ID A0A368G8L5_ANCCA Unreviewed; 823 AA.
AC A0A368G8L5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=ANCCAN_13302 {ECO:0000313|EMBL:RCN40754.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN40754.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN40754.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN40754.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCN40754.1}.
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DR EMBL; JOJR01000269; RCN40754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368G8L5; -.
DR STRING; 29170.A0A368G8L5; -.
DR Proteomes; UP000252519; 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; cd16206; EFh_PRIP; 1.
DR CDD; cd08558; PI-PLCc_eukaryota; 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:SF196; PHOSPHOINOSITIDE PHOSPHOLIPASE C; 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; 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:UP000252519};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 581..701
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 700..823
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 535..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RCN40754.1"
SQ SEQUENCE 823 AA; 93698 MW; CEA43CACADB6F1F9 CRC64;
LNSCSLTSSR KALRSSLIKH VGRQKSPGRK TVSFSSKSDD KKISNVSDCW HFMQTGSEFV
KLRGSNRHFR RFFRARLFSV LMPTFHIFDG LRPTRSRTKR ENVVRSVAIE DIREVRLGKN
TEQLRLSDSN FGDLQDECLF SVIYGDDYET LDLVASCADD ANIWVTGLMA LTSTKYDCKP
TTIAWATLRE RLVSSSFQKY VMSSTKKIRK KFRTIYENAI IWLGSVFDEE DPDRKGFIDE
NTAVKLIRQT NPTLALSRIK NKVKEAGCSL DAVKRGKIHK DEFVELYKEI ATRPEVYFLM
VRYANKDYLS CQDLRLFLET EQGMVGVTTE FCENVVEQYE PSPEAKQNNF MTVDGFTAFL
LSKDCSIFDP SHSRVWMDMK QPFSKYFIAS SHKTYLVEDQ QGPANVDGLT SALKRNCRVI
ELDLWDPTES NGEIEPMVKN GLLALSKIPL SEALKTIRES AFDRSRYPLI LRLSVHCSCE
WQKVAAKLIV THLGTKLYLP SADPTDWSKE KAIPTPWDFQ QRILIMGKRL CCSSESGEVS
EDDDGIASTS RRKSRRKLLT TEAKNPKKCW KFSRIRLCRE LSDLVPPFLQ VKTVQDLMAT
APNSQTMNPR QHVAYLSETT ALRLTHTYAQ EFAQTSRDYV VCVSPNVTRA DSSNLNPQEF
WNHGIQMVGI NCQTPGLMVD LQEGRFAENG GCGYVLKPSV MNEDLFVAGD KLPNTPQILH
LRILSGQQLP RPRGSNAKGD SSDPFVVIEV FGIPGDCAEE RTKTIRNDGE RFFHCFHFSI
RKRNGHNPSF DESFQFQVSV PELALVRFLV LDDDFIGWAV FLC
//