ID A0A1S2ZB60_ERIEU Unreviewed; 1267 AA.
AC A0A1S2ZB60;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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|RefSeq:XP_007516682.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007516682.1};
RN [1] {ECO:0000313|RefSeq:XP_007516682.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_007516682.1; XM_007516620.2.
DR AlphaFoldDB; A0A1S2ZB60; -.
DR STRING; 9365.ENSEEUP00000008562; -.
DR GeneID; 103107807; -.
DR CTD; 5336; -.
DR eggNOG; KOG1264; Eukaryota.
DR InParanoid; A0A1S2ZB60; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:UniProtKB-UniRule.
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; PF16457; PH_12; 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.
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:UP000079721};
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 1..131
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 532..635
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 646..735
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 769..831
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 932..1046
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1040..1171
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
SQ SEQUENCE 1267 AA; 148139 MW; A8671140B947EF0E CRC64;
MTAMFNVDTL PEYEKSQIKR ALELGTVMTV FSFRKSTPER RTVQVIMETR QVAWSKTADK
IEGFLDIMEI KEIRPGKNSK DFERAKAVRQ KEDCCFTILY GTQFVLSTLS LAADSKDDAN
KWLSGLKILH QEAMSASTPT IIESWLRKQI YSVDQTRRNS ISLRELKTIL PLVNFKVSSA
KFLKDKFVEI GAHKDELSFE QFHLFYKKLM FEQQKLILDE FKKDSSVFIL GNTDRPDASA
VHLHDFQRFL LHEQQEVWAQ DLSKVRERMT KFIDDTMRET AEPFLFVDEF LTYLFSRENS
IWDEKYDVVD MQDMNNPLSH YWISSSHNTY LTGDQLRSES STEAYIRCLR MGCRCIELDC
WDGPDGKPII YHGWTRTTKI KFDDVVQAIK DHAFVTSSFP VILSIEEHCG VEQQRHMARV
FKEVLGDLLL MKPTEASADQ LPSPSQLREK IIIKHKKLGP RGDVDVNMED KKEEHKQQGE
LYMWDSIDQK WTRHYCAIAD AKLSFSDDIE QTVEEELPQD TPPTELHFGE KWFHKKVEKR
TSAEKLLQEY CAETGGKDGT FLVRESETFP NDYTLSFWRS GRVQHCRIRS TMEGGTMKYY
LTDNLMFTSI YDLIQHYREA HLRCAEFELR LTDPVPNPNP HESKPWYYDG LSRGEAEDML
MRVPRDGAFL IRKREGTDSY AITFRAKGKV KHCRINRDNR LFVLGTSAYF ESLVELVSYY
EKHALYRKMK LRYPVTPELL ERYNMERDIN SLYDVSRMYV DPSEINPSMP QRTVKALYDY
TAKRSDELTF CRGALIHNVS RDPSLQGWWK GDYGTRIQQY FPSNYVEDIS TADVEEMEKQ
IIEDNPLGSL CRGILDLNTY NVVKAPQGKN QKPFVFILEP KKQGDPPVEF ATDRVEELFE
WFQSIREITW KIDTKENNMK YWEKNQSIAI ELSDLVVYCK PTSKTKDNLE NPDFREIRSF
VETKADSVTR QKPIDLLKYN QKGLTRVYPK GQRVDSSNYD PFRLWLCGSQ MVALNFQTAD
KYMQMNHALF SLNGRTGYVL QPESMRTEKY DPMPPESQRK ILMTLTVKVL GARHLPKLGR
SIACPFVEVE ICGAEYDNNK FKTTVVNDNG LSPIWASTQE KVTFEIYDPN LAFLRFVVYE
EDMFSDPNFL AHATYPIKGI KSGFRSVPLK NGYSEDIELA SLLVFCEMRP VLESEEELYS
SCRQLRRRQE ELNNQLFLYD THTNLRNANR DALVKEFNVN ENQLQLYQER CNRRLKEKRV
SNSKFYS
//
