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Database: UniProt
Entry: A0A368G8L5_ANCCA
LinkDB: A0A368G8L5_ANCCA
Original site: A0A368G8L5_ANCCA 
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
//
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