ID A0A093QPY5_PYGAD Unreviewed; 831 AA.
AC A0A093QPY5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 35.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
DE Flags: Fragment;
GN ORFNames=AS28_10367 {ECO:0000313|EMBL:KFW60759.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW60759.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW60759.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW60759.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL224504; KFW60759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QPY5; -.
DR STRING; 9238.A0A093QPY5; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
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; cd16209; EFh_PI-PLCbeta2; 1.
DR CDD; cd13361; PH_PLC_beta; 1.
DR CDD; cd08624; PI-PLCc_beta2; 1.
DR Gene3D; 2.30.29.240; -; 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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR028403; PLC-beta2_cat.
DR InterPro; IPR037862; PLC-beta_PH.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR015359; PLC_EF-hand-like.
DR InterPro; IPR046969; PLCbeta2_EF.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF10; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-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; PF17787; PH_14; 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; 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; 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:UP000054081};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 544..660
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 660..786
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 465..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 831
FT /evidence="ECO:0000313|EMBL:KFW60759.1"
SQ SEQUENCE 831 AA; 95525 MW; AD4830D9FB5B78BB CRC64;
MSMLTPVLQP PEVKEYLCKG ERFIKWDDET ASASPVILRV DPKGFYLYWT YQNKEMEILD
ITSIRDTRVG RFAKIPKCQK LREVFNLDYP HSTFLLKTLT IVSGPDMVDL TFHNFVSYKE
NVGKSWAEDI MAIVRNPLTY NASRYTFLEK ILVKLKMQLN AEGKIPVRNI FQMFPADRKR
VEAALSACHL PKGKNDAINP EDFPETVYKT FLMNLCPRPE IDEIFTSHHL KAKPYMTKEH
LAKFINKKQR DSRLNDILFP PAKPEQVQSL IEKYEPSVIN IQRGQLSPEG MVWFLCGPEN
NVIALDKLVL YQDMTQPLSH YFINSSHNTY LTAGQFSGIS SPEMYRQTLL AGCRCVELDC
WKGRPPDEEP IITHGFTMTT EILFKDAIEA IAESAFKTSL YPVILSFENH VDSPKQQAKM
AEYCRTIFGD MLLTEPLEKY PLKPGVPLPS PKDLLGKILI KNKKKQSISG KRQNSLKKGK
NVEPEIIEQP TPMDAEDTVW AGDVAEEEPE EEDEHHGNLD EEEIKKMQSD EGTAGLEVTA
YEEMSSLVNY IQPIKFDSFE VSAQKNRSYV ISSFTELKAY DLLTKFPVQF VEYNKRQMSR
IYPKGTRMDS SNYMPQMFWN VGCQMVALNF QTMDVPMQQN MALFEFNGQC GYLLKHEFMR
RPDKQFDPFS VDRIDVVVAS TLSILSGQFL SDRSVKTYVE VELFGLPRDT KRKYRTKLTS
TANSINPVWK EEAFVFEKIM MPELASLKIV AWEEGGKFIG HRVIPVIAVH SGYHHVCLRS
ESNMPLTMPS LFVYLEIKDY VPDAWADLTI ALSNPIKFFS LQDKRSVKLK D
//
