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 01-MAY-2013, entry version 116.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1;
DE EC=3.1.4.11;
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; Synonyms=Plcb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Swiss;
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
RT and 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
RT within 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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=C57BL/6; 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-145.
RC STRAIN=C57BL/6;
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
RT isoforms of 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;
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+
RT spiking.";
RL Biochem. J. 316:583-591(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; TYR-334 AND
RP THR-336, AND MASS SPECTROMETRY.
RC TISSUE=Forebrain;
RX PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA Blackstock W.P., Choudhary J.S., Grant S.G.;
RT "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL J. Biol. Chem. 280:5972-5982(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in
RT naive and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [9]
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
RT to caveolae in adult cardiac myocytes.";
RL Circ. Res. 103:992-1000(2008).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC mediated by activated phosphatidylinositol-specific phospholipase
CC C enzymes (By similarity).
CC -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC diacylglycerol.
CC -!- COFACTOR: Calcium (By similarity).
CC -!- SUBUNIT: Interacts with DGKQ (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus membrane. Cytoplasm (By similarity).
CC Note=Colocalizes with the adrenergic receptors, ADREN1A and
CC ADREN1B, at the nuclear membrane of cardiac myocytes (By
CC similarity).
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 Note=No experimental confirmation available;
CC -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
CC mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
CC -!- SIMILARITY: Contains 1 C2 domain.
CC -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
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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; AL928635; CAM23602.1; -; Genomic_DNA.
DR EMBL; AL840635; CAM23602.1; JOINED; Genomic_DNA.
DR EMBL; AL928956; CAM23602.1; JOINED; Genomic_DNA.
DR EMBL; AL935278; CAM23602.1; JOINED; Genomic_DNA.
DR EMBL; AL840635; CAM23766.1; -; Genomic_DNA.
DR EMBL; AL928635; CAM23766.1; JOINED; Genomic_DNA.
DR EMBL; AL928956; CAM23766.1; JOINED; Genomic_DNA.
DR EMBL; AL935278; CAM23766.1; JOINED; Genomic_DNA.
DR EMBL; AL928956; CAM26804.1; -; Genomic_DNA.
DR EMBL; AL840635; CAM26804.1; JOINED; Genomic_DNA.
DR EMBL; AL928635; CAM26804.1; JOINED; Genomic_DNA.
DR EMBL; AL935278; CAM26804.1; JOINED; Genomic_DNA.
DR EMBL; AL935278; CAM27130.1; -; Genomic_DNA.
DR EMBL; AL840635; CAM27130.1; JOINED; Genomic_DNA.
DR EMBL; AL928635; CAM27130.1; JOINED; Genomic_DNA.
DR EMBL; AL928956; CAM27130.1; JOINED; Genomic_DNA.
DR EMBL; BC058710; AAH58710.1; -; mRNA.
DR EMBL; AF022801; AAD01749.1; -; mRNA.
DR EMBL; X95344; CAA64637.1; -; mRNA.
DR IPI; IPI00130045; -.
DR IPI; IPI00323250; -.
DR IPI; IPI00468121; -.
DR PIR; S68256; S68256.
DR RefSeq; NP_001139302.1; NM_001145830.1.
DR RefSeq; NP_062651.2; NM_019677.2.
DR UniGene; Mm.330607; -.
DR ProteinModelPortal; Q9Z1B3; -.
DR SMR; Q9Z1B3; 12-833, 1001-1170.
DR IntAct; Q9Z1B3; 3.
DR PhosphoSite; Q9Z1B3; -.
DR PaxDb; Q9Z1B3; -.
DR PRIDE; Q9Z1B3; -.
DR Ensembl; ENSMUST00000070724; ENSMUSP00000064844; ENSMUSG00000051177.
DR Ensembl; ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177.
DR GeneID; 18795; -.
DR KEGG; mmu:18795; -.
DR CTD; 23236; -.
DR MGI; MGI:97613; Plcb1.
DR eggNOG; NOG149692; -.
DR GeneTree; ENSGT00700000104415; -.
DR HOVERGEN; HBG053609; -.
DR InParanoid; Q6PDH1; -.
DR KO; K05858; -.
DR OMA; YRVFLNN; -.
DR OrthoDB; EOG40S0DW; -.
DR BRENDA; 3.1.4.11; 3474.
DR Reactome; REACT_112621; Metabolism.
DR ChiTaRS; PLCB1; mouse.
DR NextBio; 295080; -.
DR ArrayExpress; Q9Z1B3; -.
DR Bgee; Q9Z1B3; -.
DR CleanEx; MM_PLCB1; -.
DR Genevestigator; Q9Z1B3; -.
DR GermOnline; ENSMUSG00000051177; Mus musculus.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IEA:Compara.
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:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; IDA:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IC:BHF-UCL.
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:0051318; P:G1 phase; IDA: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: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; IEA:Compara.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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-dependent; IDA:BHF-UCL.
DR GO; GO:0001556; P:oocyte maturation; NAS:BHF-UCL.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:BHF-UCL.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IMP:BHF-UCL.
DR GO; GO:2000560; P:positive regulation of CD24 biosynthetic process; 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: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:hydrogen antiporter activity; NAS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:BHF-UCL.
DR GO; GO:0080154; P:regulation of fertilization; IMP:BHF-UCL.
DR GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IMP:BHF-UCL.
DR Gene3D; 1.10.238.10; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR InterPro; IPR000008; C2_Ca-dep.
DR InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR InterPro; IPR018029; C2_membr_targeting.
DR InterPro; IPR011992; EF-hand-like_dom.
DR InterPro; IPR001192; Pinositol_PLipase_C.
DR InterPro; IPR016280; PLC-beta.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLipase_C_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 Pfam; PF00168; C2; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF09279; efhand_like; 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; SSF49562; C2_CaLB; 1.
DR SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 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; Complete proteome; Cytoplasm;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1 1216 1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-1.
FT /FTId=PRO_0000088487.
FT DOMAIN 316 467 PI-PLC X-box.
FT DOMAIN 540 656 PI-PLC Y-box.
FT DOMAIN 663 761 C2.
FT COMPBIAS 914 1088 Lys-rich.
FT ACT_SITE 331 331 By similarity.
FT ACT_SITE 378 378 By similarity.
FT MOD_RES 333 333 Phosphothreonine.
FT MOD_RES 334 334 Phosphotyrosine.
FT MOD_RES 336 336 Phosphothreonine.
FT MOD_RES 887 887 Phosphoserine; by PKC (By similarity).
FT MOD_RES 1197 1197 Phosphoserine.
FT VAR_SEQ 1142 1216 LQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSA
FT PPSLASDAAKVNLKSPSSEEIERENPGREFDTPL -> GEG
FT PSSVLSEGCHEDPSVPPNFTPPNPQALKW (in isoform
FT B).
FT /FTId=VSP_008917.
FT VAR_SEQ 1199 1216 Missing (in isoform C).
FT /FTId=VSP_008918.
FT CONFLICT 28 28 F -> L (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 41 41 I -> T (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 67 67 S -> T (in Ref. 5; AAD01749).
FT CONFLICT 79 79 K -> E (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 112 112 V -> A (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 561 561 R -> I (in Ref. 6; CAA64637).
FT CONFLICT 613 613 L -> I (in Ref. 6; CAA64637).
FT CONFLICT 622 622 V -> M (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 714 714 K -> T (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 795 795 V -> D (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 923 923 Q -> H (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 957 957 N -> I (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
FT CONFLICT 1084 1084 K -> T (in Ref. 1; AAD00571/AAD00572/
FT AAD00573).
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
//
