PLCB1_MOUSE
ID PLCB1_MOUSE Reviewed; 1216 AA.
AC Q9Z1B3; Q62075; Q6PDH1; Q8K5A5; Q8K5A6; Q9Z0E5; Q9Z2T5;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:Q9NQ66};
DE AltName: Full=PLC-154;
DE AltName: Full=Phosphoinositide phospholipase C-beta-1;
DE AltName: Full=Phospholipase C-beta-1;
DE Short=PLC-beta-1;
GN Name=Plcb1 {ECO:0000312|MGI:MGI:97613}; Synonyms=Plcb;
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 [MRNA] (ISOFORMS A AND B).
RC STRAIN=SWR/J;
RA Bai J., Wu K., Marks D.L., Machamer C., Pagano R.E.;
RT "Cloning of PI-specific phospholipase C's from 3T3 cells. Expression and
RT membrane targeting of a novel phospholipase C-beta-1 isoform.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 29-145.
RC STRAIN=C57BL/6J;
RX PubMed=9753089; DOI=10.1046/j.1460-9568.1998.00213.x;
RA Watanabe M., Nakamura M., Sato K., Kano M., Simon M.I., Inoue Y.;
RT "Patterns of expression for the mRNA corresponding to the four isoforms of
RT phospholipase Cbeta in mouse brain.";
RL Eur. J. Neurosci. 10:2016-2025(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 428-615.
RC TISSUE=Oocyte;
RX PubMed=8687404; DOI=10.1042/bj3160583;
RA Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F.;
RT "Phospholipase C in mouse oocytes: characterization of beta and gamma
RT isoforms and their possible involvement in sperm-induced Ca2+ spiking.";
RL Biochem. J. 316:583-591(1996).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=18802028; DOI=10.1161/circresaha.108.176024;
RA Wright C.D., Chen Q., Baye N.L., Huang Y., Healy C.L., Kasinathan S.,
RA O'Connell T.D.;
RT "Nuclear alpha1-adrenergic receptors signal activated ERK localization to
RT caveolae in adult cardiac myocytes.";
RL Circ. Res. 103:992-1000(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-417; THR-509;
RP SER-511; SER-582; SER-978; SER-987; SER-1197; SER-1199 AND SER-1200, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Pancreas;
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 [9]
RP FUNCTION, AND PALMITOYLATION AT CYS-17 BY ZDHHC21.
RX PubMed=27653213; DOI=10.1038/ncomms12823;
RA Beard R.S. Jr., Yang X., Meegan J.E., Overstreet J.W., Yang C.G.,
RA Elliott J.A., Reynolds J.J., Cha B.J., Pivetti C.D., Mitchell D.A.,
RA Wu M.H., Deschenes R.J., Yuan S.Y.;
RT "Palmitoyl acyltransferase DHHC21 mediates endothelial dysfunction in
RT systemic inflammatory response syndrome.";
RL Nat. Commun. 7:12823-12823(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-
CC bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate
CC (IP3) and mediates intracellular signaling downstream of G protein-
CC coupled receptors (PubMed:27653213). Regulates the function of the
CC endothelial barrier (PubMed:27653213). {ECO:0000269|PubMed:27653213,
CC ECO:0000303|PubMed:27653213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-
CC diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456,
CC ChEBI:CHEBI:203600; EC=3.1.4.11;
CC Evidence={ECO:0000250|UniProtKB:Q9NQ66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:Q9NQ66};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + H2O =
CC 1D-myo-inositol 1-phosphate + a 1,2-diacyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:43484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:58433;
CC Evidence={ECO:0000250|UniProtKB:P10687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:P10687};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with DGKQ. {ECO:0000250|UniProtKB:Q9NQ66}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:18802028}.
CC Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the
CC adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of
CC cardiac myocytes. {ECO:0000269|PubMed:18802028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=C-beta-1a;
CC IsoId=Q9Z1B3-1; Sequence=Displayed;
CC Name=B; Synonyms=C-beta-1b;
CC IsoId=Q9Z1B3-2; Sequence=VSP_008917;
CC Name=C;
CC IsoId=Q9Z1B3-3; Sequence=VSP_008918;
CC -!- PTM: Palmitoylated (PubMed:27653213). Palmitoylation at Cys-17 by
CC ZDHHC21 regulates the signaling activity of PLCB1 and the function of
CC the endothelial barrier (Probable). Palmitoylation by ZDHHC21 is
CC stimulated by inflammation (PubMed:27653213).
CC {ECO:0000269|PubMed:27653213, ECO:0000305|PubMed:27653213}.
CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
CC mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
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DR EMBL; U85712; AAD00571.1; -; mRNA.
DR EMBL; U85713; AAD00572.1; -; mRNA.
DR EMBL; U85714; AAD00573.1; -; mRNA.
DR EMBL; AF498249; AAM22966.1; -; mRNA.
DR EMBL; AF498250; AAM22967.1; -; mRNA.
DR EMBL; AL840635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL935278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058710; AAH58710.1; -; mRNA.
DR EMBL; AF022801; AAD01749.1; -; mRNA.
DR EMBL; X95344; CAA64637.1; -; mRNA.
DR CCDS; CCDS16787.1; -. [Q9Z1B3-2]
DR CCDS; CCDS50729.1; -. [Q9Z1B3-1]
DR PIR; S68256; S68256.
DR RefSeq; NP_001139302.1; NM_001145830.1. [Q9Z1B3-1]
DR RefSeq; NP_062651.2; NM_019677.2. [Q9Z1B3-2]
DR AlphaFoldDB; Q9Z1B3; -.
DR SMR; Q9Z1B3; -.
DR BioGRID; 202232; 10.
DR IntAct; Q9Z1B3; 5.
DR MINT; Q9Z1B3; -.
DR STRING; 10090.ENSMUSP00000105743; -.
DR iPTMnet; Q9Z1B3; -.
DR PhosphoSitePlus; Q9Z1B3; -.
DR SwissPalm; Q9Z1B3; -.
DR MaxQB; Q9Z1B3; -.
DR PaxDb; Q9Z1B3; -.
DR PeptideAtlas; Q9Z1B3; -.
DR PRIDE; Q9Z1B3; -.
DR ProteomicsDB; 289918; -. [Q9Z1B3-1]
DR ProteomicsDB; 289919; -. [Q9Z1B3-2]
DR ProteomicsDB; 289920; -. [Q9Z1B3-3]
DR Antibodypedia; 3795; 278 antibodies from 36 providers.
DR DNASU; 18795; -.
DR Ensembl; ENSMUST00000070724; ENSMUSP00000064844; ENSMUSG00000051177. [Q9Z1B3-2]
DR Ensembl; ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177. [Q9Z1B3-1]
DR Ensembl; ENSMUST00000131552; ENSMUSP00000118756; ENSMUSG00000051177. [Q9Z1B3-2]
DR GeneID; 18795; -.
DR KEGG; mmu:18795; -.
DR UCSC; uc008mnx.2; mouse. [Q9Z1B3-2]
DR UCSC; uc008mny.2; mouse. [Q9Z1B3-1]
DR CTD; 23236; -.
DR MGI; MGI:97613; Plcb1.
DR VEuPathDB; HostDB:ENSMUSG00000051177; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000155428; -.
DR InParanoid; Q9Z1B3; -.
DR OMA; GKVNHKP; -.
DR PhylomeDB; Q9Z1B3; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 3474.
DR Reactome; R-MMU-112043; PLC beta mediated events.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-MMU-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-MMU-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR BioGRID-ORCS; 18795; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Plcb1; mouse.
DR PRO; PR:Q9Z1B3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z1B3; protein.
DR Bgee; ENSMUSG00000051177; Expressed in caudate-putamen and 239 other tissues.
DR ExpressionAtlas; Q9Z1B3; baseline and differential.
DR Genevisible; Q9Z1B3; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0005521; F:lamin binding; IPI:BHF-UCL.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:BHF-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:BHF-UCL.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IDA:BHF-UCL.
DR GO; GO:0007420; P:brain development; NAS:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IC:BHF-UCL.
DR GO; GO:1902618; P:cellular response to fluoride; ISO:MGI.
DR GO; GO:1905631; P:cellular response to glyceraldehyde; ISO:MGI.
DR GO; GO:1904637; P:cellular response to ionomycin; ISO:MGI.
DR GO; GO:1904117; P:cellular response to vasopressin; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:BHF-UCL.
DR GO; GO:0030218; P:erythrocyte differentiation; TAS:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IDA:BHF-UCL.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:BHF-UCL.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; ISO:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:BHF-UCL.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0030225; P:macrophage differentiation; NAS:BHF-UCL.
DR GO; GO:0007613; P:memory; IMP:BHF-UCL.
DR GO; GO:0006397; P:mRNA processing; TAS:BHF-UCL.
DR GO; GO:2000438; P:negative regulation of monocyte extravasation; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0001556; P:oocyte maturation; NAS:BHF-UCL.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:BHF-UCL.
DR GO; GO:2000560; P:positive regulation of CD24 production; IDA:BHF-UCL.
DR GO; GO:0048639; P:positive regulation of developmental growth; IMP:BHF-UCL.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:BHF-UCL.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISS:BHF-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:BHF-UCL.
DR GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; NAS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0080154; P:regulation of fertilization; IMP:BHF-UCL.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; IMP:SynGO.
DR GO; GO:0034284; P:response to monosaccharide; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:BHF-UCL.
DR CDD; cd13361; PH_PLC_beta; 1.
DR Gene3D; 1.20.1230.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR028400; PLC-beta1.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF12; PTHR10336:SF12; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF17787; PH_14; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PIRSF; PIRSF000956; PLC-beta; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lipoprotein; Membrane; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..1216
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-1"
FT /id="PRO_0000088487"
FT DOMAIN 316..467
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 540..656
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 656..786
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 469..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 887
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P10894"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT LIPID 17
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:27653213"
FT VAR_SEQ 1142..1216
FT /note="LQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPPSLASDAAKV
FT NLKSPSSEEIERENPGREFDTPL -> GEGPSSVLSEGCHEDPSVPPNFTPPNPQALKW
FT (in isoform B)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_008917"
FT VAR_SEQ 1199..1216
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:11471062"
FT /id="VSP_008918"
FT CONFLICT 28
FT /note="F -> L (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="I -> T (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="S -> T (in Ref. 5; AAD01749)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="K -> E (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> A (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="R -> I (in Ref. 6; CAA64637)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="L -> I (in Ref. 6; CAA64637)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="V -> M (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="K -> T (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="V -> D (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="Q -> H (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 957
FT /note="N -> I (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="K -> T (in Ref. 1; AAD00571/AAD00572/AAD00573)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 138396 MW; CC751D49895A47D0 CRC64;
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL
RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHNE IRQQILDEKP
KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSPSS
EEIERENPGR EFDTPL
