ID   LIP1_CANAX              Reviewed;         468 AA.
AC   O94091; Q9P8W6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Lipase 1;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP1;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-468.
RC   STRAIN=ATCC 36082;
RX   PubMed=9043110; DOI=10.1099/00221287-143-2-331;
RA   Fu Y., Ibrahim A.S., Fonzi W., Zhou X., Ramos C.F., Ghannoum M.A.;
RT   "Cloning and characterization of a gene (LIP1) which encodes a lipase from
RT   the pathogenic yeast Candida albicans.";
RL   Microbiology 143:331-340(1997).
CC   -!- FUNCTION: Hydrolyzes triglycerides.
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; AF188894; AAF35171.1; -; Genomic_DNA.
DR   EMBL; U34807; AAC99990.1; -; Genomic_DNA.
DR   AlphaFoldDB; O94091; -.
DR   SMR; O94091; -.
DR   ESTHER; canal-LIP1; Fungal-Bact_LIP.
DR   CGD; CAL0000177069; LIP1.
DR   VEuPathDB; FungiDB:C1_09580C_A; -.
DR   VEuPathDB; FungiDB:CAWG_00472; -.
DR   OMA; EGCTIQN; -.
DR   PhylomeDB; O94091; -.
DR   GO; GO:0005576; C:extracellular region; IDA:CGD.
DR   GO; GO:0016298; F:lipase activity; IDA:CGD.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IDA:CGD.
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..468
FT                   /note="Lipase 1"
FT                   /id="PRO_0000017820"
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        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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   468 AA;  50811 MW;  4FF3C05A948B14DA CRC64;
     MRGIAVFLAF ISLIFASPLT VKSPLVDDFY TAPDGYESAK LGEILKLRKT PSKLSSMFFE
     IDIKNSWQLL VRSEDSFGNA TAIVTTVIEP YNADPSKVLS YQTFEDSANI ECSPSYGMQY
     GAPWSTVATQ IDMALMVPML KQGYYVVSPD YEGPKSTFTV GRQSGKATLD SIRAILKSNK
     FTGIKSDAKV AMWGYSGGSL ASGWAAALQP KYAPELKKNL IGAALGGFVT NITATAEATD
     GTLFAGLVPN ALSGLANEYP EFKEILYQKV SKAATDNLRQ GTEHCIGGAI LYFAEDQYFT
     GDDRAFPGGY GLLKEEVVNK TISENNLMQM DKDYLPDIPI FVYHGALDSI VPISNVHVTY
     KNWCDWGINS FEFSEDLLNG HITETIVGAP AAITWLEARF DGEPVVKGCK KTSRITNFSY
     PNISDSTSSI FEGILNSVTG SELGPGVTSD NITLDGLTGF LGNFIDLK