ID A0A1E3NHB0_9ASCO Unreviewed; 948 AA.
AC A0A1E3NHB0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphoinositide phospholipase C {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
DE EC=3.1.4.11 {ECO:0000256|ARBA:ARBA00012368, ECO:0000256|RuleBase:RU361133};
GN ORFNames=PICMEDRAFT_74439 {ECO:0000313|EMBL:ODQ44733.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ44733.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ44733.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ44733.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454006; ODQ44733.1; -; Genomic_DNA.
DR RefSeq; XP_019015846.1; XM_019164771.1.
DR AlphaFoldDB; A0A1E3NHB0; -.
DR STRING; 763406.A0A1E3NHB0; -.
DR GeneID; 30181458; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000094455; 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 GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProt.
DR CDD; cd08598; PI-PLC1c_yeast; 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; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR InterPro; IPR001711; PLipase_C_Pinositol-sp_Y.
DR PANTHER; PTHR10336:SF36; 1-PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE PHOSPHODIESTERASE GAMMA PLC-3; 1.
DR PANTHER; PTHR10336; PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C FAMILY PROTEIN; 1.
DR Pfam; PF00388; PI-PLC-X; 1.
DR Pfam; PF00387; PI-PLC-Y; 1.
DR PRINTS; PR00390; PHPHLIPASEC.
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; 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:UP000094455}.
FT DOMAIN 556..681
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 108111 MW; C67BD9C97A317898 CRC64;
MPPKEQLVPP PSAHEEAGDP SNYQPGSPVI EEDSVKLIDP FDPSDPDSFP PDLLSPGIDM
IRVTRRKRIR RAFKLTLPSL TLTWNSKSKS KVEMDKIQSI RVGEDARNYR EEFNVSKEFN
ALWITVIYIS SNSSHSSALL CNDLKALHMI ATTKRNYDIM LKTLKLLSQW SKEQESLVSC
ADVNEFSKIK WDNKTKKLER QLLSFEDVLK LTSELHVYMD VSYLRLYFDQ CDTNKKKSLD
FPQFQTFVSK LRSRPEFGAI FHGLNIRNGK MLLSDFRIFV RETQNESSLS DTLINDIFVK
FSHGKSLDSY MSTSDLSYYL NSPYATALFN EESLDPHYYS HPLTDYFISS SHNTYLLGKQ
FHGFSSIEGY IHALQRGCRC IEIDVWDGIS TSTKEQHPIV THGHTLTNSI EFKLVVDIIR
KYAFITTPYP LIISLEIRCS QESQLKCVAI MKTIFGDMLV LHSKVNESIM PSPEELKHKI
LVKVKKSKST TIIEPQGSPH SLHSSFSTSS TQSDDINPNY TENKYDEEEV THRDNSNSLK
KMVSKPTART LIVPELTALA PYFVGIKFRN FSLPESKTYN HVFSFSDRTL LLLLRDKTKL
VSILKHNRRG MMRVYPSVVR FRSDNFNPIT FWELGCQMAA TNWQIWDCGE ELSESLFASI
GSEMASGLGY SGYRLKPKNM RNLEMNTSTY DKEKLKVQTL SSLVFDKEHF FDVSILSGQQ
LPKPKDFGNT GSDGYTPWVE VEVYNVLPVH AEIVHLHRYN RAGTLDEEKD DIEDEKDGEV
GEAENEKEET RKEDEFNIST DKQQAIENAS DGKINSKLTK AGSVKLSHVE AMSANPNHSV
LFKTRFAENP GNAFSPKWNA SCRLKYLTNE NDLAFIRVAV KTLRASKTKS GVIGKVSTVV
KNNNNDYTIG SWCCKIGDLK QGYRHIRLGD NKGEELIYSS LFIKIETK
//
