ID   LIP3_CANAX              Reviewed;         471 AA.
AC   Q9P8W2;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 2.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Lipase 3;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP3;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=1161;
RX   PubMed=11131027; DOI=10.1007/s002030000218;
RA   Hube B., Stehr F., Bossenz M., Mazur A., Kretschmar M., Schaefer W.;
RT   "Secreted lipases of Candida albicans: cloning, characterisation and
RT   expression analysis of a new gene family with at least ten members.";
RL   Arch. Microbiol. 174:362-374(2000).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11131027}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF191316; AAF69520.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P8W2; -.
DR   SMR; Q9P8W2; -.
DR   ESTHER; canal-LIP3; Fungal-Bact_LIP.
DR   PRIDE; Q9P8W2; -.
DR   CGD; CAL0000182579; LIP3.
DR   VEuPathDB; FungiDB:C1_09900W_A; -.
DR   VEuPathDB; FungiDB:CAWG_00442; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR005152; Lipase_secreted.
DR   PANTHER; PTHR34853; PTHR34853; 1.
DR   Pfam; PF03583; LIP; 1.
DR   PIRSF; PIRSF029171; Esterase_LipA; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism; Secreted;
KW   Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..471
FT                   /note="Lipase 3"
FT                   /id="PRO_0000017822"
FT   ACT_SITE        196
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        344
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        422
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  51226 MW;  15AC64A3B11BD868 CRC64;
     MKTLVVLCTL LSIIFASPLS LKSPLVDDFY NPPRGYESAK LGEILKLRKT PGKISSLFIP
     VEVKNSWQLL VRSEDSFGNA AAIVTTVIEP FNADPSKVVS YQSWEDAANI ECSPSYGMQF
     GAPLSSVQTQ VDMIFIVPLL DKGCFVVLPD YEGPKSTFGV GRQSGKATLD SIKAVLKTKD
     FSGINDDAQV AMWGYSGGTI AAGWAATLQP KYAQELKKNL IGAALGGFVI NITATAEATD
     GTLFAGLIPN ALNGLANEFP DFKKRMYEVV EKRYEGALQQ GTQHCLGGAI LHFAFDQVFT
     GDHRYFEQGY GLLEEEVFNR TISGNSLLYM DQEYLPDIPI FVYHGSLDGI VPIPDVHGVY
     KNWCDWGIDS FEFAEDSLNG HLTEIVVGAP AAITWLDARF DGQPVVEGCK KTTRITNFSY
     PNISDSTRNF FKGILDSLTA SQLGPGVTSD NVTLSGLTGF MGGLSKFKKS V