ID   LIP5_DIURU              Reviewed;         549 AA.
AC   P32949;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Lipase 5;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP5;
OS   Diutina rugosa (Yeast) (Candida rugosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetales incertae sedis; Diutina.
OX   NCBI_TaxID=5481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506;
RX   PubMed=8440480; DOI=10.1016/0378-1119(93)90760-z;
RA   Lotti M., Grandori R., Fusetti F., Longhi S., Brocca S., Tramontano A.,
RA   Alberghina L.;
RT   "Cloning and analysis of Candida cylindracea lipase sequences.";
RL   Gene 124:45-55(1993).
RN   [2]
RP   REVIEW.
RX   PubMed=9778794;
RX   DOI=10.1002/(sici)1097-0061(19980915)14:12<1069::aid-yea303>3.0.co;2-k;
RA   Benjamin S., Pandey A.;
RT   "Candida rugosa lipases: molecular biology and versatility in
RT   biotechnology.";
RL   Yeast 14:1069-1087(1998).
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; X66008; CAA46807.1; -; Genomic_DNA.
DR   PIR; JN0553; JN0553.
DR   AlphaFoldDB; P32949; -.
DR   SMR; P32949; -.
DR   ESTHER; canru-5lipa; Fungal_carboxylesterase_lipase.
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   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Signal.
FT   SIGNAL          1..15
FT   CHAIN           16..549
FT                   /note="Lipase 5"
FT                   /id="PRO_0000008623"
FT   ACT_SITE        224
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        356
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        464
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        75..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        283..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   549 AA;  58420 MW;  0F3D04C9716F6F22 CRC64;
     MKLALALSLI ASVAAAPTAT LANGDTITGL NAIINEAFLG IPFAEPPVGN LRFKDPVPYR
     GSLNGQSFTA YGPSCMQQNP EGTYEENLPK VALDLVMQSK VFQAVLPNSE DCLTINVVRP
     PGTKAGANLP VMLWIFGGGF EIGSPTIFPP AQMVSKSVLM GKPIIHVAVN YRLASFGFLA
     GPDIKAEGSS NAGLKDQRLG MQWVADNIAG FGGDPSKVTI FGESAGSMSV LCHLLWNGGD
     NTYKGKPLFR AGIMQSGAMV PSDPVDGTYG TQIYDTLVAS TGCSSASNKL ACLRGLSTQA
     LLDATNDTPG FLSYTSLRLS YLPRPDGANI TDDMYKLVRD GKYASVPVII GDQNDEGFLF
     GLSSLNTTTE ADAEAYLRKS FIHATDADIT ALKAAYPSDV TQGSPFDTGI LNALTPQLKR
     INAVLGDLTF TLSRRYFLNH YTGGPKYSFL SKQLSGLPIL GTFHANDIVW QHFLLGSGSV
     IYNNAFIAFA TDLDPNTAGL SVQWPKSTSS SQAGDNLMQI SALGLYTGKD NFRTAGYNAL
     FADPSHFFV