TRPM4_MOUSE
ID TRPM4_MOUSE Reviewed; 1213 AA.
AC Q7TN37; Q6PDM0; Q769E2; Q769E4; Q80Y94; Q80YB3; Q811E2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transient receptor potential cation channel subfamily M member 4;
DE AltName: Full=Calcium-activated non-selective cation channel 1;
DE AltName: Full=Long transient receptor potential channel 4;
DE Short=LTrpC-4;
DE Short=LTrpC4;
GN Name=Trpm4; Synonyms=Ltrpc4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12893253; DOI=10.1016/s0006-291x(03)01186-0;
RA Murakami M., Xu F., Miyoshi I., Sato E., Ono K., Iijima T.;
RT "Identification and characterization of the murine TRPM4 channel.";
RL Biochem. Biophys. Res. Commun. 307:522-528(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ; TISSUE=Heart;
RX PubMed=12799367; DOI=10.1074/jbc.m305127200;
RA Nilius B., Prenen J., Droogmans G., Voets T., Vennekens R., Freichel M.,
RA Wissenbach U., Flockerzi V.;
RT "Voltage dependence of the Ca2+-activated cation channel TRPM4.";
RL J. Biol. Chem. 278:30813-30820(2003).
RN [3]
RP ERRATUM OF PUBMED:12799367.
RA Nilius B., Prenen J., Droogmans G., Voets T., Vennekens R., Freichel M.,
RA Wissenbach U., Flockerzi V.;
RL J. Biol. Chem. 278:42728-42728(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=17188667; DOI=10.1016/j.cardiores.2006.11.023;
RA Demion M., Bois P., Launay P., Guinamard R.;
RT "TRPM4, a Ca2+-activated nonselective cation channel in mouse sino-atrial
RT node cells.";
RL Cardiovasc. Res. 73:531-538(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18758465; DOI=10.1038/ni.1648;
RA Barbet G., Demion M., Moura I.C., Serafini N., Leger T., Vrtovsnik F.,
RA Monteiro R.C., Guinamard R., Kinet J.P., Launay P.;
RT "The calcium-activated nonselective cation channel TRPM4 is essential for
RT the migration but not the maturation of dendritic cells.";
RL Nat. Immunol. 9:1148-1156(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8] {ECO:0007744|PDB:6BCJ, ECO:0007744|PDB:6BCL, ECO:0007744|PDB:6BCO, ECO:0007744|PDB:6BCQ}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.88 ANGSTROMS) IN COMPLEX WITH ATP,
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, DISULFIDE BONDS, AND
RP MUTAGENESIS OF HIS-160; TRP-214; TYR-228 AND GLN-973.
RX PubMed=29211714; DOI=10.1038/nature24997;
RA Guo J., She J., Zeng W., Chen Q., Bai X.C., Jiang Y.;
RT "Structures of the calcium-activated, non-selective cation channel TRPM4.";
RL Nature 552:205-209(2017).
CC -!- FUNCTION: Calcium-activated non selective (CAN) cation channel that
CC mediates membrane depolarization. While it is activated by increase in
CC intracellular Ca(2+), it is impermeable to it (PubMed:17188667,
CC PubMed:29211714). Mediates transport of monovalent cations (Na(+) >
CC K(+) > Cs(+) > Li(+)), leading to depolarize the membrane. It thereby
CC plays a central role in cadiomyocytes, neurons from entorhinal cortex,
CC dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney
CC epithelial cells, cochlea hair cells etc. Participates in T-cell
CC activation by modulating Ca(2+) oscillations after T lymphocyte
CC activation, which is required for NFAT-dependent IL2 production.
CC Involved in myogenic constriction of cerebral arteries. Controls
CC insulin secretion in pancreatic beta-cells. May also be involved in
CC pacemaking or could cause irregular electrical activity under
CC conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2
CC (Th2) cell motility and cytokine production through differential
CC regulation of calcium signaling and NFATC1 localization. Enhances cell
CC proliferation through up-regulation of the beta-catenin signaling
CC pathway (By similarity). Essential for the migration but not the
CC maturation of dendritic cells (PubMed:18758465). Plays a role in
CC keratinocyte differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q8TD43, ECO:0000269|PubMed:17188667,
CC ECO:0000269|PubMed:18758465, ECO:0000269|PubMed:29211714}.
CC -!- ACTIVITY REGULATION: Gating is voltage-dependent and repressed by
CC decavanadate. Calmodulin-binding confers the Ca(2+) sensitivity. ATP is
CC able to restore Ca(2+) sensitivity after desensitization.
CC Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances
CC activity, by increasing the channel's Ca(2+) sensitivity and shifting
CC its voltage dependence of activation towards negative potentials.
CC Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole
CC derivative (BTP2) (By similarity). Inhibited by flufenamic acid and
CC glibenclamide (PubMed:17188667). {ECO:0000250|UniProtKB:Q8TD43,
CC ECO:0000269|PubMed:17188667}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:29211714}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12893253,
CC ECO:0000269|PubMed:29211714}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29211714}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8TD43}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TN37-1; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q7TN37-2; Sequence=VSP_021444;
CC Name=3; Synonyms=B;
CC IsoId=Q7TN37-3; Sequence=VSP_021444, VSP_021445;
CC -!- TISSUE SPECIFICITY: Sino-atrial nodes (at protein level). Widely
CC expressed. {ECO:0000269|PubMed:12799367, ECO:0000269|PubMed:12893253,
CC ECO:0000269|PubMed:17188667}.
CC -!- PTM: Phosphorylation by PKC leads to increase the sensitivity to
CC Ca(2+). {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- PTM: Sumoylated. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8TD43}.
CC -!- DISRUPTION PHENOTYPE: Mice have fewer dendritic cells in lymphoid
CC organs and impaired migration of dendritic cells is seen.
CC {ECO:0000269|PubMed:18758465}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. LTrpC
CC subfamily. TRPM4 sub-subfamily. {ECO:0000305}.
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DR EMBL; AB112657; BAC81769.1; -; mRNA.
DR EMBL; AB112658; BAC81770.1; -; mRNA.
DR EMBL; AB112667; BAC81771.1; -; Genomic_DNA.
DR EMBL; AJ575814; CAE05940.1; -; mRNA.
DR EMBL; BC046472; AAH46472.1; -; mRNA.
DR EMBL; BC046537; AAH46537.1; -; mRNA.
DR EMBL; BC049993; AAH49993.1; -; mRNA.
DR EMBL; BC058632; AAH58632.1; -; mRNA.
DR EMBL; BC096475; AAH96475.1; -; mRNA.
DR CCDS; CCDS52245.1; -. [Q7TN37-1]
DR RefSeq; NP_780339.2; NM_175130.4. [Q7TN37-1]
DR PDB; 6BCJ; EM; 3.14 A; A/B/C/D=1-1213.
DR PDB; 6BCL; EM; 3.54 A; A/B/C/D=1-1213.
DR PDB; 6BCO; EM; 2.88 A; A/B/C/D=1-1213.
DR PDB; 6BCQ; EM; 3.25 A; A/B/C/D=1-1213.
DR PDBsum; 6BCJ; -.
DR PDBsum; 6BCL; -.
DR PDBsum; 6BCO; -.
DR PDBsum; 6BCQ; -.
DR AlphaFoldDB; Q7TN37; -.
DR SMR; Q7TN37; -.
DR STRING; 10090.ENSMUSP00000040367; -.
DR DrugCentral; Q7TN37; -.
DR GuidetoPHARMACOLOGY; 496; -.
DR TCDB; 1.A.4.5.12; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; Q7TN37; -.
DR PhosphoSitePlus; Q7TN37; -.
DR MaxQB; Q7TN37; -.
DR PaxDb; Q7TN37; -.
DR PeptideAtlas; Q7TN37; -.
DR PRIDE; Q7TN37; -.
DR ProteomicsDB; 300019; -. [Q7TN37-1]
DR ProteomicsDB; 300020; -. [Q7TN37-2]
DR ProteomicsDB; 300021; -. [Q7TN37-3]
DR ABCD; Q7TN37; 1 sequenced antibody.
DR Antibodypedia; 31943; 306 antibodies from 30 providers.
DR DNASU; 68667; -.
DR Ensembl; ENSMUST00000042194; ENSMUSP00000040367; ENSMUSG00000038260. [Q7TN37-1]
DR GeneID; 68667; -.
DR KEGG; mmu:68667; -.
DR UCSC; uc009gun.2; mouse. [Q7TN37-1]
DR CTD; 54795; -.
DR MGI; MGI:1915917; Trpm4.
DR VEuPathDB; HostDB:ENSMUSG00000038260; -.
DR eggNOG; KOG3614; Eukaryota.
DR GeneTree; ENSGT00940000158693; -.
DR HOGENOM; CLU_001390_0_1_1; -.
DR InParanoid; Q7TN37; -.
DR OMA; RWIVDTL; -.
DR OrthoDB; 738147at2759; -.
DR PhylomeDB; Q7TN37; -.
DR TreeFam; TF314204; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 68667; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Trpm4; mouse.
DR PRO; PR:Q7TN37; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7TN37; protein.
DR Bgee; ENSMUSG00000038260; Expressed in small intestine Peyer's patch and 165 other tissues.
DR ExpressionAtlas; Q7TN37; baseline and differential.
DR Genevisible; Q7TN37; MM.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0034706; C:sodium channel complex; ISO:MGI.
DR GO; GO:0089717; C:spanning component of membrane; ISO:MGI.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005261; F:cation channel activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
DR GO; GO:0002407; P:dendritic cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0086045; P:membrane depolarization during AV node cell action potential; ISO:MGI.
DR GO; GO:0086048; P:membrane depolarization during bundle of His cell action potential; ISO:MGI.
DR GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISS:BHF-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
DR GO; GO:1904179; P:positive regulation of adipose tissue development; ISS:BHF-UCL.
DR GO; GO:1903949; P:positive regulation of atrial cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:BHF-UCL.
DR GO; GO:0010460; P:positive regulation of heart rate; ISS:BHF-UCL.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:BHF-UCL.
DR GO; GO:1904199; P:positive regulation of regulation of vascular associated smooth muscle cell membrane depolarization; ISS:BHF-UCL.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:BHF-UCL.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0002724; P:regulation of T cell cytokine production; ISS:UniProtKB.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR029581; TRPM4.
DR InterPro; IPR041491; TRPM_SLOG.
DR PANTHER; PTHR13800:SF6; PTHR13800:SF6; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
KW Calcium; Calmodulin-binding; Cell membrane; Coiled coil; Disulfide bond;
KW Endoplasmic reticulum; Golgi apparatus; Immunity; Ion channel;
KW Ion transport; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1213
FT /note="Transient receptor potential cation channel
FT subfamily M member 4"
FT /id="PRO_0000259530"
FT TOPO_DOM 1..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 800..810
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TRANSMEM 811..831
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 832..859
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 881..882
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TRANSMEM 883..906
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 907..926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TRANSMEM 927..947
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 948..959
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:29211714"
FT INTRAMEM 960..980
FT /note="Pore-forming"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 981..1015
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29211714"
FT TOPO_DOM 1037..1213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29211714"
FT REGION 1072..1175
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 1135..1140
FT /note="Mediates modulation by decavanadate and PIP2-
FT binding"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT COILED 1133..1185
FT /evidence="ECO:0000255"
FT MOTIF 971..973
FT /note="Selectivity filter"
FT /evidence="ECO:0000269|PubMed:29211714"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000269|PubMed:29211714,
FT ECO:0007744|PDB:6BCO, ECO:0007744|PDB:6BCQ"
FT BINDING 422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29211714,
FT ECO:0007744|PDB:6BCO, ECO:0007744|PDB:6BCQ"
FT BINDING 449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29211714,
FT ECO:0007744|PDB:6BCO, ECO:0007744|PDB:6BCQ"
FT BINDING 824
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT BINDING 827
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT BINDING 861
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT BINDING 864
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESQ5"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1144
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT MOD_RES 1151
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q8TD43"
FT DISULFID 989..1007
FT /evidence="ECO:0000269|PubMed:29211714,
FT ECO:0007744|PDB:6BCJ, ECO:0007744|PDB:6BCL,
FT ECO:0007744|PDB:6BCO, ECO:0007744|PDB:6BCQ"
FT VAR_SEQ 1..725
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12893253"
FT /id="VSP_021444"
FT VAR_SEQ 812..877
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12893253"
FT /id="VSP_021445"
FT MUTAGEN 160
FT /note="H->A: Near loss of channel sensitivity to inhibition
FT by ATP."
FT /evidence="ECO:0000269|PubMed:29211714"
FT MUTAGEN 214
FT /note="W->A: Decreases channel sensitivity to inhibition by
FT ATP."
FT /evidence="ECO:0000269|PubMed:29211714"
FT MUTAGEN 228
FT /note="Y->A: Strongly decreases channel sensitivity to
FT inhibition by ATP."
FT /evidence="ECO:0000269|PubMed:29211714"
FT MUTAGEN 973
FT /note="Q->D,N: Strongly decreased selectivity for
FT monovalent cations and increased permeability for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:29211714"
FT MUTAGEN 973
FT /note="Q->E: Decreased selectivity for monovalent cations
FT and increased permeability for Ca(2+)."
FT /evidence="ECO:0000269|PubMed:29211714"
FT CONFLICT 1119..1120
FT /note="KL -> NV (in Ref. 4; AAH46537)"
FT /evidence="ECO:0000305"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6BCO"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 332..337
FT /evidence="ECO:0007829|PDB:6BCO"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 345..358
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:6BCJ"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 391..403
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 407..413
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 503..511
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6BCQ"
FT HELIX 558..568
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 572..581
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6BCQ"
FT HELIX 585..601
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 606..633
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 635..642
FT /evidence="ECO:0007829|PDB:6BCO"
FT TURN 647..651
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 654..660
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 664..667
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 670..681
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 690..698
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 700..703
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 704..708
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 766..771
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 775..798
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 808..829
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 849..856
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 860..879
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:6BCJ"
FT HELIX 884..900
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 902..905
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 906..908
FT /evidence="ECO:0007829|PDB:6BCO"
FT TURN 910..912
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 913..919
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 923..947
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 955..968
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 969..971
FT /evidence="ECO:0007829|PDB:6BCO"
FT TURN 977..979
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 981..983
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 984..987
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 990..994
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 996..998
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 1000..1004
FT /evidence="ECO:0007829|PDB:6BCO"
FT STRAND 1006..1009
FT /evidence="ECO:0007829|PDB:6BCO"
FT TURN 1011..1013
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 1014..1028
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 1030..1066
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 1073..1075
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 1077..1089
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 1114..1140
FT /evidence="ECO:0007829|PDB:6BCO"
FT HELIX 1143..1161
FT /evidence="ECO:0007829|PDB:6BCO"
SQ SEQUENCE 1213 AA; 135760 MW; E4959F53ED35FB66 CRC64;
MVGPEKEQSW IPKIFRKKVC TTFIVDLSDD AGGTLCQCGQ PRDAHPSVAV EDAFGAAVVT
EWNSDEHTTE KPTDAYGDLD FTYSGRKHSN FLRLSDRTDP ATVYSLVTRS WGFRAPNLVV
SVLGGSGGPV LQTWLQDLLR RGLVRAAQST GAWIVTGGLH TGIGRHVGVA VRDHQTASTG
SSKVVAMGVA PWGVVRNRDM LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT
YGRLGGENRF RLRFESYVAQ QKTGVGGTGI DIPVLLLLID GDEKMLKRIE DATQAQLPCL
LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA QVERIMTRKE
LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL AVAWNRVDIA QSELFRGDIQ
WRSFHLEASL MDALLNDRPE FVRLLISHGL SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ
ASHASSSKSP PVNGTVELRP PNVGQVLRTL LGETCAPRYP ARNTRDSYLG QDHRENDSLL
MDWANKQPST DASFEQAPWS DLLIWALLLN RAQMAIYFWE KGSNSVASAL GACLLLRVMA
RLESEAEEAA RRKDLAATFE SMSVDLFGEC YHNSEERAAR LLLRRCPLWG EATCLQLAMQ
ADARAFFAQD GVQSLLTQKW WGEMDSTTPI WALLLAFFCP PLIYTNLIVF RKSEEEPTQK
DLDFDMDSSI NGAGPPGTVE PSAKVALERR QRRRPGRALC CGKFSKRWSD FWGAPVTAFL
GNVVSYLLFL LLFAHVLLVD FQPTKPSVSE LLLYFWAFTL LCEELRQGLG GGWGSLASGG
RGPDRAPLRH RLHLYLSDTW NQCDLLALTC FLLGVGCRLT PGLFDLGRTV LCLDFMIFTL
RLLHIFTVNK QLGPKIVIVS KMMKDVFFFL FFLCVWLVAY GVATEGILRP QDRSLPSILR
RVFYRPYLQI FGQIPQEEMD VALMIPGNCS MERGSWAHPE GPVAGSCVSQ YANWLVVLLL
IVFLLVANIL LLNLLIAMFS YTFSKVHGNS DLYWKAQRYS LIREFHSRPA LAPPLIIISH
VRLLIKWLRR CRRCRRANLP ASPVFEHFRV CLSKEAERKL LTWESVHKEN FLLAQARDKR
DSDSERLKRT SQKVDTALKQ LGQIREYDRR LRGLEREVQH CSRVLTWMAE ALSHSALLPP
GAPPPPSPTG SKD
