ID A0A3B4D1F4_PYGNA Unreviewed; 1308 AA.
AC A0A3B4D1F4;
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 Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000017405.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000017405.1}
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};
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 RefSeq; XP_017553714.1; XM_017698225.1.
DR STRING; 42514.ENSPNAP00000017405; -.
DR Ensembl; ENSPNAT00000026175.1; ENSPNAP00000017405.1; ENSPNAG00000023788.1.
DR GeneID; 108427761; -.
DR CTD; 5335; -.
DR GeneTree; ENSGT00940000158901; -.
DR OMA; YMRNPLY; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000261440; 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; cd16214; EFh_PI-PLCgamma1; 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; 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; 3.
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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
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 545..652
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 663..751
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 786..846
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 866..926
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 948..1065
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 1066..1189
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1289..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1308 AA; 150323 MW; 04DAE7925C595C75 CRC64;
MAMAAAFFSN GPVACTPSDT ELNSIYRDLE LGTVLTLFYS KKSQRPERRT FQVKLETRQI
IWTRGTDKIE GEIDIREIKE IRSGQKSRDF ERYVEDSAAK PDQAHCFVIL YGTEFRLKSL
SLAATSDEEM TMWVKGLTWL VTDTLRSPTP LQIERWLRKQ FYAVDRSRED KISCKDLKNM
LCQVNYRVPN MKFLREKLPD GELRSGDVSY CQFAQLYRSL MFDAQKSMDI PFLLRFTERP
EQRISLEDFQ SFLIEYQKEL WATDKNKVQE FMFHYLKDPL REIEQPYYLQ DEFLTYLFSK
ENSIWDATLD HVRPEDMNNP LSHYWISSSH NTYLTGDQFS SESSLEAYAR CLRMGCRCIE
LDCWDGPDGM PVIYHGHTLT TKIKFCDVLM TIKEHAFVTS DYPIILSIED HCSIVQQRNM
ASFFKKVFGE MLLTKAVDIS ADGLPSPNQL KRKILIKHKK LAEGSAYEEV STSTPYSEND
ISNSIKNGIL FLEDPINHEW YPHFFVLTSS KIYYSEETTS NQGNEDEEEH REVGNGMDQH
VSEKWFHGKL GAGRDGRQIA ERLLSEYCLE TGAPDGSFLV RESETFVGDY TLSFWRSGRV
QHCRIHSRQE AGSPKFYLTD NLVFDTLFAL ITHYQQVALR CNEFEMKLTE PVPQTNAHES
KEWYHACLSR SQAENMLMRV PRDGAFLVRK RAEFNSFAIS FRAEGKIKHC RVLQEGQTVV
LGTSEFDSLV DLISYYEKHP LYRKMKLRYP INEETLEKIG TAEPDYGSLY EGRNPGFYVE
ANQMPTFKCT VRAMYEYKAQ RDDELSFSKN TIIQNVDKQE GGWWKGDYGG KKQLWFPANY
VEEISPTAVE PDRSATENSP LGDLLRGSVD VSSCQIVVRP DGKGSRPHVF SLLPMGSPRT
GPVLDVASSS QDELKDWVQK IREVAMTSEA KLEEGKMMER RKKIALELSD LVIYCRPVPF
DEDKIGTERA CFRDMSSFPE TKAEKYVNRI KGKKFLQYNR LQLSRIYPRG QRLDSSNYDP
LPMWLCGSQL VALNFQTADK PMQMNQALFM LNGRSGYVLQ PPIMRDDNFD PFDRHSLRGV
EPVTLIIEVL GARHLPKHGR GIVCPLIEIE VCGAEYDSAK QKTDSEADNG LNPIWPRKPF
RFTVGNPSFA FLRFVVYEID MFNDQNFLAQ ATFPINCLKP GYRSVPLKNS YSEDLELASL
LVHLDIIRGR HENGEMLSPF LGAGAVGVSV GRDRLVDTGS ISSVSSMSPL PSSPGQALGY
RGREGSFEAR YQSPLDDFRV SQESLLDHVD PQNRRLMRRP RVSADNRV
//
