ID A0A3B3ZUN7_9GOBI Unreviewed; 1295 AA.
AC A0A3B3ZUN7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma {ECO:0000256|PIRNR:PIRNR000952};
DE EC=3.1.4.11 {ECO:0000256|PIRNR:PIRNR000952};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000008417.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000008417.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 409849.ENSPMGP00000008417; -.
DR Ensembl; ENSPMGT00000008956.1; ENSPMGP00000008417.1; ENSPMGG00000006960.1.
DR Proteomes; UP000261520; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; cd13362; PH_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; cd11970; SH3_PLCgamma1; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; IPR018247; EF_Hand_1_Ca_BS.
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; 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:SF173; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 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; 2.
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; PS00018; EF_HAND_1; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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 27..142
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 547..654
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 665..753
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 788..848
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 950..1067
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1068..1191
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1226..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 149195 MW; 81E681F74962B1F1 CRC64;
MAGTTGYFSN GPAPWMDSDT EMNNLYRDLE LGTVLTLFYS KKSQRPERRT FQVKLETRTI
IWTRGTDKIE GEIDIREIKE IRPGQKSRDF ERYVEDSAAR LETAHCFVIL YGTEFRLRSL
SLAATSDEEM TMWVKGLNWL VADTLKSPTP LQIERWLRKQ FYAVDRNRED RISCKDLKNM
LSQVNYRVPN MKFLREKLPD SEMRNGDVSF SQFAQLYRSL MFDAQKSMIL SLFVFLRYID
RPEIRISLEE FKNFLLEHQN ELWATDNNKV QDFMFSYLKD PLREVEQPYF CQEEFLTYLF
SKENTIWDSS LDQVCPENMN NPLSHYWISS SHNTYLTGDQ FSSESSLEAY ARCLRMGCRC
IELDCWDGPD GMPVIYHGHT LTTKIKFCDV LNTIKEHAFV TSDYPIILSI EDHCSIVQQR
NMATFFKKVF GEMLLTKAVD IAADGLPSPN QLKRKILIKH KKLAEGSAYE EVSTSTPYSE
NDISNSIKNG ILYLEDPINH EWYPHFFVLT NSKIYYSEET SNNQGNDDEE EHREVSNGVD
QHVTEKWFHG KLGAGRDGRH IAERLLSEYC LETGAPDGSF LVRESETFVG DYTLSFWRSG
RVQHCRIHSR QEAGSPKFYL TDNLVFDTLY ALIGHYQQVA LRCNEFEMKL TEPVPQTNAH
ESKEWYHANL SRSHAENMLM RVPRDGAFLV RKRAEPNSFA ISFRAEGKIK HCRVQQEGQT
VVLGTSEFDS LVDLISYYEK HPLYRKMKLR YPINEDTLEK IGTAEPDYGS LYEGRNPGFY
VEANQMPTFK CTVKAMYEYK AQRDDELSFP KNAIINNVDK QEGGWWKGDC GGKKQMWFPA
NYVEEISPTA AEPDREVTEN SPLGDLLRGS VDVSSCHIAI RPEGKGSRPH VFSLAPNPSM
RLGPVLDVAA NSQEELNQWV LKIREVAMTS EAKLEEGKMM ERRKKIALEL SDLVIYCRPV
PFDEDKIGTE RACFRDMSSF PETKAEKYVN KIKGKKFLQY NRLQLSRIYP RGQRLDSSNY
DPLPMWLCGS QLVALNFQTA DKPMQMNQAL FMLNGRCGYV LQPPIMRDDT FDPFDRHTLR
SVEPVSLQIE VLGARHLPKH GRGIVCPLIE IEVCGAEYDS AKQKTDSEAD NGLNPTWPRK
PFQFTVCNSA FAFLRFVVYE IDMFNDQNFL AQATFPIQGL KTGYRSVPLK NSFNEDLELA
SLLVYMEITR GRASRERLGE FGSVSSLSSN MSPLPQSPAQ AQAIGYRGRE GSFESRYQSP
MDDFRLSQQS LLDHMDSQNR SRMLRGARVG GENRV
//
