ID   PLCB1_BOVIN             Reviewed;        1216 AA.
AC   P10894;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   27-MAR-2024, entry version 187.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2455601; DOI=10.1016/0092-8674(88)90549-1;
RA   Katan M., Kriz R.W., Totty N., Philp R., Meldrum E., Aldape R.A.,
RA   Knopf J.L., Parker P.J.;
RT   "Determination of the primary structure of PLC-154 demonstrates diversity
RT   of phosphoinositide-specific phospholipase C activities.";
RL   Cell 54:171-177(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 879-889, AND PHOSPHORYLATION AT SER-887.
RX   PubMed=2211670; DOI=10.1016/s0021-9258(18)38254-1;
RA   Ryu S.H., Kim U.H., Wahl M.I., Brown A.B., Carpenter G., Huang K.P.,
RA   Rhee S.G.;
RT   "Feedback regulation of phospholipase C-beta by protein kinase C.";
RL   J. Biol. Chem. 265:17941-17945(1990).
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. Regulates the function of the endothelial barrier.
CC       {ECO:0000250|UniProtKB:Q9Z1B3}.
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:P10687};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000250|UniProtKB:P10687};
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;
CC   -!- SUBUNIT: Interacts with DGKQ. {ECO:0000250|UniProtKB:Q9NQ66}.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}.
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:0000250|UniProtKB:Q9Z1B3}.
CC   -!- PTM: Palmitoylated. Palmitoylation at Cys-17 by ZDHHC21 regulates the
CC       signaling activity of PLCB1 and the function of the endothelial
CC       barrier. Palmitoylation by ZDHHC21 is stimulated by inflammation.
CC       {ECO:0000250|UniProtKB:Q9Z1B3}.
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; J03137; AAA30702.1; -; mRNA.
DR   PIR; A28822; A28822.
DR   RefSeq; NP_777242.1; NM_174817.1.
DR   AlphaFoldDB; P10894; -.
DR   SMR; P10894; -.
DR   BioGRID; 160009; 2.
DR   MINT; P10894; -.
DR   STRING; 9913.ENSBTAP00000046644; -.
DR   iPTMnet; P10894; -.
DR   PaxDb; 9913-ENSBTAP00000046644; -.
DR   Ensembl; ENSBTAT00000049812.4; ENSBTAP00000046644.3; ENSBTAG00000008338.6.
DR   GeneID; 287026; -.
DR   KEGG; bta:287026; -.
DR   CTD; 23236; -.
DR   VEuPathDB; HostDB:ENSBTAG00000008338; -.
DR   VGNC; VGNC:32980; PLCB1.
DR   eggNOG; KOG1265; Eukaryota.
DR   GeneTree; ENSGT00940000155428; -.
DR   HOGENOM; CLU_002738_2_0_1; -.
DR   InParanoid; P10894; -.
DR   OMA; GKVNHKP; -.
DR   OrthoDB; 2900494at2759; -.
DR   TreeFam; TF313216; -.
DR   Reactome; R-BTA-112043; PLC beta mediated events.
DR   Reactome; R-BTA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-BTA-399997; Acetylcholine regulates insulin secretion.
DR   Reactome; R-BTA-4086398; Ca2+ pathway.
DR   Reactome; R-BTA-416476; G alpha (q) signalling events.
DR   Reactome; R-BTA-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-BTA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR   Reactome; R-BTA-500657; Presynaptic function of Kainate receptors.
DR   SABIO-RK; P10894; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000008338; Expressed in occipital lobe and 94 other cell types or tissues.
DR   ExpressionAtlas; P10894; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IMP:AgBase.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007613; P:memory; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR   CDD; cd00275; C2_PLC_like; 1.
DR   CDD; cd16208; EFh_PI-PLCbeta1; 1.
DR   CDD; cd13361; PH_PLC_beta; 1.
DR   CDD; cd08591; PI-PLCc_beta; 1.
DR   Gene3D; 2.30.29.240; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR   Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 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_EF.
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:SF12; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-1; 1.
DR   PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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; SSF69989; C-terminal domain of PLC-beta; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF51695; PLC-like phosphodiesterases; 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   Calcium; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Lipoprotein; Membrane; Nucleus;
KW   Palmitate; Phosphoprotein; Reference proteome; Transducer.
FT   CHAIN           1..1216
FT                   /note="1-phosphatidylinositol 4,5-bisphosphate
FT                   phosphodiesterase beta-1"
FT                   /id="PRO_0000088485"
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..784
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          933..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1172..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        860..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..982
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1175..1201
FT                   /note="Polar 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:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         509
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         511
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         582
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         887
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:2211670"
FT   MOD_RES         978
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         987
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         1199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   MOD_RES         1200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
FT   LIPID           17
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1B3"
SQ   SEQUENCE   1216 AA;  138715 MW;  BEF809177F1B7ABB CRC64;
     MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WEDDSTVVTP IILRTDPQGF FFYWTDQNKE
     TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGRLEH RMITVVYGPD LVNISHLNLV
     AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
     DRKRVETALE ACSLPSSRND SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
     TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLAKKGQI SVDGFMRYLS
     GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
     ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
     QAKMAEYCRL IFGDALLMEP LDKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
     KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
     SNLVNYIQPV KFESFEISKK RNRSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
     GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
     HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
     NAVNPIWEEE PIVFKKVVLP SLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
     NQPLMLPALF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
     EADPGETPSE APSEARPTPA ENGVNHTTSL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS
     VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT KYNEIQNDYL
     RRRAALEKTA KKDNKKKSEP SSPDHVSSTI EQDLAALDAE MTQKLVDLKD KQQQQLLNLR
     QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
     TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP
     KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHS SAPPLMTSDS GKLNQKPPSS
     EELEGENPGK EFDTPL
//