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Database: UniProt
Entry: PLCB1_MOUSE
LinkDB: PLCB1_MOUSE
Original site: 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   19-MAR-2014, entry version 126.
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   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   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; 11-830, 890-1170.
DR   BioGrid; 202232; 1.
DR   IntAct; Q9Z1B3; 4.
DR   MINT; MINT-4107696; -.
DR   PhosphoSite; Q9Z1B3; -.
DR   PaxDb; Q9Z1B3; -.
DR   PRIDE; Q9Z1B3; -.
DR   Ensembl; ENSMUST00000070724; ENSMUSP00000064844; ENSMUSG00000051177. [Q9Z1B3-2]
DR   Ensembl; ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177. [Q9Z1B3-1]
DR   GeneID; 18795; -.
DR   KEGG; mmu:18795; -.
DR   UCSC; uc008mny.2; mouse. [Q9Z1B3-1]
DR   CTD; 23236; -.
DR   MGI; MGI:97613; Plcb1.
DR   eggNOG; NOG149692; -.
DR   GeneTree; ENSGT00730000110266; -.
DR   HOVERGEN; HBG053609; -.
DR   InParanoid; Q6PDH1; -.
DR   KO; K05858; -.
DR   OMA; MMDFINL; -.
DR   OrthoDB; EOG7WDN1N; -.
DR   TreeFam; TF313216; -.
DR   BRENDA; 3.1.4.11; 3474.
DR   Reactome; REACT_188937; Metabolism.
DR   ChiTaRS; PLCB1; mouse.
DR   NextBio; 295080; -.
DR   PRO; PR:Q9Z1B3; -.
DR   ArrayExpress; Q9Z1B3; -.
DR   Bgee; Q9Z1B3; -.
DR   CleanEx; MM_PLCB1; -.
DR   Genevestigator; Q9Z1B3; -.
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:Ensembl.
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: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:Ensembl.
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-templated; 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: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:hydrogen antiporter activity; NAS:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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_dom.
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; 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   PANTHER; PTHR10336:SF12; PTHR10336:SF12; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF06631; DUF1154; 1.
DR   Pfam; PF09279; EF-hand_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; 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   2: Evidence at transcript 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     887    887       Phosphoserine; by PKC (By similarity).
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
//
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