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
//
