GenomeNet

Database: UniProt
Entry: F6X0W1_HORSE
LinkDB: F6X0W1_HORSE
Original site: F6X0W1_HORSE 
ID   F6X0W1_HORSE            Unreviewed;      1300 AA.
AC   F6X0W1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE            EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
GN   Name=PLCG2 {ECO:0000313|Ensembl:ENSECAP00000002280.2,
GN   ECO:0000313|VGNC:VGNC:21543};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000002280.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000002280.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002280.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000002280.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000002280.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Mediates the production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an
CC       important role in the regulation of intracellular signaling cascades.
CC       {ECO:0000256|PIRNR:PIRNR000952}.
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:0000256|ARBA:ARBA00023674};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33180;
CC         Evidence={ECO:0000256|ARBA:ARBA00023674};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   Ensembl; ENSECAT00000003199.4; ENSECAP00000002280.2; ENSECAG00000000291.4.
DR   VGNC; VGNC:21543; PLCG2.
DR   GeneTree; ENSGT00940000157517; -.
DR   HOGENOM; CLU_002738_5_1_1; -.
DR   OrthoDB; 2900494at2759; -.
DR   TreeFam; TF313216; -.
DR   Proteomes; UP000002281; Chromosome 3.
DR   Bgee; ENSECAG00000000291; Expressed in articular cartilage of joint and 22 other cell types or tissues.
DR   ExpressionAtlas; F6X0W1; baseline.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0097708; C:intracellular vesicle; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:0140031; F:phosphorylation-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0061760; P:antifungal innate immune response; IEA:Ensembl.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR   GO; GO:0002316; P:follicular B cell differentiation; IEA:Ensembl.
DR   GO; GO:0032959; P:inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; IEA:Ensembl.
DR   GO; GO:1903721; P:positive regulation of I-kappaB phosphorylation; IEA:Ensembl.
DR   GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR   GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR   GO; GO:0032747; P:positive regulation of interleukin-23 production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0150078; P:positive regulation of neuroinflammatory response; IEA:Ensembl.
DR   GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IEA:Ensembl.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
DR   GO; GO:0012501; P:programmed cell death; IEA:Ensembl.
DR   GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR   GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR   GO; GO:0001878; P:response to yeast; IEA:Ensembl.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; IEA:Ensembl.
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   PRINTS; PR00452; SH3DOMAIN.
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.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000952, ECO:0000256|RuleBase:RU361133};
KW   Lipid degradation {ECO:0000256|PIRNR:PIRNR000952,
KW   ECO:0000256|RuleBase:RU361133};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR000952};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PIRNR:PIRNR000952}.
FT   DOMAIN          55..166
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          567..670
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          681..770
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          804..864
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          965..1079
FT                   /note="PI-PLC Y-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50008"
FT   DOMAIN          1073..1204
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
SQ   SEQUENCE   1300 AA;  151881 MW;  A1D57FC502F81938 CRC64;
     MNQIQQVLNW RGPVNSKFSR PPCSLTASFS LEWPTMNTMV NVNALPEYEK SQIKRALELG
     TVMTVFSFRK STPERRTVQV IMETRQVAWS KTADKIEGFL DIMEIKEIRP GKSSKDFERA
     KAVRQKEDCC FTILYGTQFV LSTLSLAADS REDATKWLSG LKILHQEAMS ASTPTIIESW
     LRKQIYSVDQ TRRNSISLRE LKTILPLVNF KVSSAKFLKD KFVEIGAHKD ELSFEQFHLF
     YKKLMFEQQK SILDEFKKDS SVFILGNTDR PDASAVHLHD FQRFLLHEQQ EHWAQDLNRV
     RERMTKFIDD TMRETAEPFL FVDEFLTYLF SRENSIWDEK YDVVDMQDMN NPLSHYWISS
     SHNTYLTGDQ LRSESSTEAY IRCLRMGCRC IELDCWDGPD GKPIIYHGWT RTTKIKFDDV
     VQAIKDHAFV TSSFPVILSI EEHCGVEQQR HMARVFKEVF GDQLLMKPTE ASADQLPSPS
     QLREKIIIKH KKLGPRGDVD VNMEDKKDEH KQQGELYMWD SIDQKWTRHY CAIADAKLSF
     SDDIEQTGEE EPPQDTPPTE LHFGEKWFHK KVEKRTSAEK LLQEYCAETG GKDGTFLVRE
     SETFPNDYTL SFWRSGRVQH CRIRSTMEGG TMKYYLTDNL MFTSIYALIQ HYRETHLRCA
     EFELRLTEPV PNPNPHEAKP WYYDGLSRGE AEDMLMRVPR DGAFLIRKRE GTDSYAITFR
     ARGKVKHCRI NKDGRHFVLG TSAYFESLVE LVSYYEKHAL YRKMRLRYPV TPELLERYNM
     ERDINSLYDV SRMYVDPSEI NPSMPQRTVK ALYDYKAKRS DELSFCRGAL IHNVSKEPGG
     WWKGDYGTRI QQYFPSNYVE DISTADVEEL EKQIIEDNPL GSLCRGILDL NTYNVVKAPQ
     GKNQKPFVFI LEPKKQGDPP VEFATDRVEE LFEWFQSIRE ITWKIDTKEN NMKYWEKNQS
     IAIELSDLVV YCKPTSKTKD NLENPDFREI RSFVETKADS VVRQKPIDLL KYNQKGLTRI
     YPKGQRVDSS NYDPFRFWLC GSQMAALNFQ TADKYMQMNH ALFSLNGRTG YVLQPESMRT
     EKYDPMPPES QRKILMTLTV KVLGARHLPK LGRSIACPFV EVEICGAEYD NNKFKTTVVN
     DNGLSPVWAP TQEKVTFEIY DPNLAFLRFV VYEEDMFSDP NFLAHATYPI KGIKSGFRSV
     PLKNGYSEDI ELASLLVFCE MRPVLESEEE LYSSCRQLRR RQEELNNQLF LYDTHQNLRN
     ANRDALVKEF NVNENQLQLY QEKCNRRLRE KRVSNSKFYS
//
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