854 854 Q -> R (in dbSNP:rs172155862).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066773.
VARIANT 914 914 K -> R (in PFHB1B; atrioventricular
block; dbSNP:rs172151858).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066774.
VARIANT 970 970 P -> S (in PFHB1B; incomplete right
bundle-branch block; dbSNP:rs172152859).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066775.
VARIANT 1204 1204 P -> L (in dbSNP:rs150391806).
{ECO:0000269|PubMed:21887725}.
/FTId=VAR_066776.
MUTAGEN 275 275 L->A,C: Abolishes ability to restore
sensitivity to Ca(2+) after
desensitization.
{ECO:0000269|PubMed:15590641}.
MUTAGEN 278 278 I->N: No effect.
{ECO:0000269|PubMed:15590641}.
MUTAGEN 279 279 D->N: No effect.
{ECO:0000269|PubMed:15590641}.
MUTAGEN 324 324 G->A: No effect.
{ECO:0000269|PubMed:15590641}.
MUTAGEN 325 325 G->A: Abolishes ability to restore
sensitivity to Ca(2+) after
desensitization.
{ECO:0000269|PubMed:15590641}.
MUTAGEN 327 327 R->A: No effect.
{ECO:0000269|PubMed:15590641}.
MUTAGEN 977 977 Q->E: Alters the monovalent cation
permeability sequence and results in a
pore with moderate Ca(2+) permeability.
{ECO:0000269|PubMed:15845551}.
MUTAGEN 981 986 EDMDVA->TIIDGP: Induces a functional
channel that combines the gating
hallmarks of TRPM4 (activation by Ca(2+))
with TRPV6-like sensitivity to block by
extracellular Ca(2+) and Mg(2+) as well
as Ca(2+) permeation.
{ECO:0000269|PubMed:15845551}.
MUTAGEN 981 981 E->A: Results in a channel with normal
permeability properties but with a
reduced sensitivity to block by
intracellular spermine.
{ECO:0000269|PubMed:15845551}.
MUTAGEN 982 982 D->A: Results in a functional channel
that exhibits extremely fast
desensitization, possibly indicating
destabilization of the pore.
{ECO:0000269|PubMed:15845551}.
MUTAGEN 984 984 D->A: Results in a non-functional channel
with a dominant negative phenotype.
{ECO:0000269|PubMed:15845551}.
MUTAGEN 1059 1059 K->Q: Does not affect PIP2-binding.
{ECO:0000269|PubMed:16424899}.
MUTAGEN 1072 1072 R->Q: Does not affect PIP2-binding.
{ECO:0000269|PubMed:16424899}.
MUTAGEN 1136 1141 Missing: Results in a channel with very
rapid desensitization and highly reduced
sensitivity to PIP2.
{ECO:0000269|PubMed:16424899}.
MUTAGEN 1145 1145 S->A: Decreases the sensitivity to
Ca(2+). {ECO:0000269|PubMed:15590641}.
MUTAGEN 1152 1152 S->A: Decreases the sensitivity to
Ca(2+). {ECO:0000269|PubMed:15590641}.
CONFLICT 1149 1149 K -> E (in Ref. 6; BAA90907).
{ECO:0000305}.
CONFLICT 1207 1207 P -> L (in Ref. 6; BAA90907).
{ECO:0000305}.
CONFLICT 1210 1210 P -> H (in Ref. 6; BAA90907).
{ECO:0000305}.
CONFLICT 1214 1214 D -> E (in Ref. 6; BAA90907).
{ECO:0000305}.
SEQUENCE 1214 AA; 134301 MW; 76ADA452690ED8F5 CRC64;
MVVPEKEQSW IPKIFKKKTC TTFIVDSTDP GGTLCQCGRP RTAHPAVAME DAFGAAVVTV
WDSDAHTTEK PTDAYGELDF TGAGRKHSNF LRLSDRTDPA AVYSLVTRTW GFRAPNLVVS
VLGGSGGPVL QTWLQDLLRR GLVRAAQSTG AWIVTGGLHT GIGRHVGVAV RDHQMASTGG
TKVVAMGVAP WGVVRNRDTL INPKGSFPAR YRWRGDPEDG VQFPLDYNYS AFFLVDDGTH
GCLGGENRFR LRLESYISQQ KTGVGGTGID IPVLLLLIDG DEKMLTRIEN ATQAQLPCLL
VAGSGGAADC LAETLEDTLA PGSGGARQGE ARDRIRRFFP KGDLEVLQAQ VERIMTRKEL
LTVYSSEDGS EEFETIVLKA LVKACGSSEA SAYLDELRLA VAWNRVDIAQ SELFRGDIQW
RSFHLEASLM DALLNDRPEF VRLLISHGLS LGHFLTPMRL AQLYSAAPSN SLIRNLLDQA
SHSAGTKAPA LKGGAAELRP PDVGHVLRML LGKMCAPRYP SGGAWDPHPG QGFGESMYLL
SDKATSPLSL DAGLGQAPWS DLLLWALLLN RAQMAMYFWE MGSNAVSSAL GACLLLRVMA
RLEPDAEEAA RRKDLAFKFE GMGVDLFGEC YRSSEVRAAR LLLRRCPLWG DATCLQLAMQ
ADARAFFAQD GVQSLLTQKW WGDMASTTPI WALVLAFFCP PLIYTRLITF RKSEEEPTRE
ELEFDMDSVI NGEGPVGTAD PAEKTPLGVP RQSGRPGCCG GRCGGRRCLR RWFHFWGAPV
TIFMGNVVSY LLFLLLFSRV LLVDFQPAPP GSLELLLYFW AFTLLCEELR QGLSGGGGSL
ASGGPGPGHA SLSQRLRLYL ADSWNQCDLV ALTCFLLGVG CRLTPGLYHL GRTVLCIDFM
VFTVRLLHIF TVNKQLGPKI VIVSKMMKDV FFFLFFLGVW LVAYGVATEG LLRPRDSDFP
SILRRVFYRP YLQIFGQIPQ EDMDVALMEH SNCSSEPGFW AHPPGAQAGT CVSQYANWLV
VLLLVIFLLV ANILLVNLLI AMFSYTFGKV QGNSDLYWKA QRYRLIREFH SRPALAPPFI
VISHLRLLLR QLCRRPRSPQ PSSPALEHFR VYLSKEAERK LLTWESVHKE NFLLARARDK
RESDSERLKR TSQKVDLALK QLGHIREYEQ RLKVLEREVQ QCSRVLGWVA EALSRSALLP
PGGPPPPDLP GSKD


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