ID   LIP2_CANAX              Reviewed;         466 AA.
AC   Q9P8W5;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Lipase 2;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP2;
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; AF189152; AAF34253.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P8W5; -.
DR   SMR; Q9P8W5; -.
DR   ESTHER; canal-LIP2; Fungal-Bact_LIP.
DR   VEuPathDB; FungiDB:C1_09420W_A; -.
DR   VEuPathDB; FungiDB:CAWG_00487; -.
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   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..466
FT                   /note="Lipase 2"
FT                   /id="PRO_0000017821"
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        331
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   466 AA;  50422 MW;  C4F4C994B761F42C CRC64;
     MKGLVFLLGL LPTIYASLVH ITPASEDDFY NPPAGFESAK NGDILKLRNS PNRLASFYFP
     IDVKNAWQLL VKSEDSFGNP NAFVTTLIEP YNADPSKVVS YQTWEDASNI NCSPSYGAQF
     GSPLSTITTQ IDMTLIVPPL RSGYYVVTPD YEGPKATFAV GRQSGQATLD SVRAILKSGS
     FSGINEDAKV ALWGYSGGSL ATGWAAALQP VYAPELQKNI VGAAVGGFAA NITAIAESVD
     GTIFSGLITL ALNGLANEYP DLKTAFYEEL SDFAVPEFKA GAENCLAENI FHYPLHQYFT
     GPKRAFEKGW GLLKEDIFNK SIQDNLLIGL NKTYLPQVPV LIYHGTVDEI IPIKDPHAQY
     QLWCDWGIES LEFAEDLSTG HLAETFTGAP AALAWIDARF DGKTPIQGCS HTTRLTNLLY
     PNTSDSTHSY FLGIYQAVFG TPLGPGINGD NITINSGLLG LVSSII