ID   LIP4_DIURU              Reviewed;         549 AA.
AC   P32948;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 89.
DE   RecName: Full=Lipase 4;
DE            EC=3.1.1.3;
DE   Flags: Precursor;
GN   Name=LIP4;
OS   Diutina rugosa (Yeast) (Candida rugosa).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Debaryomycetaceae; 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; X66007; CAA46806.1; -; Genomic_DNA.
DR   PIR; JN0552; JN0552.
DR   AlphaFoldDB; P32948; -.
DR   SMR; P32948; -.
DR   ESTHER; canru-4lipa; Fungal_carboxylesterase_lipase.
DR   GlyCosmos; P32948; 1 site, No reported glycans.
DR   GO; GO:0004806; F:triacylglycerol lipase activity; IEA:UniProtKB-EC.
DR   CDD; cd00312; Esterase_lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR050654; AChE-related_enzymes.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR   PANTHER; PTHR43918:SF4; CARBOXYLIC ESTER HYDROLASE; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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 4"
FT                   /id="PRO_0000008622"
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        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;  58571 MW;  39C7160852F7E655 CRC64;
     MKLALVLSLI VSVAAAPTAT LANGDTITGL NAIINEAFLG IPFAQPPVGN LRFKPPVPYS
     ASLNGQKFTS YGPSCMQMNP LGNWDSSLPK AAINSLMQSK LFQAVLPNGE DCLTINVVRP
     SGTKPGANLP VMVWIFGGGF EVGGSSLFPP AQMITASVLM GKPIIHVSMN YRVASWGFLA
     GPDIKAEGSG NAGLHDQRLG LQWVADNIAG FGGDPSKVTI FGESAGSMSV MCQLLWNDGD
     NTYNGKPLFR AAIMQSGAMV PSDPVDGPYG TQIYDQVVAS AGCGSASDKL ACLRSISNDK
     LFQATSDTPG ALAYPSLRLS FLPRPDGTFI TDDMFKLVRD GKCANVPVII GDQNDEGTVF
     ALSSLNVTTD AQARQYFKES FIHASDAEID TLMAAYPSDI TQGSPFDTGI FNAITPQFKR
     IAAVLGDLAF TLPRRYFLNH FQGGTKYSFL SKQLSGLPVI GTHHANDIVW QDFLVSHSSA
     VYNNAFIAFA NDLDPNKAGL LVNWPKYTSS SQSGNNLLQI NALGLYTGKD NFRTAGYDAL
     FTNPSSFFV
//