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   27-MAR-2024, entry version 137.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   EMDB; EMD-7081; -.
DR   EMDB; EMD-7082; -.
DR   EMDB; EMD-7083; -.
DR   EMDB; EMD-7085; -.
DR   SMR; Q7TN37; -.
DR   STRING; 10090.ENSMUSP00000040367; -.
DR   DrugCentral; Q7TN37; -.
DR   GuidetoPHARMACOLOGY; 496; -.
DR   TCDB; 1.A.4.5.12; the transient receptor potential ca2+/cation channel (trp-cc) family.
DR   iPTMnet; Q7TN37; -.
DR   PhosphoSitePlus; Q7TN37; -.
DR   MaxQB; Q7TN37; -.
DR   PaxDb; 10090-ENSMUSP00000040367; -.
DR   PeptideAtlas; Q7TN37; -.
DR   ProteomicsDB; 300019; -. [Q7TN37-1]
DR   ProteomicsDB; 300020; -. [Q7TN37-2]
DR   ProteomicsDB; 300021; -. [Q7TN37-3]
DR   Pumba; Q7TN37; -.
DR   ABCD; Q7TN37; 1 sequenced antibody.
DR   Antibodypedia; 31943; 360 antibodies from 30 providers.
DR   DNASU; 68667; -.
DR   Ensembl; ENSMUST00000042194.10; ENSMUSP00000040367.9; ENSMUSG00000038260.11. [Q7TN37-1]
DR   GeneID; 68667; -.
DR   KEGG; mmu:68667; -.
DR   UCSC; uc009gun.2; mouse. [Q7TN37-1]
DR   AGR; MGI:1915917; -.
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; WRGDRED; -.
DR   OrthoDB; 201873at2759; -.
DR   PhylomeDB; Q7TN37; -.
DR   TreeFam; TF314204; -.
DR   Reactome; R-MMU-3295583; TRP channels.
DR   BioGRID-ORCS; 68667; 3 hits in 76 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 168 other cell types or tissues.
DR   ExpressionAtlas; Q7TN37; baseline and differential.
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:0016020; C:membrane; ISO:MGI.
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:UniProtKB.
DR   GO; GO:0034706; C:sodium channel complex; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; 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:0005227; F:calcium-activated cation channel activity; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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 monoatomic 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: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   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR041491; TRPM_SLOG.
DR   PANTHER; PTHR13800:SF6; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 4; 1.
DR   PANTHER; PTHR13800; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL, SUBFAMILY M, MEMBER 6; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF18139; LSDAT_euk; 1.
DR   SUPFAM; SSF140860; Pseudo ankyrin repeat-like; 1.
DR   Genevisible; Q7TN37; MM.
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
//