ID   LIP1_YARLI              Reviewed;         486 AA.
AC   Q99156; Q6C6C2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP1; OrderedLocusNames=YALI0E10659g;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 90811 / CLIB 163 / JM12;
RA   Gonzalez F.;
RL   Thesis (1996), University of Salamanca, Spain.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC         H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; Z50020; CAA90323.1; -; Genomic_DNA.
DR   EMBL; CR382131; CAG79381.1; -; Genomic_DNA.
DR   RefSeq; XP_503790.1; XM_503790.1.
DR   AlphaFoldDB; Q99156; -.
DR   SMR; Q99156; -.
DR   STRING; 284591.Q99156; -.
DR   ESTHER; yarli-lipa1; Fungal_carboxylesterase_lipase.
DR   EnsemblFungi; CAG79381; CAG79381; YALI0_E10659g.
DR   GeneID; 2912789; -.
DR   KEGG; yli:YALI0E10659g; -.
DR   VEuPathDB; FungiDB:YALI0_E10659g; -.
DR   HOGENOM; CLU_006586_14_0_1; -.
DR   InParanoid; Q99156; -.
DR   OMA; SFFLEWE; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Reference proteome; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..486
FT                   /note="Lipase 1"
FT                   /id="PRO_0000008627"
FT   ACT_SITE        193
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        303
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        392
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        58..82
FT                   /evidence="ECO:0000250"
FT   CONFLICT        31..32
FT                   /note="IP -> RR (in Ref. 1; CAA90323)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="N -> D (in Ref. 1; CAA90323)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  55380 MW;  497A796EF64D7EA7 CRC64;
     MSVTSTSLNG TFNGISEDGI EIFKGIKYAN IPYRWAYAER IDDYDNGVFD CTQEGMACPQ
     VLPFDYNIEK GPKEMPFDEF ECSNLMITRP QGATNLPVFV WIHGGGNLAG NGYCSDHNPV
     PFVKHSIVAG RPVLHVMIEY RLSAFGYLAV PDTNGNWVGN WGARDQYTAL QWISKHIVEF
     GGDPSQITIG GESAGSIGLH ALMVHESMKP KEECIIHNVI LSSGTMDRMG TGTISENAFK
     PIYDGIKTLV GDINTCSADE LLEAQIKAGL DLGFYLQDDF FPPDWRNVRF KVSRVLLSDV
     IVDGTNFKNK INPAVRVTPE NDFDHKVFKL YNISTEDTWE DYHYKMMLFK GDETFIRGNQ
     QLELLFEQEN IPVWRQLFDQ IHPNDPSRLC HHAVDLYYMW DNWEMPEDKH AVARQYQDTL
     TKFVYGQDPW PVDKLHYVHD NQFEILDKSQ FGDFRNVPAL KFLLGFSAEE LGELTKKYTG
     EGHYTL