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Database: UniProt
Entry: A0A3Q1IT80_ANATE
LinkDB: A0A3Q1IT80_ANATE
Original site: A0A3Q1IT80_ANATE 
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
//
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