ID PLCG1_RAT Reviewed; 1290 AA.
AC P10686;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 27-MAR-2024, entry version 233.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 {ECO:0000305};
DE EC=3.1.4.11 {ECO:0000269|PubMed:7531435};
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|RGD:3347};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2840660; DOI=10.1073/pnas.85.15.5419;
RA Suh P.-G., Ryu S.H., Moon K.H., Suh H.W., Rhee S.G.;
RT "Inositol phospholipid-specific phospholipase C: complete cDNA and protein
RT sequences and sequence homology to tyrosine kinase-related oncogene
RT products.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5419-5423(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=8392838; DOI=10.1006/bbrc.1993.1818;
RA Lee S.J., Ryu S.H., Suh P.G.;
RT "Promoter region of the rat phospholipase C-gamma 1 gene.";
RL Biochem. Biophys. Res. Commun. 194:294-300(1993).
RN [3]
RP INTERACTION WITH FGFR4, AND PHOSPHORYLATION.
RX PubMed=7518429; DOI=10.1016/s0021-9258(17)32309-8;
RA Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K.;
RT "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4).
RT Comparison with FGFR-1.";
RL J. Biol. Chem. 269:18320-18326(1994).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7531435; DOI=10.1042/bj3050745;
RA Koblan K.S., Schaber M.D., Edwards G., Gibbs J.B., Pompliano D.L.;
RT "src-homology 2 (SH2) domain ligation as an allosteric regulator:
RT modulation of phosphoinositide-specific phospholipase C gamma 1 structure
RT and activity.";
RL Biochem. J. 305:745-751(1995).
RN [5]
RP INTERACTION WITH AGAP2, AND MUTAGENESIS OF PRO-842.
RX PubMed=11823862; DOI=10.1038/415541a;
RA Ye K., Aghdasi B., Luo H.R., Moriarity J.L., Wu F.Y., Hong J.J., Hurt K.J.,
RA Bae S.S., Suh P.-G., Snyder S.H.;
RT "Phospholipase C gamma 1 is a physiological guanine nucleotide exchange
RT factor for the nuclear GTPase PIKE.";
RL Nature 415:541-544(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH DNM1.
RX PubMed=15252117; DOI=10.1242/jcs.01220;
RA Choi J.H., Park J.B., Bae S.S., Yun S., Kim H.S., Hong W.P., Kim I.S.,
RA Kim J.H., Han M.Y., Ryu S.H., Patterson R.L., Snyder S.H., Suh P.G.;
RT "Phospholipase C-gamma1 is a guanine nucleotide exchange factor for
RT dynamin-1 and enhances dynamin-1-dependent epidermal growth factor receptor
RT endocytosis.";
RL J. Cell Sci. 117:3785-3795(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221 AND SER-1248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP STRUCTURE BY NMR OF 489-553 AND 663-759.
RX PubMed=16500902; DOI=10.1074/jbc.m600336200;
RA Wen W., Yan J., Zhang M.;
RT "Structural characterization of the split pleckstrin homology domain in
RT phospholipase C-gamma1 and its interaction with TRPC3.";
RL J. Biol. Chem. 281:12060-12068(2006).
CC -!- FUNCTION: Mediates the production of the second messenger molecules
CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3)
CC (PubMed:7531435). Plays an important role in the regulation of
CC intracellular signaling cascades. Becomes activated in response to
CC ligand-mediated activation of receptor-type tyrosine kinases, such as
CC PDGFRA, PDGFRB, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:7531435).
CC Plays a role in actin reorganization and cell migration (By
CC similarity). Guanine nucleotide exchange factor that binds the GTPase
CC DNM1 and catalyzes the dissociation of GDP, allowing a GTP molecule to
CC bind in its place, therefore enhancing DNM1-dependent endocytosis
CC (PubMed:15252117). {ECO:0000250|UniProtKB:P19174,
CC ECO:0000250|UniProtKB:Q62077, ECO:0000269|PubMed:15252117,
CC ECO:0000269|PubMed:7531435}.
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:7531435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC Evidence={ECO:0000305|PubMed:7531435};
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:0000269|PubMed:7531435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43485;
CC Evidence={ECO:0000305|PubMed:7531435};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:7531435};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on tyrosine residues.
CC {ECO:0000250|UniProtKB:P19174}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=13.8 umol/min/mg enzyme toward phosphatidylinositol
CC {ECO:0000269|PubMed:7531435};
CC Vmax=0.6 umol/min/mg enzyme toward 1,2-diacyl-sn-glycero-3-phospho-
CC (1D-myo-inositol-4,5-bisphosphate) {ECO:0000269|PubMed:7531435};
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:7531435};
CC -!- SUBUNIT: Interacts with AGAP2 via its SH3 domain. Interacts (via SH2
CC domain) with RET. Interacts with FLT1 (tyrosine-phosphorylated) (By
CC similarity). Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and
CC FGFR4 (phosphorylated). Interacts with LAT (phosphorylated) upon TCR
CC 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 (By similarity). Interacts with AXL, FLT4 and KIT. Interacts with
CC RALGPS1. Interacts (via the SH2 domains) with VIL1 (phosphorylated at
CC C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain)
CC with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with
CC PIP5K1C (By similarity). Interacts with NTRK1 and NTRK2 (phosphorylated
CC upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts
CC with GRB2, LAT and THEMIS upon TCR activation in thymocytes (By
CC similarity). Interacts with TESPA1; the association is increased with
CC prolonged stimulation of the TCR and may facilitate the assembly of the
CC LAT signalosome (By similarity). Interacts (via C-terminal proline-rich
CC domain (PRD)) with PLCG1 (via SH3 domain); this interaction leads to
CC guanine nucleotide exchange from PlCG1 to DNM1 and enhances DNM1-
CC dependent endocytosis (PubMed:15252117). {ECO:0000250|UniProtKB:P19174,
CC ECO:0000250|UniProtKB:Q62077, ECO:0000269|PubMed:15252117}.
CC -!- INTERACTION:
CC P10686; Q04589: Fgfr1; NbExp=2; IntAct=EBI-520788, EBI-2480918;
CC P10686; P11362: FGFR1; Xeno; NbExp=4; IntAct=EBI-520788, EBI-1028277;
CC P10686; Q08881: ITK; Xeno; NbExp=2; IntAct=EBI-520788, EBI-968552;
CC P10686; Q62120: Jak2; Xeno; NbExp=3; IntAct=EBI-520788, EBI-646604;
CC P10686; Q60749: Khdrbs1; Xeno; NbExp=2; IntAct=EBI-520788, EBI-519077;
CC P10686; Q9WU01: Khdrbs2; Xeno; NbExp=2; IntAct=EBI-520788, EBI-8339046;
CC P10686; P18031: PTPN1; Xeno; NbExp=4; IntAct=EBI-520788, EBI-968788;
CC P10686; Q13507: TRPC3; Xeno; NbExp=2; IntAct=EBI-520788, EBI-520807;
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 CLNK (By similarity).
CC The SH3 domain also mediates interaction with RALGPS1 (By similarity).
CC {ECO:0000250|UniProtKB:P19174, ECO:0000250|UniProtKB:Q62077}.
CC -!- PTM: Ubiquitinated by CBLB in activated T-cells.
CC {ECO:0000250|UniProtKB:Q62077}.
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. May be dephosphorylated by PTPRJ. Phosphorylated by ITK
CC and TXK on Tyr-783 upon TCR activation in T-cells (By similarity).
CC {ECO:0000250|UniProtKB:P19174, ECO:0000250|UniProtKB:Q62077}.
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; J03806; AAA41921.1; -; mRNA.
DR EMBL; L14476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A31317; A31317.
DR RefSeq; NP_037319.1; NM_013187.1.
DR PDB; 1Y0M; X-ray; 1.20 A; A=791-851.
DR PDB; 1YWO; X-ray; 1.81 A; A=790-851.
DR PDB; 1YWP; X-ray; 1.60 A; A=790-851.
DR PDB; 2FJL; NMR; -; A=489-547, A=851-933.
DR PDB; 3GQI; X-ray; 2.50 A; B=545-770.
DR PDB; 4K44; X-ray; 1.70 A; A/B=664-766.
DR PDB; 4K45; X-ray; 1.50 A; A=664-766, B=770-787.
DR PDB; 5EG3; X-ray; 2.61 A; B=661-773.
DR PDB; 6PBC; X-ray; 2.46 A; A=21-200, A=791-1215.
DR PDB; 7T8T; EM; 3.68 A; A=20-1215.
DR PDB; 7Z3J; X-ray; 2.00 A; A=20-765, A=791-1215.
DR PDBsum; 1Y0M; -.
DR PDBsum; 1YWO; -.
DR PDBsum; 1YWP; -.
DR PDBsum; 2FJL; -.
DR PDBsum; 3GQI; -.
DR PDBsum; 4K44; -.
DR PDBsum; 4K45; -.
DR PDBsum; 5EG3; -.
DR PDBsum; 6PBC; -.
DR PDBsum; 7T8T; -.
DR PDBsum; 7Z3J; -.
DR AlphaFoldDB; P10686; -.
DR SMR; P10686; -.
DR BioGRID; 247766; 5.
DR CORUM; P10686; -.
DR DIP; DIP-2863N; -.
DR IntAct; P10686; 27.
DR MINT; P10686; -.
DR STRING; 10116.ENSRNOP00000069822; -.
DR BindingDB; P10686; -.
DR ChEMBL; CHEMBL5188; -.
DR SwissLipids; SLP:000000960; -.
DR iPTMnet; P10686; -.
DR PhosphoSitePlus; P10686; -.
DR PaxDb; 10116-ENSRNOP00000022276; -.
DR GeneID; 25738; -.
DR KEGG; rno:25738; -.
DR UCSC; RGD:3347; rat.
DR AGR; RGD:3347; -.
DR CTD; 5335; -.
DR RGD; 3347; Plcg1.
DR eggNOG; KOG1264; Eukaryota.
DR InParanoid; P10686; -.
DR OrthoDB; 2900494at2759; -.
DR PhylomeDB; P10686; -.
DR BRENDA; 3.1.4.11; 5301.
DR Reactome; R-RNO-1169408; ISG15 antiviral mechanism.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-201556; Signaling by ALK.
DR Reactome; R-RNO-202433; Generation of second messenger molecules.
DR Reactome; R-RNO-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-RNO-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-RNO-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-RNO-5654228; Phospholipase C-mediated cascade, FGFR4.
DR Reactome; R-RNO-8853659; RET signaling.
DR Reactome; R-RNO-9026527; Activated NTRK2 signals through PLCG1.
DR Reactome; R-RNO-9034793; Activated NTRK3 signals through PLCG1.
DR EvolutionaryTrace; P10686; -.
DR PRO; PR:P10686; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:RGD.
DR GO; GO:0008180; C:COP9 signalosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050429; F:calcium-dependent phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0035254; F:glutamate receptor binding; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; IDA:RGD.
DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; ISO:RGD.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0004629; F:phospholipase C activity; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; IMP:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IMP:RGD.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0031161; P:phosphatidylinositol catabolic process; IDA:RGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR GO; GO:1904643; P:response to curcumin; IDA:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
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 DisProt; DP01851; -.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 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 3D-structure; Acetylation; Calcium; Cell projection; Hydrolase;
KW Lipid degradation; Lipid metabolism; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH2 domain; SH3 domain; Transducer;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P19174"
FT CHAIN 2..1290
FT /note="1-phosphatidylinositol 4,5-bisphosphate
FT phosphodiesterase gamma-1"
FT /id="PRO_0000088500"
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..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1290
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:0000250|UniProtKB:Q62077"
FT MOD_RES 771
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:P08487"
FT MOD_RES 775
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19174"
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:0000250|UniProtKB:Q62077"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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 MUTAGEN 842
FT /note="P->L: Inhibits interaction with AGAP2."
FT /evidence="ECO:0000269|PubMed:11823862"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 129..146
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 224..227
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 270..281
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 285..288
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 350..358
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 490..498
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 514..522
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:3GQI"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:3GQI"
FT HELIX 559..576
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 595..601
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 604..613
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 615..617
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 628..631
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 632..639
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 665..668
FT /evidence="ECO:0007829|PDB:4K45"
FT STRAND 669..672
FT /evidence="ECO:0007829|PDB:4K45"
FT HELIX 675..682
FT /evidence="ECO:0007829|PDB:4K45"
FT STRAND 690..695
FT /evidence="ECO:0007829|PDB:4K45"
FT STRAND 701..708
FT /evidence="ECO:0007829|PDB:4K45"
FT STRAND 711..720
FT /evidence="ECO:0007829|PDB:4K45"
FT STRAND 723..726
FT /evidence="ECO:0007829|PDB:4K45"
FT STRAND 729..733
FT /evidence="ECO:0007829|PDB:4K45"
FT HELIX 734..743
FT /evidence="ECO:0007829|PDB:4K45"
FT HELIX 758..762
FT /evidence="ECO:0007829|PDB:4K45"
FT TURN 763..765
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 796..800
FT /evidence="ECO:0007829|PDB:1Y0M"
FT STRAND 817..822
FT /evidence="ECO:0007829|PDB:1Y0M"
FT STRAND 825..833
FT /evidence="ECO:0007829|PDB:1Y0M"
FT STRAND 836..842
FT /evidence="ECO:0007829|PDB:1Y0M"
FT HELIX 843..845
FT /evidence="ECO:0007829|PDB:1Y0M"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:1Y0M"
FT HELIX 852..854
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6PBC"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 872..877
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 882..886
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 893..900
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 904..906
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 908..912
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 916..931
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 951..954
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 967..969
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 979..984
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 985..989
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 994..996
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 997..1006
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1009..1012
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 1026..1029
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 1030..1032
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1034..1038
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 1045..1053
FT /evidence="ECO:0007829|PDB:7Z3J"
FT TURN 1054..1058
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1061..1064
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 1067..1070
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1071..1073
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 1079..1082
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1088..1099
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1103..1106
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1110..1119
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 1120..1122
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1124..1127
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1132..1137
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1145..1150
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1154..1164
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1170..1179
FT /evidence="ECO:0007829|PDB:7Z3J"
FT HELIX 1180..1182
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1186..1193
FT /evidence="ECO:0007829|PDB:7Z3J"
FT STRAND 1199..1213
FT /evidence="ECO:0007829|PDB:7Z3J"
SQ SEQUENCE 1290 AA; 148548 MW; BB3240C27972CE3B CRC64;
MAGVGTPCAN GCGPSAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI
TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL
SLQATSEDEV NMWIKGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM
LSQVNYRVPN MRFLRERLTD FEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNTLRT
GERPELCQVS LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
FLFSKENSVW NSQLDAVCPE TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG
CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA
QQRNMAQHFR KVLGDTLLTK PVDIAADGLP SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM
YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG
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 NPAILEPERE 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 SPFSGTSLRE RASDASSQLF HVRAREGSFE ARYQQPFEDF
RISQEHLADH FDSRERRAPR RTRVNGDNRL
//
