ID A0A0K0CT27_ANGCA Unreviewed; 628 AA.
AC A0A0K0CT27;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
OS Angiostrongylus cantonensis (Rat lungworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=6313 {ECO:0000313|Proteomes:UP000035642, ECO:0000313|WBParaSite:ACAC_0000018401-mRNA-1};
RN [1] {ECO:0000313|Proteomes:UP000035642}
RP NUCLEOTIDE SEQUENCE.
RA Martin A.A.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:ACAC_0000018401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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 AlphaFoldDB; A0A0K0CT27; -.
DR STRING; 6313.A0A0K0CT27; -.
DR WBParaSite; ACAC_0000018401-mRNA-1; ACAC_0000018401-mRNA-1; ACAC_0000018401.
DR Proteomes; UP000035642; 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 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; IPR042531; PLC-beta_C_sf.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF211; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE BETA-4; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00239; C2; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000035642}.
FT DOMAIN 71..187
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 190..312
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 349..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 495..522
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 561..610
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 628 AA; 71508 MW; 4D3DD5413AED857C CRC64;
SYFECTDFSG DPVQCKEIDE AHPELKQNFI SKNLKSLGFS KKQPILTKEE EERIFAEYHY
TGATTNIHPL LSSLINYTHP VKFSGFDVAE NNNLHFHMSS FSESTGLGYL KQCAPEFVNY
NKRQLSRIYP KGARVDSSNF LPQIFWNAGC QMVALNFQTA DVYMQLNMGK FEYNSGSGYL
LKPDFMRRPD RTFDPFSESP VDGVIAAHCS VRVISGQFLT DRKVGTYVEV EMYGLPTDTI
RKEHRTKVIP ANGLNPVYNE VPFTMVLAPT LFVHIVIKTY VPDELSGLVD ALADPRAYLS
EQKKRQEALA HMGVDDSDIV EVPTGKSLSA KTKMLQKTNG STANLLMEKE NPPSARSEGC
GATSGTSKAN NEALPAAVDK FKVDPIDVDE LKKDKLNGKG YEYCLIVTFQ QTNVDKLMTN
NRRSMRKEKG TRRQISENLD EAGASDIANN DRVRTLVTVQ TDEWSAMMRR HETEEFELRK
AQLREQTEIL RKLLLEAQKV QMHGLKLRLE SETKELKLAQ TKKSMEDAKV LSLCDCFATE
LVIDFKDKGI KTKAERERRL KELHEKNLKM FVEERKRLAK KAEKHEEQLA KRHQDQLEHL
DREAIHALEQ EEANFKEDQL SSKPASIV
//
