PLCG2_MOUSE
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 03-AUG-2022, entry version 168.
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 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 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 [7]
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: Interacts (via SH2 domain) with CSF1R (tyrosine
CC phosphorylated). Interacts constitutively with THEMIS2
CC (PubMed:27992403). {ECO:0000269|PubMed:27992403,
CC 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 -!- 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}.
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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; Q8CIH5; -.
DR PeptideAtlas; Q8CIH5; -.
DR PRIDE; Q8CIH5; -.
DR ProteomicsDB; 289530; -.
DR Antibodypedia; 3797; 1047 antibodies from 43 providers.
DR DNASU; 234779; -.
DR Ensembl; ENSMUST00000081232; ENSMUSP00000079991; ENSMUSG00000034330.
DR GeneID; 234779; -.
DR KEGG; mmu:234779; -.
DR UCSC; uc009npc.1; mouse.
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; QQRYMAR; -.
DR OrthoDB; 368239at2759; -.
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 64 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 219 other tissues.
DR Genevisible; Q8CIH5; MM.
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:0016020; C:membrane; ISO:MGI.
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: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:0032237; P:activation of store-operated calcium channel activity; IMP: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: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:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP:ARUK-UCL.
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; 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; 2.30.29.30; -; 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; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR016279; PLC-gamma.
DR InterPro; IPR028381; PLC-gamma2.
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; PTHR10336; 1.
DR PANTHER; PTHR10336:SF25; PTHR10336:SF25; 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; 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Hydrolase; Lipid degradation; Lipid metabolism;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain;
KW 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
