PLCG1_MOUSE
ID PLCG1_MOUSE Reviewed; 1302 AA.
AC Q62077; Q6P1G1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000250|UniProtKB:P10686};
DE AltName: Full=Phosphoinositide phospholipase C-gamma-1;
DE AltName: Full=Phospholipase C-gamma-1;
DE Short=PLC-gamma-1;
GN Name=Plcg1 {ECO:0000312|MGI:MGI:97615}; Synonyms=Plcg-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 846-1052.
RC TISSUE=Oocyte;
RX PubMed=8687404; DOI=10.1042/bj3160583;
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+ spiking.";
RL Biochem. J. 316:583-591(1996).
RN [3]
RP INTERACTION WITH KIT, AND PHOSPHORYLATION.
RX PubMed=1714377; DOI=10.1002/j.1460-2075.1991.tb07784.x;
RA Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E.,
RA Bernstein A., Pawson T.;
RT "Signal transduction by normal isoforms and W mutant variants of the Kit
RT receptor tyrosine kinase.";
RL EMBO J. 10:2451-2459(1991).
RN [4]
RP INTERACTION WITH PDGFRA, AND ACTIVATION BY PDGFRA.
RX PubMed=1646396; DOI=10.1128/mcb.11.7.3780-3785.1991;
RA Yu J.C., Heidaran M.A., Pierce J.H., Gutkind J.S., Lombardi D.,
RA Ruggiero M., Aaronson S.A.;
RT "Tyrosine mutations within the alpha platelet-derived growth factor
RT receptor kinase insert domain abrogate receptor-associated
RT phosphatidylinositol-3 kinase activity without affecting mitogenic or
RT chemotactic signal transduction.";
RL Mol. Cell. Biol. 11:3780-3785(1991).
RN [5]
RP INTERACTION WITH PDGFRA.
RX PubMed=8943348; DOI=10.1128/mcb.16.12.6926;
RA Bazenet C.E., Gelderloos J.A., Kazlauskas A.;
RT "Phosphorylation of tyrosine 720 in the platelet-derived growth factor
RT alpha receptor is required for binding of Grb2 and SHP-2 but not for
RT activation of Ras or cell proliferation.";
RL Mol. Cell. Biol. 16:6926-6936(1996).
RN [6]
RP PHOSPHORYLATION, AND INTERACTION WITH FLT1.
RX PubMed=9299537; DOI=10.1006/bbrc.1997.7327;
RA Sawano A., Takahashi T., Yamaguchi S., Shibuya M.;
RT "The phosphorylated 1169-tyrosine containing region of flt-1 kinase (VEGFR-
RT 1) is a major binding site for PLCgamma.";
RL Biochem. Biophys. Res. Commun. 238:487-491(1997).
RN [7]
RP INTERACTION WITH KHDRBS1.
RX PubMed=10748127; DOI=10.1074/jbc.m909368199;
RA Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.;
RT "Arginine methylation inhibits the binding of proline-rich ligands to Src
RT homology 3, but not WW, domains.";
RL J. Biol. Chem. 275:16030-16036(2000).
RN [8]
RP INTERACTION WITH CBLB.
RX PubMed=10646608; DOI=10.1038/35003228;
RA Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T.,
RA Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A.,
RA Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M.;
RT "Negative regulation of lymphocyte activation and autoimmunity by the
RT molecular adaptor Cbl-b.";
RL Nature 403:211-216(2000).
RN [9]
RP INTERACTION WITH CLNK, AND DOMAIN.
RX PubMed=11463797; DOI=10.1074/jbc.m106390200;
RA Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
RT "MIST functions through distinct domains in immunoreceptor signaling in the
RT presence and absence of LAT.";
RL J. Biol. Chem. 276:36043-36050(2001).
RN [10]
RP INTERACTION WITH NTRK2.
RX PubMed=12367511; DOI=10.1016/s0896-6273(02)00942-x;
RA Minichiello L., Calella A.M., Medina D.L., Bonhoeffer T., Klein R.,
RA Korte M.;
RT "Mechanism of TrkB-mediated hippocampal long-term potentiation.";
RL Neuron 36:121-137(2002).
RN [11]
RP PHOSPHORYLATION, UBIQUITINATION, AND FUNCTION.
RX PubMed=15308098; DOI=10.1016/j.immuni.2004.07.013;
RA Jeon M.-S., Atfield A., Venuprasad K., Krawczyk C., Sarao R., Elly C.,
RA Yang C., Arya S., Bachmaier K., Su L., Bouchard D., Jones R., Gronski M.,
RA Ohashi P., Wada T., Bloom D., Fathman C.G., Liu Y.-C., Penninger J.M.;
RT "Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy
RT induction.";
RL Immunity 21:167-177(2004).
RN [12]
RP INTERACTION WITH FGFR2, AND PHOSPHORYLATION.
RX PubMed=15629145; DOI=10.1016/j.bbrc.2004.12.031;
RA Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R.;
RT "Tyrosine 769 of the keratinocyte growth factor receptor is required for
RT receptor signaling but not endocytosis.";
RL Biochem. Biophys. Res. Commun. 327:523-532(2005).
RN [13]
RP INTERACTION WITH INPP5D.
RX PubMed=16000869; DOI=10.1038/emm.2005.22;
RA Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G.;
RT "Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1 and
RT modulates EGF-induced PLC activity.";
RL Exp. Mol. Med. 37:161-168(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [15]
RP INTERACTION WITH PDGFRB.
RX PubMed=17620338; DOI=10.1074/jbc.m701797200;
RA Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J.,
RA Naramura M., Band V., Band H.;
RT "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived
RT growth factor receptor beta provides a dual mechanism of negative
RT regulation.";
RL J. Biol. Chem. 282:29336-29347(2007).
RN [16]
RP INTERACTION WITH PIP5K1C.
RX PubMed=17635937; DOI=10.1083/jcb.200701078;
RA Sun Y., Ling K., Wagoner M.P., Anderson R.A.;
RT "Type I gamma phosphatidylinositol phosphate kinase is required for EGF-
RT stimulated directional cell migration.";
RL J. Cell Biol. 178:297-308(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-506 AND TYR-977, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [19]
RP INTERACTION WITH THEMIS.
RX PubMed=19597499; DOI=10.1038/ni.1766;
RA Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C.,
RA Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J.,
RA Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J.;
RT "Themis controls thymocyte selection through regulation of T cell antigen
RT receptor-mediated signaling.";
RL Nat. Immunol. 10:848-856(2009).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [21]
RP INTERACTION WITH GRB2; LAT AND THEMIS.
RC TISSUE=Thymocyte;
RX PubMed=22561606; DOI=10.1038/ni.2301;
RA Wang D., Zheng M., Lei L., Ji J., Yao Y., Qiu Y., Ma L., Lou J., Ouyang C.,
RA Zhang X., He Y., Chi J., Wang L., Kuang Y., Wang J., Cao X., Lu L.;
RT "Tespa1 is involved in late thymocyte development through the regulation of
RT TCR-mediated signaling.";
RL Nat. Immunol. 13:560-568(2012).
RN [22]
RP PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
RX PubMed=21262971; DOI=10.1074/jbc.m110.205021;
RA Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
RA Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
RA Muller J.P.;
RT "Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3
RT signaling.";
RL J. Biol. Chem. 286:10918-10929(2011).
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an
CC important role in the regulation of intracellular signaling cascades.
CC Becomes activated in response to ligand-mediated activation of
CC receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, EGFR, FGFR1,
CC FGFR2, FGFR3 and FGFR4 (By similarity). Plays a role in actin
CC reorganization and cell migration (By similarity).
CC {ECO:0000250|UniProtKB:P10686, ECO:0000250|UniProtKB:P19174,
CC ECO:0000269|PubMed:15308098}.
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:P10686};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000250|UniProtKB:P10686};
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:P10686};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000250|UniProtKB:P10686};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P10686};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on tyrosine residues.
CC {ECO:0000250|UniProtKB:P19174}.
CC -!- SUBUNIT: Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4
CC (phosphorylated). Interacts with RALGPS1. Interacts (via SH2 domains)
CC with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation
CC sites). Interacts (via SH2 domain) with RET (By similarity). Interacts
CC with AGAP2 via its SH3 domain. Interacts with LAT (phosphorylated) upon
CC TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of
CC TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen
CC receptor-dependent fashion. Interacts with CBLB in activated T-cells;
CC which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3
CC domain) with the Arg/Gly-rich-flanked Pro-rich domains of
CC KHDRBS1/SAM68. This interaction is selectively regulated by arginine
CC methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and
CC CLNK. Interacts with FLT4 and KIT. Interacts with AXL (By similarity).
CC Interacts with SYK; activates PLCG1 (By similarity). Interacts with
CC FLT1 (tyrosine-phosphorylated). Interacts (via SH2 domain) with PDGFRA
CC and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C. Interacts
CC with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts
CC with TESPA1 (By similarity). Interacts with GRB2, LAT and THEMIS upon
CC TCR activation in thymocytes; the association is weaker in the absence
CC of TESPA1. {ECO:0000250|UniProtKB:P19174, ECO:0000269|PubMed:10646608,
CC ECO:0000269|PubMed:10748127, ECO:0000269|PubMed:11463797,
CC ECO:0000269|PubMed:12367511, ECO:0000269|PubMed:15629145,
CC ECO:0000269|PubMed:16000869, ECO:0000269|PubMed:1646396,
CC ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:17620338,
CC ECO:0000269|PubMed:17635937, ECO:0000269|PubMed:19597499,
CC ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:8943348,
CC ECO:0000269|PubMed:9299537}.
CC -!- INTERACTION:
CC Q62077; P14753: Epor; NbExp=4; IntAct=EBI-300133, EBI-617901;
CC Q62077; Q60631: Grb2; NbExp=2; IntAct=EBI-300133, EBI-1688;
CC Q62077; O54957: Lat; NbExp=5; IntAct=EBI-300133, EBI-6390034;
CC Q62077; P48356: Lepr; NbExp=2; IntAct=EBI-300133, EBI-2257257;
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P19174}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P19174}. Note=Rapidly redistributed to ruffles
CC and lamellipodia structures in response to epidermal growth factor
CC (EGF) treatment. {ECO:0000250|UniProtKB:P19174}.
CC -!- DOMAIN: The SH3 domain mediates interaction with RALGPS1 (By
CC similarity). The SH3 domain also mediates interaction with CLNK.
CC {ECO:0000250|UniProtKB:P19174, ECO:0000269|PubMed:11463797}.
CC -!- PTM: Tyrosine phosphorylated in response to signaling via activated
CC FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by
CC activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by
CC activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB.
CC The receptor-mediated activation of PLCG1 involves its phosphorylation
CC by tyrosine kinases in response to ligation of a variety of growth
CC factor receptors and immune system receptors. For instance, SYK
CC phosphorylates and activates PLCG1 in response to ligation of the B-
CC cell receptor. Phosphorylated by ITK and TXK on Tyr-783 upon TCR
CC activation in T-cells. May be dephosphorylated by PTPRJ (By
CC similarity). {ECO:0000250|UniProtKB:P19174}.
CC -!- PTM: Ubiquitinated by CBLB in activated T-cells.
CC {ECO:0000269|PubMed:15308098}.
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DR EMBL; BC065091; AAH65091.1; -; mRNA.
DR EMBL; X95346; CAA64639.1; -; mRNA.
DR CCDS; CCDS16996.1; -.
DR RefSeq; NP_067255.2; NM_021280.3.
DR AlphaFoldDB; Q62077; -.
DR SMR; Q62077; -.
DR BioGRID; 202238; 41.
DR CORUM; Q62077; -.
DR DIP; DIP-29284N; -.
DR IntAct; Q62077; 22.
DR MINT; Q62077; -.
DR STRING; 10090.ENSMUSP00000099404; -.
DR iPTMnet; Q62077; -.
DR PhosphoSitePlus; Q62077; -.
DR EPD; Q62077; -.
DR jPOST; Q62077; -.
DR MaxQB; Q62077; -.
DR PaxDb; Q62077; -.
DR PRIDE; Q62077; -.
DR ProteomicsDB; 289615; -.
DR ABCD; Q62077; 1 sequenced antibody.
DR Antibodypedia; 3796; 1181 antibodies from 42 providers.
DR DNASU; 18803; -.
DR Ensembl; ENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933.
DR GeneID; 18803; -.
DR KEGG; mmu:18803; -.
DR UCSC; uc008nra.1; mouse.
DR CTD; 5335; -.
DR MGI; MGI:97615; Plcg1.
DR VEuPathDB; HostDB:ENSMUSG00000016933; -.
DR eggNOG; KOG1264; Eukaryota.
DR GeneTree; ENSGT00940000158901; -.
DR InParanoid; Q62077; -.
DR OMA; FNPVPFW; -.
DR OrthoDB; 368239at2759; -.
DR PhylomeDB; Q62077; -.
DR TreeFam; TF313216; -.
DR BRENDA; 3.1.4.11; 3474.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-201556; Signaling by ALK.
DR Reactome; R-MMU-202433; Generation of second messenger molecules.
DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-MMU-210990; PECAM1 interactions.
DR Reactome; R-MMU-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-MMU-2424491; DAP12 signaling.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-MMU-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-MMU-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-MMU-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-MMU-5654228; Phospholipase C-mediated cascade, FGFR4.
DR Reactome; R-MMU-8853659; RET signaling.
DR Reactome; R-MMU-9026527; Activated NTRK2 signals through PLCG1.
DR Reactome; R-MMU-9034793; Activated NTRK3 signals through PLCG1.
DR BioGRID-ORCS; 18803; 2 hits in 62 CRISPR screens.
DR ChiTaRS; Plcg1; mouse.
DR PRO; PR:Q62077; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q62077; protein.
DR Bgee; ENSMUSG00000016933; Expressed in floor plate of midbrain and 224 other tissues.
DR ExpressionAtlas; Q62077; baseline and differential.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050429; F:calcium-dependent phospholipase C activity; ISS:UniProtKB.
DR GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; EXP:Reactome.
DR GO; GO:0004629; F:phospholipase C activity; IMP:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; ISO:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:MGI.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:0009306; P:protein secretion; ISO:MGI.
DR GO; GO:1901339; P:regulation of store-operated calcium channel activity; ISO:MGI.
DR GO; GO:1904643; P:response to curcumin; ISO:MGI.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR CDD; cd09932; SH2_C-SH2_PLC_gamma_like; 1.
DR CDD; cd10341; SH2_N-SH2_PLC_gamma_like; 1.
DR CDD; cd11970; SH3_PLCgamma1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.20.20.190; -; 2.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016279; PLC-gamma.
DR InterPro; IPR028380; PLC-gamma1.
DR InterPro; IPR035023; PLC-gamma_C-SH2.
DR InterPro; IPR035024; PLC-gamma_N-SH2.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR035724; PLCgamma1_SH3.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10336; PTHR10336; 1.
DR PANTHER; PTHR10336:SF173; PTHR10336:SF173; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PIRSF; PIRSF000952; PLC-gamma; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 3.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cell projection; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; SH2 domain; SH3 domain; Transducer; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT CHAIN 2..1302
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase gamma-1"
FT /id="PRO_0000088499"
FT DOMAIN 27..142
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 152..187
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 320..464
FT /note="PI-PLC X-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT DOMAIN 489..523
FT /note="PH 2; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 550..657
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 668..756
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 791..851
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 895..931
FT /note="PH 2; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 953..1070
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271"
FT DOMAIN 1071..1194
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 522..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT ACT_SITE 380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT MOD_RES 506
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 771
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:17947660"
FT MOD_RES 775
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 783
FT /note="Phosphotyrosine; by ITK, SYK and TXK"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT MOD_RES 977
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT MOD_RES 1227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT MOD_RES 1233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT MOD_RES 1248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT MOD_RES 1253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08487"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT CONFLICT 966
FT /note="D -> A (in Ref. 2; CAA64639)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="P -> R (in Ref. 2; CAA64639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1302 AA; 149668 MW; 5D123C508D425EB2 CRC64;
MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI
TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL
SLQATSEDEV NMWIKGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM
LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT
GERPEHCQVS LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG
CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA
QQRNMAQHFR KVLGDTLLTK PVDIAADGLP SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM
YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS
STELHSSEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT
NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE
GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP
GFYVEANPMP TFKCAVKALF DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW
FPSNYVEEMI NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA LELSELVVYC
RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS
SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFMAGGHC GYVLQPSTMR DEAFDPFDKS
SLRGLEPCVI CIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW
PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE ARYQQPFEDF
RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC SL
