ID PLCG2_MOUSE Reviewed; 1265 AA. AC Q8CIH5; Q3UBA8; Q3UQT0; Q8VE69; DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 176. DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2 {ECO:0000305}; DE EC=3.1.4.11 {ECO:0000250|UniProtKB:P16885}; DE AltName: Full=Phosphoinositide phospholipase C-gamma-2; DE AltName: Full=Phospholipase C-gamma-2; DE Short=PLC-gamma-2; GN Name=Plcg2 {ECO:0000312|MGI:MGI:97616}; 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=Bone marrow macrophage, and Embryonic heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; 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 [3] RP PHOSPHORYLATION, AND INTERACTION WITH CSF1R. RX PubMed=9312046; DOI=10.1093/emboj/16.19.5880; RA Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.; RT "Sequential activation of phoshatidylinositol 3-kinase and phospholipase C- RT gamma2 by the M-CSF receptor is necessary for differentiation signaling."; RL EMBO J. 16:5880-5893(1997). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-753; TYR-1217 AND TYR-1245, RP AND 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 [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and RC Spleen; 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 [6] RP IDENTIFICATION IN A COMPLEX WITH EEIG1; TNFRSF11A; GAB2; TEC AND BTK, AND RP SUBCELLULAR LOCATION. RX PubMed=23478294; DOI=10.1038/cr.2013.33; RA Choi H.K., Kang H.R., Jung E., Kim T.E., Lin J.J., Lee S.Y.; RT "Early estrogen-induced gene 1, a novel RANK signaling component, is RT essential for osteoclastogenesis."; RL Cell Res. 23:524-536(2013). RN [7] RP INTERACTION WITH THEMIS2. RX PubMed=27992403; DOI=10.1038/ni.3642; RA Cheng D., Deobagkar-Lele M., Zvezdova E., Choi S., Uehara S., Baup D., RA Bennett S.C., Bull K.R., Crockford T.L., Ferry H., Warzecha C., RA Marcellin M., de Peredo A.G., Lesourne R., Anzilotti C., Love P.E., RA Cornall R.J.; RT "Themis2 lowers the threshold for B cell activation during positive RT selection."; RL Nat. Immunol. 18:205-213(2017). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 516-640. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of the N-terminal SH2 domain of mouse phospholipase c- RT gamma 2."; RL Submitted (SEP-2007) to the PDB data bank. CC -!- FUNCTION: The production of the second messenger molecules CC diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated CC by activated phosphatidylinositol-specific phospholipase C enzymes. It CC is a crucial enzyme in transmembrane signaling. CC {ECO:0000250|UniProtKB:P16885}. 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:P16885}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180; CC Evidence={ECO:0000250|UniProtKB:P16885}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC -!- SUBUNIT: Part of a complex composed of EEIG1, TNFRSF11A/RANK, PLCG2, CC GAB2, TEC and BTK; complex formation increases in the presence of CC TNFSF11/RANKL (PubMed:23478294). Interacts (via SH2 domain) with CSF1R CC (tyrosine phosphorylated). Interacts constitutively with THEMIS2 CC (PubMed:27992403). {ECO:0000269|PubMed:23478294, CC ECO:0000269|PubMed:27992403, ECO:0000269|PubMed:9312046}. CC -!- INTERACTION: CC Q8CIH5; P14753: Epor; NbExp=2; IntAct=EBI-617954, EBI-617901; CC Q8CIH5; O70433: Fhl2; NbExp=3; IntAct=EBI-617954, EBI-299379; CC Q8CIH5; Q8BTM8: Flna; NbExp=3; IntAct=EBI-617954, EBI-641991; CC Q8CIH5; P11276: Fn1; NbExp=6; IntAct=EBI-617954, EBI-641955; CC Q8CIH5; Q9ES52: Inpp5d; NbExp=3; IntAct=EBI-617954, EBI-300210; CC Q8CIH5; P25911: Lyn; NbExp=2; IntAct=EBI-617954, EBI-643537; CC Q8CIH5; Q9WU78: Pdcd6ip; NbExp=7; IntAct=EBI-617954, EBI-641897; CC Q8CIH5; Q62158: Trim27; NbExp=4; IntAct=EBI-617954, EBI-642025; CC Q8CIH5; Q64321: Zbtb7b; NbExp=3; IntAct=EBI-617954, EBI-642868; CC -!- SUBCELLULAR LOCATION: Membrane raft {ECO:0000269|PubMed:23478294}. CC -!- PTM: Phosphorylated on tyrosine residues by BTK and SYK; upon ligand- CC induced activation of a variety of growth factor receptors and immune CC system receptors. Phosphorylation leads to increased phospholipase CC activity (By similarity). Phosphorylated on tyrosine residues by CSF1R. CC {ECO:0000250|UniProtKB:P16885, ECO:0000269|PubMed:9312046}. 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; AK142173; BAE24959.1; -; mRNA. DR EMBL; AK151039; BAE30056.1; -; mRNA. DR EMBL; BC019654; AAH19654.1; -; mRNA. DR EMBL; BC023877; AAH23877.1; -; mRNA. DR CCDS; CCDS22700.1; -. DR RefSeq; NP_758489.1; NM_172285.2. DR PDB; 2DX0; X-ray; 2.50 A; A/B=516-640. DR PDB; 2EQI; NMR; -; A=772-827. DR PDBsum; 2DX0; -. DR PDBsum; 2EQI; -. DR AlphaFoldDB; Q8CIH5; -. DR BMRB; Q8CIH5; -. DR SMR; Q8CIH5; -. DR BioGRID; 231578; 10. DR CORUM; Q8CIH5; -. DR DIP; DIP-33368N; -. DR IntAct; Q8CIH5; 33. DR MINT; Q8CIH5; -. DR STRING; 10090.ENSMUSP00000079991; -. DR ChEMBL; CHEMBL3608199; -. DR iPTMnet; Q8CIH5; -. DR PhosphoSitePlus; Q8CIH5; -. DR EPD; Q8CIH5; -. DR MaxQB; Q8CIH5; -. DR PaxDb; 10090-ENSMUSP00000079991; -. DR PeptideAtlas; Q8CIH5; -. DR ProteomicsDB; 289530; -. DR Antibodypedia; 3797; 1157 antibodies from 43 providers. DR DNASU; 234779; -. DR Ensembl; ENSMUST00000081232.9; ENSMUSP00000079991.8; ENSMUSG00000034330.11. DR GeneID; 234779; -. DR KEGG; mmu:234779; -. DR UCSC; uc009npc.1; mouse. DR AGR; MGI:97616; -. DR CTD; 5336; -. DR MGI; MGI:97616; Plcg2. DR VEuPathDB; HostDB:ENSMUSG00000034330; -. DR eggNOG; KOG1264; Eukaryota. DR GeneTree; ENSGT00940000157517; -. DR HOGENOM; CLU_002738_5_1_1; -. DR InParanoid; Q8CIH5; -. DR OMA; EDPPVEF; -. DR OrthoDB; 2900494at2759; -. DR PhylomeDB; Q8CIH5; -. DR TreeFam; TF313216; -. DR BRENDA; 3.1.4.11; 3474. DR Reactome; R-MMU-114604; GPVI-mediated activation cascade. DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-MMU-1855204; Synthesis of IP3 and IP4 in the cytosol. DR Reactome; R-MMU-202433; Generation of second messenger molecules. DR Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis. 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-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-MMU-5621480; Dectin-2 family. DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. DR BioGRID-ORCS; 234779; 2 hits in 67 CRISPR screens. DR ChiTaRS; Plcg2; mouse. DR EvolutionaryTrace; Q8CIH5; -. DR PRO; PR:Q8CIH5; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q8CIH5; Protein. DR Bgee; ENSMUSG00000034330; Expressed in basioccipital bone and 223 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IMP:UniProtKB. DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; ISO:MGI. DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; TAS:Reactome. DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; EXP:Reactome. DR GO; GO:0004629; F:phospholipase C activity; TAS:MGI. DR GO; GO:0140031; F:phosphorylation-dependent protein binding; IPI:UniProtKB. DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI. DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI. DR GO; GO:0061760; P:antifungal innate immune response; IMP:ARUK-UCL. DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB. DR GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI. DR GO; GO:0001775; P:cell activation; IMP:ARUK-UCL. DR GO; GO:0071277; P:cellular response to calcium ion; ISO:MGI. DR GO; GO:1990858; P:cellular response to lectin; IMP:ARUK-UCL. DR GO; GO:0071396; P:cellular response to lipid; ISO:MGI. DR GO; GO:0002316; P:follicular B cell differentiation; IMP:MGI. DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IDA:MGI. DR GO; GO:0035556; P:intracellular signal transduction; IMP:ARUK-UCL. DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISO:MGI. DR GO; GO:0002281; P:macrophage activation involved in immune response; IMP:ARUK-UCL. DR GO; GO:0043069; P:negative regulation of programmed cell death; IMP:MGI. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB. DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central. DR GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro. DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IMP:ARUK-UCL. DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISO:MGI. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI. DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IMP:ARUK-UCL. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:ARUK-UCL. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IBA:GO_Central. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IMP:ARUK-UCL. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:ARUK-UCL. DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:ARUK-UCL. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:ARUK-UCL. DR GO; GO:0032747; P:positive regulation of interleukin-23 production; IMP:ARUK-UCL. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:ARUK-UCL. DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:ARUK-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:ARUK-UCL. DR GO; GO:0150078; P:positive regulation of neuroinflammatory response; ISO:MGI. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:ARUK-UCL. DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; ISO:MGI. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:ARUK-UCL. DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI. DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:ARUK-UCL. DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:CACAO. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL. DR GO; GO:0032481; P:positive regulation of type I interferon production; IMP:CACAO. DR GO; GO:0012501; P:programmed cell death; IMP:MGI. DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IMP:ARUK-UCL. DR GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IMP:ARUK-UCL. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB. DR GO; GO:0033198; P:response to ATP; ISO:MGI. DR GO; GO:0048678; P:response to axon injury; ISO:MGI. DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI. DR GO; GO:0032026; P:response to magnesium ion; ISO:MGI. DR GO; GO:0001878; P:response to yeast; IMP:ARUK-UCL. DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IMP:ARUK-UCL. DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI. DR GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:ARUK-UCL. DR CDD; cd00275; C2_PLC_like; 1. DR CDD; cd16215; EFh_PI-PLCgamma2; 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; cd11969; SH3_PLCgamma2; 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; 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; IPR035723; PLCgamma2_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:SF25; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-2; 1. DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 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 SMART; SM00239; C2; 1. DR SMART; SM00233; PH; 2. 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; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1. DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1. DR PROSITE; PS50001; SH2; 2. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q8CIH5; MM. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Hydrolase; Lipid degradation; Lipid metabolism; KW Membrane; Phosphoprotein; Reference proteome; Repeat; SH2 domain; KW SH3 domain; Transducer. FT CHAIN 1..1265 FT /note="1-phosphatidylinositol 4,5-bisphosphate FT phosphodiesterase gamma-2" FT /id="PRO_0000342364" FT DOMAIN 1..131 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 312..456 FT /note="PI-PLC X-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT DOMAIN 532..635 FT /note="SH2 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 646..735 FT /note="SH2 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 769..829 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 930..1044 FT /note="PI-PLC Y-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00271" FT DOMAIN 1038..1169 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT ACT_SITE 327 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT ACT_SITE 372 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00270" FT MOD_RES 753 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 759 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000250|UniProtKB:P16885" FT MOD_RES 1197 FT /note="Phosphotyrosine; by BTK" FT /evidence="ECO:0000250|UniProtKB:P24135" FT MOD_RES 1217 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 1245 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT CONFLICT 787 FT /note="E -> G (in Ref. 1; BAE24959)" FT /evidence="ECO:0000305" FT HELIX 523..525 FT /evidence="ECO:0007829|PDB:2DX0" FT HELIX 540..551 FT /evidence="ECO:0007829|PDB:2DX0" FT TURN 552..555 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 561..565 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 567..569 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 573..579 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 582..593 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 596..602 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 607..609 FT /evidence="ECO:0007829|PDB:2DX0" FT HELIX 610..616 FT /evidence="ECO:0007829|PDB:2DX0" FT TURN 617..619 FT /evidence="ECO:0007829|PDB:2DX0" FT HELIX 625..627 FT /evidence="ECO:0007829|PDB:2DX0" FT STRAND 773..778 FT /evidence="ECO:0007829|PDB:2EQI" FT STRAND 784..786 FT /evidence="ECO:0007829|PDB:2EQI" FT STRAND 795..798 FT /evidence="ECO:0007829|PDB:2EQI" FT STRAND 803..805 FT /evidence="ECO:0007829|PDB:2EQI" FT STRAND 807..811 FT /evidence="ECO:0007829|PDB:2EQI" FT STRAND 814..819 FT /evidence="ECO:0007829|PDB:2EQI" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:2EQI" FT STRAND 824..826 FT /evidence="ECO:0007829|PDB:2EQI" SQ SEQUENCE 1265 AA; 147592 MW; E4A2A6AD6F05160E CRC64; MTTMVNVDTL PEYEKSQIKR ALELGTVMTV FNARKSTPER RTVQMIMETR QVAWSKTADK IEGFLDIMEI KEIRPGKNSK DFERAKAVRH KAECCFTILY GTQFVLSTLS LATDSKEDAV KWLSGLKILH QEAMSASTPT MIESWLRKQI YSVDQTRRNS ISLRELKTIL PLVNFKVSGI KFLKDKLVEI GAQKDELSFE QFHLFYKKLM FDQQKSILDE FKKDSSVFIL GNTDRPDASA VYLQDFQRFL LHEQQELWAQ DLNKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS IWDEKYDAVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR AGCRCIELDC WDGPDGKPII YHGWTRTTKI KFDDVVQAIR DHAFVTSSFP VILSIEEHCS VEQQRHMAKV FKEVLGDMLL TKPTEASADQ LPSPSQLREK IIIKHKKLGP KGDVDVNVED KKDEHKPQGE LYMWDSIDQK WTRHYCAIAD AKLSFGDDIE QAVEEEPVQD TPPTELHFGE KWFHKKVESR TSAEKLLQEY CAETGAKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMENGVMKYY LTDNLTFNSI YALIQHYREA HLRCAEFELR LTDPVPNPNP HESKPWYYDS LSRGEAEDML MRIPRDGAFL IRKREGTNSY AITFRARGKV KHCRINRDGR HFVLGTSAYF ESLVELVSYY EKHALYRKMR LRYPVTPELL ERYNMERDIN SLYDVSRMYV DPSEINPSMP QRTVKALYDY KAKRSDELTF CRGALIHNVS KEPGGWWKGD YGTRIQQYFP SNYVEDISAG DAEEMEKQII EDNPLGSLCK GILDLNTYNV VKAPQGKNQK AFVFILEPKK QGDPPVEFAT DRVEELFEWF QSIREITWKM DTKENNMKYW ERNQSIAIEL SDLVVYCKPT SKTKDHLENP DFREIRSFVE TKADSIVRQK PVDLLRYNQK GLTRVYPKGQ RVDSSNYDPF RLWLCGSQMV ALNFQTPDKY MQMNHALFSL NGRTGYVLQP ESMRSEKYDP MPLESQRKIL MTLTVKVLGA RHLPKLGRSI ACPFVEVEIC GAEYDSNKFK TTVVNDNGLS PVWAPTQEKV TFEIYDPNLA FLRFVVYEED MFSDPNFLAH ATYPIKGIKS GFRSVPLKNG YSEDIELASL LVFCEMRPVL ESEEELYSSC RQLRRRQEEL NNQLFLYDTH QNLRGANRDA LVKEFNVNEN QLQLYQEKCN RRLREKRVSN SRFYS //