PLCB1_HUMAN
ID PLCB1_HUMAN Reviewed; 1216 AA.
AC Q9NQ66; D3DW12; D3DW13; O60325; Q17RQ6; Q5TFF7; Q5TGC9; Q8IV93; Q9BQW2;
AC Q9H4H2; Q9H8H5; Q9NQ65; Q9NQH9; Q9NTH4; Q9UJP6; Q9UM26;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:9188725};
DE AltName: Full=PLC-154;
DE AltName: Full=Phosphoinositide phospholipase C-beta-1;
DE AltName: Full=Phospholipase C-I;
DE Short=PLC-I;
DE AltName: Full=Phospholipase C-beta-1;
DE Short=PLC-beta-1;
GN Name=PLCB1 {ECO:0000312|HGNC:HGNC:15917}; Synonyms=KIAA0581;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC TISSUE=Brain;
RX PubMed=11118617; DOI=10.1016/s0167-4781(00)00260-8;
RA Caricasole A., Sala C., Roncarati R., Formenti E., Terstappen G.C.;
RT "Cloning and characterization of the human phosphoinositide-specific
RT phospholipase C-beta 1 (PLCbeta1).";
RL Biochim. Biophys. Acta 1517:63-72(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Brain;
RX PubMed=10760467; DOI=10.1016/s1388-1981(00)00012-3;
RA Peruzzi D., Calabrese G., Faenza I., Manzoli L., Matteucci A.,
RA Gianfrancesco F., Billi A.M., Stuppia L., Palka G., Cocco L.;
RT "Identification and chromosomal localisation by fluorescence in situ
RT hybridisation of human gene of phosphoinositide-specific phospholipase C
RT beta 1.";
RL Biochim. Biophys. Acta 1484:175-182(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC 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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1216 (ISOFORM B).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 417-1062 (ISOFORMS A AND B).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9188725; DOI=10.1021/bi9702288;
RA Tall E., Dorman G., Garcia P., Runnels L., Shah S., Chen J., Profit A.,
RA Gu Q.M., Chaudhary A., Prestwich G.D., Rebecchi M.J.;
RT "Phosphoinositide binding specificity among phospholipase C isozymes as
RT determined by photo-cross-linking to novel substrate and product analogs.";
RL Biochemistry 36:7239-7248(1997).
RN [11]
RP INTERACTION WITH DGKQ.
RX PubMed=12799190; DOI=10.1016/s0014-4827(03)00115-0;
RA Tabellini G., Bortul R., Santi S., Riccio M., Baldini G., Cappellini A.,
RA Billi A.M., Berezney R., Ruggeri A., Cocco L., Martelli A.M.;
RT "Diacylglycerol kinase-theta is localized in the speckle domains of the
RT nucleus.";
RL Exp. Cell Res. 287:143-154(2003).
RN [12]
RP INVOLVEMENT IN DEE12.
RX PubMed=20833646; DOI=10.1093/brain/awq238;
RA Kurian M.A., Meyer E., Vassallo G., Morgan N.V., Prakash N., Pasha S.,
RA Hai N.A., Shuib S., Rahman F., Wassmer E., Cross J.H., O'Callaghan F.J.,
RA Osborne J.P., Scheffer I.E., Gissen P., Maher E.R.;
RT "Phospholipase C beta 1 deficiency is associated with early-onset epileptic
RT encephalopathy.";
RL Brain 133:2964-2970(2010).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-907.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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:9188725). Regulates the function of the
CC endothelial barrier. {ECO:0000250|UniProtKB:Q9Z1B3,
CC ECO:0000269|PubMed:9188725}.
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:0000269|PubMed:9188725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:9188725};
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:0000269|PubMed:12799190}.
CC -!- INTERACTION:
CC Q9NQ66; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-3396023, EBI-742887;
CC Q9NQ66; Q13363-2: CTBP1; NbExp=3; IntAct=EBI-3396023, EBI-10171858;
CC Q9NQ66; P56545: CTBP2; NbExp=3; IntAct=EBI-3396023, EBI-741533;
CC Q9NQ66; P56545-3: CTBP2; NbExp=3; IntAct=EBI-3396023, EBI-10171902;
CC Q9NQ66; Q12800: TFCP2; NbExp=3; IntAct=EBI-3396023, EBI-717422;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9NQ66-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9NQ66-2; Sequence=VSP_004718;
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 -!- DISEASE: Developmental and epileptic encephalopathy 12 (DEE12)
CC [MIM:613722]: A form of epilepsy characterized by frequent tonic
CC seizures or spasms beginning in infancy with a specific EEG finding of
CC suppression-burst patterns, characterized by high-voltage bursts
CC alternating with almost flat suppression phases. Patients may progress
CC to West syndrome, which is characterized by tonic spasms with
CC clustering, arrest of psychomotor development, and hypsarrhythmia on
CC EEG. {ECO:0000269|PubMed:20833646}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAA25507.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PLCB1ID41742ch20p12.html";
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DR EMBL; AJ278313; CAB98142.1; -; mRNA.
DR EMBL; AJ278314; CAB98143.1; -; mRNA.
DR EMBL; AY004175; AAF86613.1; -; mRNA.
DR EMBL; AB011153; BAA25507.3; ALT_INIT; mRNA.
DR EMBL; AL031683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL049632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10372.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10373.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10374.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10376.1; -; Genomic_DNA.
DR EMBL; BC069420; AAH69420.1; -; mRNA.
DR EMBL; BC117231; AAI17232.1; -; mRNA.
DR EMBL; AL137267; CAB70666.1; -; mRNA.
DR EMBL; AK023689; BAB14641.1; ALT_INIT; mRNA.
DR CCDS; CCDS13102.1; -. [Q9NQ66-1]
DR CCDS; CCDS13103.1; -. [Q9NQ66-2]
DR RefSeq; NP_056007.1; NM_015192.3. [Q9NQ66-1]
DR RefSeq; NP_877398.1; NM_182734.2. [Q9NQ66-2]
DR AlphaFoldDB; Q9NQ66; -.
DR SMR; Q9NQ66; -.
DR BioGRID; 116841; 46.
DR CORUM; Q9NQ66; -.
DR IntAct; Q9NQ66; 17.
DR MINT; Q9NQ66; -.
DR STRING; 9606.ENSP00000338185; -.
DR BindingDB; Q9NQ66; -.
DR ChEMBL; CHEMBL4034; -.
DR SwissLipids; SLP:000000662; -.
DR iPTMnet; Q9NQ66; -.
DR PhosphoSitePlus; Q9NQ66; -.
DR SwissPalm; Q9NQ66; -.
DR BioMuta; PLCB1; -.
DR DMDM; 12643814; -.
DR EPD; Q9NQ66; -.
DR jPOST; Q9NQ66; -.
DR MassIVE; Q9NQ66; -.
DR MaxQB; Q9NQ66; -.
DR PaxDb; Q9NQ66; -.
DR PeptideAtlas; Q9NQ66; -.
DR PRIDE; Q9NQ66; -.
DR ProteomicsDB; 82087; -. [Q9NQ66-1]
DR ProteomicsDB; 82088; -. [Q9NQ66-2]
DR Antibodypedia; 3795; 278 antibodies from 36 providers.
DR DNASU; 23236; -.
DR Ensembl; ENST00000338037.11; ENSP00000338185.6; ENSG00000182621.18. [Q9NQ66-1]
DR Ensembl; ENST00000378637.6; ENSP00000367904.2; ENSG00000182621.18. [Q9NQ66-2]
DR Ensembl; ENST00000378641.7; ENSP00000367908.3; ENSG00000182621.18. [Q9NQ66-2]
DR GeneID; 23236; -.
DR KEGG; hsa:23236; -.
DR MANE-Select; ENST00000338037.11; ENSP00000338185.6; NM_015192.4; NP_056007.1.
DR UCSC; uc002wna.5; human. [Q9NQ66-1]
DR CTD; 23236; -.
DR DisGeNET; 23236; -.
DR GeneCards; PLCB1; -.
DR HGNC; HGNC:15917; PLCB1.
DR HPA; ENSG00000182621; Tissue enhanced (brain).
DR MalaCards; PLCB1; -.
DR MIM; 607120; gene.
DR MIM; 613722; phenotype.
DR neXtProt; NX_Q9NQ66; -.
DR OpenTargets; ENSG00000182621; -.
DR Orphanet; 3451; Infantile spasms syndrome.
DR Orphanet; 293181; Malignant migrating focal seizures of infancy.
DR PharmGKB; PA33384; -.
DR VEuPathDB; HostDB:ENSG00000182621; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000155428; -.
DR InParanoid; Q9NQ66; -.
DR OMA; GKVNHKP; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q9NQ66; -.
DR TreeFam; TF313216; -.
DR BioCyc; MetaCyc:HS11935-MON; -.
DR BRENDA; 3.1.4.11; 2681.
DR PathwayCommons; Q9NQ66; -.
DR Reactome; R-HSA-112043; PLC beta mediated events.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-HSA-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-HSA-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR SignaLink; Q9NQ66; -.
DR SIGNOR; Q9NQ66; -.
DR BioGRID-ORCS; 23236; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; PLCB1; human.
DR GeneWiki; PLCB1; -.
DR GenomeRNAi; 23236; -.
DR Pharos; Q9NQ66; Tbio.
DR PRO; PR:Q9NQ66; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NQ66; protein.
DR Bgee; ENSG00000182621; Expressed in endothelial cell and 195 other tissues.
DR ExpressionAtlas; Q9NQ66; baseline and differential.
DR Genevisible; Q9NQ66; HS.
DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
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; NAS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0005521; F:lamin binding; IEA:Ensembl.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0004629; F:phospholipase C activity; TAS:Reactome.
DR GO; GO:0060466; P:activation of meiosis involved in egg activation; ISS:BHF-UCL.
DR GO; GO:1902618; P:cellular response to fluoride; IEA:Ensembl.
DR GO; GO:1905631; P:cellular response to glyceraldehyde; IEA:Ensembl.
DR GO; GO:1904637; P:cellular response to ionomycin; IEA:Ensembl.
DR GO; GO:1904117; P:cellular response to vasopressin; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; ISS:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:BHF-UCL.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:Ensembl.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035722; P:interleukin-12-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0007613; P:memory; ISS:BHF-UCL.
DR GO; GO:2000438; P:negative regulation of monocyte extravasation; ISS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IEA:Ensembl.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISS:BHF-UCL.
DR GO; GO:2000560; P:positive regulation of CD24 production; ISS:BHF-UCL.
DR GO; GO:0048639; P:positive regulation of developmental growth; ISS:BHF-UCL.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:BHF-UCL.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISS:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0080154; P:regulation of fertilization; ISS:BHF-UCL.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0099178; P:regulation of retrograde trans-synaptic signaling by endocanabinoid; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
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; Epilepsy; 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_0000088486"
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 963..994
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 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 851..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..982
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1194
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:0000250|UniProtKB:P10894"
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"
FT VAR_SEQ 1142..1216
FT /note="LQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKV
FT NHKTPSSEELGGDIPGKEFDTPL -> GEGSSSFLSETCHEDPSVSPNFTPPNPQALKW
FT (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11118617,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_004718"
FT VARIANT 854
FT /note="E -> K (in dbSNP:rs2076413)"
FT /id="VAR_050541"
FT VARIANT 907
FT /note="A -> P (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036547"
FT CONFLICT 1..34
FT /note="MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDD -> MGSLQGIATKILIR
FT ILSDALIRKETDLKS (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="L -> M (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="P -> L (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="L -> F (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="P -> L (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="L -> P (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="P -> T (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="Q -> R (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="V -> A (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="K -> R (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="E -> K (in Ref. 2; AAF86613)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="P -> S (in Ref. 1; CAB98143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 138567 MW; 6F4263D1A50C6FD1 CRC64;
MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
TELLDLSLVK DARCGRHAKA PKDPKLRELL DVGNIGRLEQ RMITVVYGPD LVNISHLNLV
AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
DRKRVETALE ACSLPSSRND SIPQEDFTPE VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NNSLARKGQI SVDGFMRYLS
GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
KLSEQASNTY SDSSSMFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
GTRVDSSNYM PQLFWNAGCQ MVALNFQTMD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
NAVNPVWEEE PIVFKKVVLP TLACLRIAVY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
EADPGETPSE APSEARTTPA ENGVNHTTTL TPKPPSQALH SQPAPGSVKA PAKTEDLIQS
VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTDLIKEHTT KYNEIQNDYL
RRRAALEKSA KKDSKKKSEP SSPDHGSSTI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHKE IRQQILDEKP
KLQVELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPLSLSSDP GKVNHKTPSS
EELGGDIPGK EFDTPL
