PLCB3_HUMAN
ID PLCB3_HUMAN Reviewed; 1234 AA.
AC Q01970; A5PKZ6; G5E960; Q8N1A4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:9188725};
DE AltName: Full=Phosphoinositide phospholipase C-beta-3;
DE AltName: Full=Phospholipase C-beta-3;
DE Short=PLC-beta-3;
GN Name=PLCB3 {ECO:0000312|EMBL:AAA77683.1};
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 [GENOMIC DNA].
RX PubMed=7612006; DOI=10.1006/bbrc.1995.1955;
RA Mazuruk K., Schoen T.J., Chader G.J., Rodriguez I.R.;
RT "Structural organization and expression of the human phosphatidylinositol-
RT specific phospholipase C beta-3 gene.";
RL Biochem. Biophys. Res. Commun. 212:190-195(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7607669; DOI=10.1016/0888-7543(95)80164-h;
RA Lagercrantz J., Carson E., Phelan C., Grimmond S., Rosen A., Dare E.,
RA Nordenskjoeld M., Hayward N.K., Larsson C., Weber G.;
RT "Genomic organization and complete cDNA sequence of the human
RT phosphoinositide-specific phospholipase C beta 3 gene (PLCB3).";
RL Genomics 26:467-472(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 184-1234 (ISOFORM 1/2).
RX PubMed=1333955; DOI=10.1111/j.1432-1033.1992.tb17450.x;
RA Carozzi A.J., Kriz R.W., Webster C., Parker P.J.;
RT "Identification, purification and characterization of a novel
RT phosphatidylinositol-specific phospholipase C, a third member of the beta
RT subfamily.";
RL Eur. J. Biochem. 210:521-529(1992).
RN [7]
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 [8]
RP INTERACTION WITH LPAR2.
RX PubMed=15143197; DOI=10.1128/mcb.24.11.5069-5079.2004;
RA Oh Y.-S., Jo N.W., Choi J.W., Kim H.S., Seo S.-W., Kang K.-O., Hwang J.-I.,
RA Heo K., Kim S.-H., Kim Y.-H., Kim I.-H., Kim J.H., Banno Y., Ryu S.H.,
RA Suh P.-G.;
RT "NHERF2 specifically interacts with LPA2 receptor and defines the
RT specificity and efficiency of receptor-mediated phospholipase C-beta3
RT activation.";
RL Mol. Cell. Biol. 24:5069-5079(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-537 AND SER-1105,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-926, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-495 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP INVOLVEMENT IN SMDCD, VARIANT SMDCD SER-878, CHARACTERIZATION OF VARIANT
RP SMDCD SER-878, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29122926; DOI=10.1136/jmedgenet-2017-104827;
RA Ben-Salem S., Robbins S.M., Lm Sobreira N., Lyon A., Al-Shamsi A.M.,
RA Islam B.K., Akawi N.A., John A., Thachillath P., Al Hamed S., Valle D.,
RA Ali B.R., Al-Gazali L.;
RT "Defect in phosphoinositide signalling through a homozygous variant in
RT PLCB3 causes a new form of spondylometaphyseal dysplasia with corneal
RT dystrophy.";
RL J. Med. Genet. 55:122-130(2018).
CC -!- FUNCTION: The production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated
CC by activated phosphatidylinositol-specific phospholipase C enzymes.
CC {ECO:0000269|PubMed:29122926, 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:Q99JE6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:Q99JE6};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBUNIT: Interacts with SHANK2 (By similarity). Interacts with LPAR2
CC (PubMed:15143197). {ECO:0000250|UniProtKB:Q99JE6,
CC ECO:0000269|PubMed:15143197}.
CC -!- INTERACTION:
CC Q01970; P21279: Gnaq; Xeno; NbExp=6; IntAct=EBI-4289548, EBI-771975;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29122926}. Membrane
CC {ECO:0000250|UniProtKB:Q99JE6}. Nucleus {ECO:0000250|UniProtKB:P51432}.
CC Note=And particulate fractions. {ECO:0000250|UniProtKB:Q99JE6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01970-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01970-2; Sequence=VSP_046054;
CC -!- DISEASE: Spondylometaphyseal dysplasia with corneal dystrophy (SMDCD)
CC [MIM:618961]: An autosomal recessive disorder characterized by
CC postnatal growth deficiency, profound limb shortening with proximal and
CC distal segments involvement, narrow chest, radiological abnormalities
CC involving the spine, pelvis and metaphyses, corneal clouding, and
CC intellectual disability. {ECO:0000269|PubMed:29122926}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32659.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U26425; AAA77683.1; -; Genomic_DNA.
DR EMBL; Z37544; CAA85776.1; -; Genomic_DNA.
DR EMBL; Z37545; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37546; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37547; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37548; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37549; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37550; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37551; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37552; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37553; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37554; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37555; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37556; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37557; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37558; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37559; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37560; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37561; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37562; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37564; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37565; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37566; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37567; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37568; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37569; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37570; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37571; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37572; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37573; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; Z37574; CAA85776.1; JOINED; Genomic_DNA.
DR EMBL; AP001453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74230.1; -; Genomic_DNA.
DR EMBL; CH471076; EAW74231.1; -; Genomic_DNA.
DR EMBL; BC032659; AAH32659.1; ALT_INIT; mRNA.
DR EMBL; BC142681; AAI42682.1; -; mRNA.
DR EMBL; Z16411; CAA78903.1; -; mRNA.
DR CCDS; CCDS53654.1; -. [Q01970-2]
DR CCDS; CCDS8064.1; -. [Q01970-1]
DR PIR; I38994; I38994.
DR PIR; S27002; S27002.
DR PIR; S52099; S52099.
DR RefSeq; NP_000923.1; NM_000932.2. [Q01970-1]
DR RefSeq; NP_001171812.1; NM_001184883.1. [Q01970-2]
DR RefSeq; NP_001303243.1; NM_001316314.1. [Q01970-1]
DR PDB; 4GNK; X-ray; 4.00 A; B/D=10-1234, E=934-1192.
DR PDB; 4QJ3; X-ray; 3.00 A; B=10-891.
DR PDB; 4QJ4; X-ray; 3.30 A; B=10-891.
DR PDB; 4QJ5; X-ray; 3.41 A; B=10-891.
DR PDB; 7SQ2; X-ray; 2.60 A; B=10-886.
DR PDBsum; 4GNK; -.
DR PDBsum; 4QJ3; -.
DR PDBsum; 4QJ4; -.
DR PDBsum; 4QJ5; -.
DR PDBsum; 7SQ2; -.
DR AlphaFoldDB; Q01970; -.
DR SMR; Q01970; -.
DR BioGRID; 111347; 80.
DR CORUM; Q01970; -.
DR DIP; DIP-41928N; -.
DR IntAct; Q01970; 8.
DR MINT; Q01970; -.
DR STRING; 9606.ENSP00000443631; -.
DR BindingDB; Q01970; -.
DR ChEMBL; CHEMBL5449; -.
DR SwissLipids; SLP:000001756; -.
DR iPTMnet; Q01970; -.
DR PhosphoSitePlus; Q01970; -.
DR BioMuta; PLCB3; -.
DR DMDM; 1730573; -.
DR EPD; Q01970; -.
DR jPOST; Q01970; -.
DR MassIVE; Q01970; -.
DR MaxQB; Q01970; -.
DR PaxDb; Q01970; -.
DR PeptideAtlas; Q01970; -.
DR PRIDE; Q01970; -.
DR ProteomicsDB; 33840; -.
DR ProteomicsDB; 58024; -. [Q01970-1]
DR Antibodypedia; 3983; 413 antibodies from 36 providers.
DR DNASU; 5331; -.
DR Ensembl; ENST00000279230.12; ENSP00000279230.6; ENSG00000149782.13. [Q01970-1]
DR Ensembl; ENST00000325234.5; ENSP00000324660.5; ENSG00000149782.13. [Q01970-2]
DR Ensembl; ENST00000540288.5; ENSP00000443631.1; ENSG00000149782.13. [Q01970-1]
DR GeneID; 5331; -.
DR KEGG; hsa:5331; -.
DR MANE-Select; ENST00000279230.12; ENSP00000279230.6; NM_000932.5; NP_000923.1.
DR UCSC; uc009ypg.3; human. [Q01970-1]
DR CTD; 5331; -.
DR DisGeNET; 5331; -.
DR GeneCards; PLCB3; -.
DR HGNC; HGNC:9056; PLCB3.
DR HPA; ENSG00000149782; Tissue enhanced (intestine).
DR MalaCards; PLCB3; -.
DR MIM; 600230; gene.
DR MIM; 618961; phenotype.
DR neXtProt; NX_Q01970; -.
DR OpenTargets; ENSG00000149782; -.
DR Orphanet; 589435; Spondylometaphyseal dysplasia-corneal dystrophy syndrome.
DR PharmGKB; PA33386; -.
DR VEuPathDB; HostDB:ENSG00000149782; -.
DR eggNOG; KOG1265; Eukaryota.
DR GeneTree; ENSGT00940000160539; -.
DR HOGENOM; CLU_002738_2_0_1; -.
DR InParanoid; Q01970; -.
DR OMA; PNMEVDI; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q01970; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 2681.
DR PathwayCommons; Q01970; -.
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; Q01970; -.
DR SIGNOR; Q01970; -.
DR BioGRID-ORCS; 5331; 21 hits in 1078 CRISPR screens.
DR ChiTaRS; PLCB3; human.
DR GeneWiki; PLCB3; -.
DR GenomeRNAi; 5331; -.
DR Pharos; Q01970; Tbio.
DR PRO; PR:Q01970; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q01970; protein.
DR Bgee; ENSG00000149782; Expressed in lower esophagus mucosa and 140 other tissues.
DR Genevisible; Q01970; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IDA:BHF-UCL.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0004629; F:phospholipase C activity; TAS:Reactome.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0003073; P:regulation of systemic arterial blood pressure; IDA:MGI.
DR CDD; cd13361; PH_PLC_beta; 1.
DR DisProt; DP02477; -.
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; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
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 Pfam; PF00168; C2; 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 3D-structure; Acetylation; Alternative splicing; Calcium; Cytoplasm;
KW Dwarfism; Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1234
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase beta-3"
FT /id="PRO_0000088491"
FT DOMAIN 318..468
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 590..706
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 707..835
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 467..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1234
FT /note="Interaction with SHANK2"
FT /evidence="ECO:0000250"
FT COMPBIAS 485..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 379
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 33..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046054"
FT VARIANT 483
FT /note="R -> H (in dbSNP:rs12146487)"
FT /id="VAR_029229"
FT VARIANT 878
FT /note="A -> S (in SMDCD; strong reduction in protein levels
FT and marked increase in cellular phosphatidylinositol 4,5
FT bisphosphate levels in patient cells)"
FT /evidence="ECO:0000269|PubMed:29122926"
FT /id="VAR_084509"
FT CONFLICT 845
FT /note="S -> L (in Ref. 6; CAA78903)"
FT /evidence="ECO:0000305"
FT CONFLICT 881
FT /note="G -> E (in Ref. 2; CAA85776)"
FT /evidence="ECO:0000305"
FT CONFLICT 1089..1119
FT /note="REKKELQKILDRKRHNSISEAKMRDKHKKEA -> SWPSWPRSVRSSGRGSP
FT RRSAGACWARCRRG (in Ref. 2; CAA85776)"
FT /evidence="ECO:0000305"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4QJ3"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:4QJ3"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:4QJ3"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:7SQ2"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:7SQ2"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 269..279
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 389..399
FT /evidence="ECO:0007829|PDB:7SQ2"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:4QJ3"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 578..581
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 588..591
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 616..621
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 622..631
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 633..640
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 645..648
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 662..665
FT /evidence="ECO:0007829|PDB:7SQ2"
FT TURN 666..668
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 681..691
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 726..737
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 740..742
FT /evidence="ECO:0007829|PDB:4QJ3"
FT STRAND 745..754
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 759..763
FT /evidence="ECO:0007829|PDB:4QJ4"
FT STRAND 771..773
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 781..787
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 793..800
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 805..812
FT /evidence="ECO:0007829|PDB:7SQ2"
FT TURN 813..815
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 819..826
FT /evidence="ECO:0007829|PDB:7SQ2"
FT STRAND 832..846
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 850..852
FT /evidence="ECO:0007829|PDB:4QJ5"
FT HELIX 853..860
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 862..874
FT /evidence="ECO:0007829|PDB:7SQ2"
FT HELIX 877..880
FT /evidence="ECO:0007829|PDB:4QJ3"
SQ SEQUENCE 1234 AA; 138799 MW; C5106EFBA8037788 CRC64;
MAGAQPGVHA LQLEPPTVVE TLRRGSKFIK WDEETSSRNL VTLRVDPNGF FLYWTGPNME
VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDARLE EKLMTVVSGP DPVNTVFLNF
MAVQDDTAKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS
ADKKRVETAL ESCGLKFNRS ESIRPDEFSL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY
LTLEQLMDFI NQKQRDPRLN EVLYPPLRPS QARLLIEKYE PNQQFLERDQ MSMEGFSRYL
GGEENGILPL EALDLSTDMT QPLSAYFINS SHNTYLTAGQ LAGTSSVEMY RQALLWGCRC
VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAETA FKTSPYPVIL SFENHVDSAK
QQAKMAEYCR SIFGDALLIE PLDKYPLAPG VPLPSPQDLM GRILVKNKKR HRPSAGGPDS
AGRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKP SLEPQKSLGD
EGLNRGPYVL GPADREDEEE DEEEEEQTDP KKPTTDEGTA SSEVNATEEM STLVNYIEPV
KFKSFEAARK RNKCFEMSSF VETKAMEQLT KSPMEFVEYN KQQLSRIYPK GTRVDSSNYM
PQLFWNVGCQ LVALNFQTLD VAMQLNAGVF EYNGRSGYLL KPEFMRRPDK SFDPFTEVIV
DGIVANALRV KVISGQFLSD RKVGIYVEVD MFGLPVDTRR KYRTRTSQGN SFNPVWDEEP
FDFPKVVLPT LASLRIAAFE EGGKFVGHRI LPVSAIRSGY HYVCLRNEAN QPLCLPALLI
YTEASDYIPD DHQDYAEALI NPIKHVSLMD QRARQLAALI GESEAQAGQE TCQDTQSQQL
GSQPSSNPTP SPLDASPRRP PGPTTSPAST SLSSPGQRDD LIASILSEVA PTPLDELRGH
KALVKLRSRQ ERDLRELRKK HQRKAVTLTR RLLDGLAQAQ AEGRCRLRPG ALGGAADVED
TKEGEDEAKR YQEFQNRQVQ SLLELREAQV DAEAQRRLEH LRQALQRLRE VVLDANTTQF
KRLKEMNERE KKELQKILDR KRHNSISEAK MRDKHKKEAE LTEINRRHIT ESVNSIRRLE
EAQKQRHDRL VAGQQQVLQQ LAEEEPKLLA QLAQECQEQR ARLPQEIRRS LLGEMPEGLG
DGPLVACASN GHAPGSSGHL SGADSESQEE NTQL
