ID A0A3Q0RUK3_AMPCI Unreviewed; 1003 AA.
AC A0A3Q0RUK3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000014396.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000014396.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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|RuleBase:RU361133};
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DR AlphaFoldDB; A0A3Q0RUK3; -.
DR STRING; 61819.ENSACIP00000014396; -.
DR Ensembl; ENSACIT00000014780.1; ENSACIP00000014396.1; ENSACIG00000011203.1.
DR GeneTree; ENSGT00940000164828; -.
DR OMA; MHGIPAD; -.
DR Proteomes; UP000261340; Unplaced.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:UniProtKB-EC.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16206; EFh_PRIP; 1.
DR CDD; cd13364; PH_PLC_eta; 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; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF85; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF16457; PH_12; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 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 PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 17..127
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 494..610
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 610..739
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 114069 MW; 3BFF87BA414C6E95 CRC64;
SSMPSDRKIN STAACMAFMM EGCEMKKVRS NSRMYNRYFL LDPDMHWLRW EPSKKDSEKA
KLEIKSIKEV RLGKKTPVLR SNGLSDQFPD ECAFSIIYGD NYESLDLVAS TADVVSTWVM
GLRYLVSYGR HTVDMMEPSQ PSLRTSWIGS VFELADVEKE GHIDLFRATQ IIKGLNPGMK
ESRIQLKFKE FQKAKDQYGE AINLDTFVEA YCELCTRPEI FFLLVQFSSN KEYLDSKDLM
LFVEVEQGVE GVTEDMCRDI VQKFEPSAEG RERGYLSIDG FTHYLLSSEC HIFDPQHKRV
CQDMTQPLSH YYINSSHNAS LLEDHFWGSS DISSYIRALR MGCRSIEVIV WDGPDNEPVV
YVGSSVASQL VFSKVLDIIN QYAFESSEYP LILCLVTHCC IPQQRVMAQH MKKILGDKLF
IDSPNKEENY LPSPEKLKGK ILLKGKKLPP SCTDAEGDVT DEEEGLEMSQ RVGTDEKDQL
NGLGCKTLRL CRELSDLVSL CKSVQFRDFE FSKRDQKYWE ICSFNEVDAN KFANEFPEEF
VCYNKRFLSR VYPTPMRIDA SNMNPQDFWK CGCQIVAMNY QTPGLMMDLN LGWFRQNGNC
GYVLRPAIMR EEVSYFSANA RDSLPGVSAQ LLHIKVISGQ NLPKPRGSAA KGDVVEPYIY
VEIHGIPADC AEQRTKTVSQ NGDNPIFDES FEFQINLPEL AVLRFVVLDD DYIGDEFIGQ
YTIPFECLQP GYRHVPLQSL TGEFLPNTTL FIHVAITNRR GGGKAHKKGI SVRKSRKARE
YTTTKTTGIK VVDELFRAST QPLREATDLR ENVQNAMVSF KELCGLTPAA NMKQCILTVS
TWLMNSERSL RVTVDLSETY PTMEAQGVVP ELLRKVLNAY DMMIQTSKTL IESADVVYSK
LTQAQRAGLD FHEDLHRIGG KEGLKGRKLQ KAMESYAWNI TVLKGQADLL KHAKSEALDT
LRQIHYAAQS CGLSKNGAAS PQLQLKEMMM RRKIRRVRSE TQV
//
