ID   LIP3_YARLI              Reviewed;         498 AA.
AC   Q96VC9; Q6CFD8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Lipase 3;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP3; OrderedLocusNames=YALI0B08030g;
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=INAG135668;
RA   Choupina A.;
RT   "Isolation and characterization of genes encoding lipase activities in
RT   Yarrowia lipolytica.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
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; AJ249751; CAC43239.1; -; Genomic_DNA.
DR   EMBL; CR382128; CAG82865.1; -; Genomic_DNA.
DR   RefSeq; XP_500624.1; XM_500624.1.
DR   AlphaFoldDB; Q96VC9; -.
DR   SMR; Q96VC9; -.
DR   STRING; 284591.Q96VC9; -.
DR   ESTHER; yarli-LIP3; Fungal_carboxylesterase_lipase.
DR   MEROPS; S09.A63; -.
DR   EnsemblFungi; CAG82865; CAG82865; YALI0_B08030g.
DR   GeneID; 2907630; -.
DR   KEGG; yli:YALI0B08030g; -.
DR   VEuPathDB; FungiDB:YALI0_B08030g; -.
DR   HOGENOM; CLU_006586_14_0_1; -.
DR   InParanoid; Q96VC9; -.
DR   OMA; WIYGGSQ; -.
DR   Proteomes; UP000001300; Chromosome B.
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           ?..498
FT                   /note="Lipase 3"
FT                   /id="PRO_0000008628"
FT   ACT_SITE        200
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        409
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        384
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        60..91
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   498 AA;  55872 MW;  0F11DE0449B5580F CRC64;
     MPLELPSLNA SIVGNTVQNG AVEQFLNIRY ADIPGKFEKP VLKNDWNGAE IDATKVGPVC
     PQPRTPFNFF SVPDDLWEKV NVDTYQDGLL CDNLIVTRPK GVSANARLPT VVWIHGGSNI
     EGSIYNLIYE PQFLVAESVR VGKPIVHVCI EYRLGLAGFL TKNGKGNWGT WDQYTGCQWV
     NRHIQDFGGD PLNVTLTGES AGSVAVHNML IKDSMNGRKL FRNAVMMSGT LETITPQPPK
     WHARLEEKVA KVTGKEVADL ASLSDKELLD AQIKLNVAVC MTCDDGDFFE PGWKQHLTPD
     WLDKLIISDC KDEGMLYFLP VNAQDDEELL AKVAKSPVGK EISELYGIKE GGDIKSACLD
     LKTDATFNYF NHLLFKKMEE ARNNGSTSRV YRLAVDEPNP HNPDQRAHHA VDVLYMFNST
     KFNEHGDKLS RLFQSHFLRL AYGLEPWDHR NFGVYRNGGY QQLPLSELNK VRPVERYEAL
     SKMDFGQVGR LSNALSRL