ID A0A093GWQ8_TYTAL Unreviewed; 791 AA.
AC A0A093GWQ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=N341_01360 {ECO:0000313|EMBL:KFV46973.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV46973.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV46973.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV46973.1};
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};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; KK378096; KFV46973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093GWQ8; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd08591; PI-PLCc_beta; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR Gene3D; 1.20.1230.10; Phospholipase C beta, distal C-terminal domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR014815; PLC-beta_C.
DR InterPro; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR009535; PLC-beta_CS.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF12; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-1; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF06631; DUF1154; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR Pfam; PF08703; PLC-beta_C; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 1.
DR SMART; SM00148; PLCXc; 1.
DR SMART; SM00149; PLCYc; 1.
DR SUPFAM; SSF69989; C-terminal domain of PLC-beta; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..791
FT /note="Phosphoinositide phospholipase C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001886522"
FT DOMAIN 201..317
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 317..447
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 131..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 642..670
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV46973.1"
FT NON_TER 791
FT /evidence="ECO:0000313|EMBL:KFV46973.1"
SQ SEQUENCE 791 AA; 90242 MW; E81444B4F3364811 CRC64;
AGPRLTRVFF QVLLSGCRCV ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF
KTSPFPILLS FENHVDSPKQ QAKMAEYCRL IFGDALLMDP LEKYPLEPGV PLPSPTDLMY
KILVKNKKKS HKSADGSAKK KLSEQASNTC SDTSSMFEPS SPGAGEAEIE SDDDDDYDDD
CKKSSMDEGT AGSEAMATEE MSNLVNYIQP VKFESFEVSK KRNKSFEMSS FVETKGLEQL
TKSPVEFVEY NKMQLSRIYP KGTRVDSSNY MPQVFWNAGC QMVALNFQTV DLSMQINMGM
YEYNGKSGYR LKPEFMRRPD KHFDPFTESI VDGIVANTLS VKIISGQFLS DKKVGTYVEV
DMFGLPVDTR RKALKTKTSQ GNAVNPVWEE ETIVFKKVVL PSLACLRLAV YEEGGKFIGH
RILPVSAIRP GYHYICLRNE RNQPLTLPAL FVYIEVKDYV PDTYADVIEA LSNPIRYVNL
MEQRAKQLAA LTLEDEEEVK KEIDHGDAPS EANNEPRPTP AENGSSLLPL GSVKAPAKTE
DLIQSVLTEV EAQTIEELKQ QKSFVKLQKK HYKEMKDLVK RHHKKTTDLI KEHTAKKKSK
AARFLGKKKS GPVIRKSSEK ALLMISETGS PDHSSSTIEQ ELAALDSEMS QKLVELKEKQ
QQQLLNLRQE QYYSEKYQKR EHIKLLIQKL TDVAEECQNS QLKKLKETCE KEKKELKKKM
DKKRQEKITE AKSKDKNQME EEKTEMIRSY IQEVVQYIKR LEDAQSKRQE KLVEKHKEIR
QQILDEKPKV K
//
