ID A0A091L3L5_CATAU Unreviewed; 565 AA.
AC A0A091L3L5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JUN-2023, entry version 40.
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=N323_08625 {ECO:0000313|EMBL:KFP49908.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP49908.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP49908.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP49908.1};
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; KL292965; KFP49908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091L3L5; -.
DR Proteomes; UP000053745; 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; cd08629; PI-PLCc_delta1; 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; 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:SF80; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA-1; 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; 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; 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:UP000053745};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 306..422
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 422..550
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 248..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP49908.1"
FT NON_TER 565
FT /evidence="ECO:0000313|EMBL:KFP49908.1"
SQ SEQUENCE 565 AA; 64352 MW; 190C91EAFE731582 CRC64;
DKSKTEALED DEIEEFYKIL TERKEIDKIF QKYSDAEGFM SCQNLVRFLY EMQQEEDAVV
AAPALIQRYE PNERARRGNA MTKDGFLMYL LSDDGNIFNS SHRKVYQDMT QPLSHYLVSS
SHNTYLMEDQ LTGPSSTEAY IRALTKGCRC VELDCWDGPN SEPIIYHGYT LTSKILFSDV
IKAIKNYAFK TSPYPVIISL ENHCSVDQQK VMAQHMTTIL QDMLLVAPVD GNKSQFPSPE
QLKGKILVKG KKLSREEDPT GTNGNNNLEA EDVSDEDEAA EIEDESVKTE IQQKGKSDTL
KLAKELSDTV VYCKSVHFNG FEDPSHPRAF YEMSSFTESK ALKLAQESGT SFIHHNIRHL
SRIYPAGWRT DSSNYNPVDL WNVGCQIVAL NFQTAGTEMD VYQGRFQDNG FSGYVLKPEF
LRDEQTKFNP KSITEGTWGT KKKLLLKIIS GQQLPKVNKS KNSIVDPKVT VEIHGVQQDN
NKKQTKVIEN NGFNPKWDEE FTFDIEIPAL ALVRFVVEDF DMSTKNDFIG QYTLPFTSLK
QGYRHIHLLT KNGDPYSSST LFVYI
//
