ID A0A1Y3BNL5_EURMA Unreviewed; 464 AA.
AC A0A1Y3BNL5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 21.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|RuleBase:RU361133};
GN ORFNames=BLA29_005084 {ECO:0000313|EMBL:OTF81186.1};
OS Euroglyphus maynei (Mayne's house dust mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Analgoidea;
OC Pyroglyphidae; Pyroglyphinae; Euroglyphus.
OX NCBI_TaxID=6958 {ECO:0000313|EMBL:OTF81186.1, ECO:0000313|Proteomes:UP000194236};
RN [1] {ECO:0000313|EMBL:OTF81186.1, ECO:0000313|Proteomes:UP000194236}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:OTF81186.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:OTF81186.1};
RA Arlian L.G., Morgan M.S., Rider S.D.;
RT "Genome Survey of Euroglyphus maynei.";
RL Submitted (MAR-2017) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
CC sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
CC Evidence={ECO:0000256|ARBA:ARBA00000110};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:OTF81186.1}.
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DR EMBL; MUJZ01014904; OTF81186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3BNL5; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000194236; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 2.30.29.240; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
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 PANTHER; PTHR10336:SF149; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE CLASSES I AND II; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF09279; EF-hand_like; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
DR SMART; SM00148; PLCXc; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000194236}.
FT DOMAIN 149..299
FT /note="Phosphatidylinositol-specific phospholipase C X"
FT /evidence="ECO:0000259|SMART:SM00148"
FT REGION 297..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 53260 MW; 7E97F022CF598000 CRC64;
MKMFANHKDD RKKIEKALES CSLSSAKNDS ISLEKFDMNT FFNFYKHLIC RNEVLEIFEK
ICCDHTYGNT KVMTVEQFVQ FLNKEQRDPR LNEILYPYAN LSRGMDLIEQ HEPDPEISQK
GFLSFDGFLR YLMSDDNAII PSEKFDLNSD MDQPLSHYFI NSSHNTYLTG HQLTGRSSVE
IYRQCLLGGC RCIELDCWNG RSDDEPIITH GYTVVTDVPL KEVLEAIAES AFKTSHYPVI
LSFENHCSNK QQLAKMARYC RQIFGEMLLT EPLPSHPLKP GVPLPSPNLL LKKIIIKDKK
EHKHSRRKSK NLESNHEESS NIPNVSTATS FDEVRPENTN QVNVAVSNKQ QNHQQQQQQQ
STSQQKTNDL ETNENHSNDL NSSTDLNSNK NYSCDIEDPE SGDSCSDDDE VMNEEQSISA
DLPVAKETAD SPYVYRSEMS ELVIYVQPIQ FRAFDMAESK ILFF
//
