PLCG1_RAT
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 03-AUG-2022, entry version 224.
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 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 [7]
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). {ECO:0000250|UniProtKB:P19174,
CC ECO:0000250|UniProtKB:Q62077, 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). {ECO:0000250|UniProtKB:P19174,
CC ECO:0000250|UniProtKB:Q62077}.
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}.
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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 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 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.ENSRNOP00000022276; -.
DR BindingDB; P10686; -.
DR ChEMBL; CHEMBL5188; -.
DR SwissLipids; SLP:000000960; -.
DR iPTMnet; P10686; -.
DR PhosphoSitePlus; P10686; -.
DR PaxDb; P10686; -.
DR PRIDE; P10686; -.
DR GeneID; 25738; -.
DR KEGG; rno:25738; -.
DR UCSC; RGD:3347; rat.
DR CTD; 5335; -.
DR RGD; 3347; Plcg1.
DR eggNOG; KOG1264; Eukaryota.
DR InParanoid; P10686; -.
DR OrthoDB; 368239at2759; -.
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:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
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: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: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:0009306; P:protein secretion; IMP:RGD.
DR GO; GO:1901339; P:regulation of store-operated calcium channel activity; IMP:RGD.
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:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; TAS:RGD.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISO:RGD.
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; 2.30.29.30; -; 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 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 STRAND 551..553
FT /evidence="ECO:0007829|PDB:3GQI"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:3GQI"
FT HELIX 561..576
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 583..587
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 594..600
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 605..613
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:3GQI"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:3GQI"
FT HELIX 632..641
FT /evidence="ECO:0007829|PDB:3GQI"
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 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 STRAND 860..862
FT /evidence="ECO:0007829|PDB:2FJL"
FT TURN 864..870
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 874..876
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 882..886
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 890..892
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 896..900
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 904..906
FT /evidence="ECO:0007829|PDB:2FJL"
FT STRAND 909..912
FT /evidence="ECO:0007829|PDB:2FJL"
FT HELIX 916..930
FT /evidence="ECO:0007829|PDB:2FJL"
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
