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 24-JAN-2024, entry version 211. 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, RC Pancreas, 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). Guanine nucleotide CC exchange factor that binds the GTPase DNM1 and catalyzes the CC dissociation of GDP, allowing a GTP molecule to bind in its place, CC therefore enhancing DNM1-dependent endocytosis (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. Interacts (via C-terminal proline-rich domain (PRD)) with CC PLCG1 (via SH3 domain); this interaction leads to guanine nucleotide CC exchange from PlCG1 to DNM1 and enhances DNM1-dependent endocytosis (By CC similarity). {ECO:0000250|UniProtKB:P10686, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; Q62077; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q62077; -. DR PhosphoSitePlus; Q62077; -. DR SwissPalm; Q62077; -. DR EPD; Q62077; -. DR jPOST; Q62077; -. DR MaxQB; Q62077; -. DR PaxDb; 10090-ENSMUSP00000099404; -. DR ProteomicsDB; 289615; -. DR Pumba; Q62077; -. DR ABCD; Q62077; 1 sequenced antibody. DR Antibodypedia; 3796; 1319 antibodies from 42 providers. DR DNASU; 18803; -. DR Ensembl; ENSMUST00000103115.8; ENSMUSP00000099404.2; ENSMUSG00000016933.18. DR GeneID; 18803; -. DR KEGG; mmu:18803; -. DR UCSC; uc008nra.1; mouse. DR AGR; MGI:97615; -. DR CTD; 5335; -. DR MGI; MGI:97615; Plcg1. DR VEuPathDB; HostDB:ENSMUSG00000016933; -. DR eggNOG; KOG1264; Eukaryota. DR GeneTree; ENSGT00940000158901; -. DR InParanoid; Q62077; -. DR OMA; YMRNPLY; -. DR OrthoDB; 2900494at2759; -. 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 65 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 227 other cell types or 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; IDA:SynGO. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. 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; IDA: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:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB. 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; IDA:SynGO. DR GO; GO:0031161; P:phosphatidylinositol catabolic process; ISO:MGI. DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central. 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:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central. 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; cd00275; C2_PLC_like; 1. DR CDD; cd13362; PH_PLC_gamma; 1. DR CDD; cd13234; PHsplit_PLC_gamma; 1. DR CDD; cd08592; PI-PLCc_gamma; 1. 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; 2.60.40.150; C2 domain; 1. DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 2. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 3.30.505.10; SH2 domain; 2. DR Gene3D; 2.30.30.40; SH3 Domains; 1. 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; 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:SF173; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-1; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1. DR Pfam; PF00168; C2; 1. DR Pfam; PF00169; PH; 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; 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 SUPFAM; SSF55550; SH2 domain; 2. DR SUPFAM; SSF50044; SH3-domain; 1. 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 //