ID A0A3Q1IT80_ANATE Unreviewed; 1113 AA.
AC A0A3Q1IT80;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000007041.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000007041.2}
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; A0A3Q1IT80; -.
DR Ensembl; ENSATET00000007161.2; ENSATEP00000007041.2; ENSATEG00000004933.2.
DR GeneTree; ENSGT00940000155660; -.
DR InParanoid; A0A3Q1IT80; -.
DR Proteomes; UP000265040; 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; cd13364; PH_PLC_eta; 1.
DR CDD; cd08597; PI-PLCc_PRIP_metazoa; 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:SF84; INACTIVE PHOSPHOLIPASE C-LIKE PROTEIN 2; 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 Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 121..231
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 596..712
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 712..841
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 125057 MW; F88C77F19140F580 CRC64;
MLEVPMAECG EDGSLPPLNL GDTAVPSDED TGKTHCEVSV LNGECGMSEN MVGSGSIVAP
GNEAGVDTAN TSVGLDGKSD LPRRSSIIKD GSRQRKERKK TVSFSSMPTE KKISSASDCI
SAMVDGSELK KVRSNSRIYH RYFLLDADMQ SLRWEPSKKE SEKAKIDVKS IKEVRTGKNT
DTFRTNGTYD QISEDCAFSI IFGENYESLD LVANTADVAN IWVTGLRYLI SYGKHTLNMM
ETSQNNMHLS WLGEFFDEVD SNNSRQITIC AAVQLVKRLN PGLKNVKIEL KFKELHKAKD
KTGSDVTKEE FIEVFHDLST RPEIYFLFVQ FSSNKEFMDS KDLMIFLEAE QGMAEVSEDT
SLEVIQKYEP SKEGQLKGWL SLHGFTNYLM SPECHIFDPE QKTVCQDMNQ PLSHYYINSS
HNTYLIEDQF RGPSDVTGYI RALKMGCRSV ELDVWDGPDN EPVIYTGHTM TSQIVFRSVI
DVINKYAFVA SEFPLILCLE NHCSLKQQRV MFQHLKKIFG DKLYLDTPKT EDCYLPTPYD
LKGKILLKGK KLSTNCTASE GEVTDEDEGA EMSQRVSIES DEQTVAPKKF QLSKDLSDLV
TLCKSVEFKD FQTSFQCQKY WELCSFNEVF ASRCASDSPG EFVNYNKRFL ARVYPSPMRI
DSSNMNPQDF WKCGCQIVAM NYQTPGLMMD LNIGWFRQNG NCGYVLRPAI MREQVSYFSA
NTKDSVPGVS PQLLHIKIIS GQNFPKPKGS GAKGDVVDPY VYVEIHGIPA DCAEQRTKTV
NQNGDNPLFD ESFEFQINLP ELAMVRFVVL DDDYIGDEFI GQYTIPFECL QPGFRHIPLQ
SLTGELLPHS LLFVHVAITN RRGGGKPHKR GLSVRKGKRS REYASMRVLL IKAVDDVFKT
AIVPLREATD LRENMQNAIV SFKELCGLSA VANLKQCILA LSPRLIGPDN SPLLVFNLND
QYPNMEAQGL IPEVLKKVTT NYEMVIQTSK TLLENFDGVY ERILQTQKAA MEFHENLHEL
AVKEGLKGRK LHKAVESFTW NITILKGQAD LLKHARSEVQ ENLKQIHYAA LTSNLSKGGA
VGGSTGSESK SRRSLEAIPE KATAEEELTD EDN
//