ID Q6CD33_YARLI Unreviewed; 955 AA.
AC Q6CD33;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 143.
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=YALI0_C04180g {ECO:0000313|EMBL:CAG81728.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG81728.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG81728.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382129; CAG81728.1; -; Genomic_DNA.
DR RefSeq; XP_501429.1; XM_501429.1.
DR AlphaFoldDB; Q6CD33; -.
DR STRING; 284591.Q6CD33; -.
DR EnsemblFungi; CAG81728; CAG81728; YALI0_C04180g.
DR GeneID; 2909392; -.
DR KEGG; yli:YALI0C04180g; -.
DR VEuPathDB; FungiDB:YALI0_C04180g; -.
DR HOGENOM; CLU_002738_1_2_1; -.
DR InParanoid; Q6CD33; -.
DR OMA; HWQREMS; -.
DR OrthoDB; 2900494at2759; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR CDD; cd00275; C2_PLC_like; 1.
DR CDD; cd16207; EFh_ScPlc1p_like; 1.
DR CDD; cd13360; PH_PLC_fungal; 1.
DR CDD; cd08598; PI-PLC1c_yeast; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001192; PI-PLC_fam.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR037755; Plc1_PH.
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; PF00168; C2; 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; SM00054; EFh; 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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361133};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|RuleBase:RU361133};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU361133};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT DOMAIN 379..414
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 707..822
FT /note="PI-PLC Y-box"
FT /evidence="ECO:0000259|PROSITE:PS50008"
FT DOMAIN 810..941
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 56..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 107404 MW; 8399EDB522CB1A4B CRC64;
MSLEHIAPLD LENRPQRAIA RYKSLEALRG RKDSYPPLRN SVIQETQDDS ALDLELSEHS
DPNDTNDPND TNNSNDTSLF ATDLSPAASA PVLGTVPPLI PPIVTNTTPF SVPISPRLST
SSSPRFSPRF SPSSLANTLA SSLSISPTLG STVMELPTAL ARKLSRRGLS TSPPFRSRSS
SCPSVEMPIT RHKNSEEQSA GNVATVSSIL SSESAEVTVP LVLQQGMPFL RITHKKKVQR
MFKIDPVTGK VSWDDKKASA CFSVDTICEI SLQENARNHR EELKVSSNHE SRWVTITYMK
NKRRKPLHLV APTKEEFTLF VDALQNLVYF RQELMRGFQS SNPKIASVHW KSYAAKEQGE
ERLTFEAVQR LAQRHHVLCS KAYLKSKFDE ADVDKSGFLE FNEFKIFVKL LKRRPEIVTL
YYQTLGKPEP ANIWSDDRMT RDDLLGFLDH VQRTRFEPHI FEKIWAKFAP KDDTFDSSLD
YWTVDSFNDF LLSSYNLFVK PETNLNRPLN EYYISTSHNT YLIGRQVADT SSEEGYIRAL
QSGCRSVEID IWDGPDDRPV VKHGRTFTSS VSVEDVCSAI RKYGFIASPN PLILSLEIHC
SASNQLKVVD ILKGTFGENL VTQPLVPGAL NLPSPHELKH RVLIKVKAGR EPVAGDKNNG
ASFSSSYTSS STTTASEFDD LSGTPSVSGG GKRKDTSGTT KKIVPALGEL GVYVQGLKFR
NFAFPESKTT NHCFSFSERK FISICKDPEN REQMMKHNRR YLTRIYPSGY RVKSSNLNPL
YFWQNGAQMV ALNWQTYDLP AQLNDAMFAA RGGYVLKPPY LRHLKSPRSG HSVNLSFISA
QQLPRPKDLG KSSFDPYIVA QLHGPGENHK LKTSPVIDNG FNPRWNKDWS LSLSPEDYEF
SFVQITLYTQ DRPFAVSCLR LSSLNEGYRH VPLNDLQGEE YLFSTLFMKV SKISN
//
