ID   MDLA_PENCA              Reviewed;         305 AA.
AC   P61870; P25234;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Mono- and diacylglycerol lipase;
DE            Short=MDGL;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=mdlA;
OS   Penicillium camembertii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-60 AND
RP   261-296.
RC   STRAIN=U-150;
RX   PubMed=1879699; DOI=10.1016/0378-1119(91)90391-n;
RA   Yamaguchi S., Mase T., Takeuchi K.;
RT   "Cloning and structure of the mono- and diacylglycerol lipase-encoding gene
RT   from Penicillium camembertii U-150.";
RL   Gene 103:61-67(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-302, AND DISULFIDE BONDS.
RC   STRAIN=U-150;
RX   PubMed=8458423; DOI=10.1016/0014-5793(93)80071-2;
RA   Isobe K., Nokihara K.;
RT   "Primary structure determination of mono- and diacylglycerol lipase from
RT   Penicillium camembertii.";
RL   FEBS Lett. 320:101-106(1993).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=7656005; DOI=10.1038/nsb0194-36;
RA   Derewenda U., Swenson L., Green R., Wei Y., Dodson G.G., Yamaguchi S.,
RA   Haas M.J., Derewenda Z.S.;
RT   "An unusual buried polar cluster in a family of fungal lipases.";
RL   Nat. Struct. Biol. 1:36-47(1994).
CC   -!- FUNCTION: Hydrolyzes mono- and diacylglycerol but not triacylglycerol.
CC   -!- PTM: Multiple forms of this lipase are due to the presence of different
CC       carbohydrates, which may contribute to the stability of this lipase but
CC       not to the enzyme activity.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; D90315; BAA14345.1; -; Genomic_DNA.
DR   PIR; JQ1188; JQ1188.
DR   PDB; 1TIA; X-ray; 2.10 A; A=27-305.
DR   PDBsum; 1TIA; -.
DR   AlphaFoldDB; P61870; -.
DR   SMR; P61870; -.
DR   ESTHER; penca-mdgli; Lipase_3.
DR   EvolutionaryTrace; P61870; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR002921; Fungal_lipase-like.
DR   InterPro; IPR005592; Mono/diacylglycerol_lipase_N.
DR   Pfam; PF03893; Lipase3_N; 1.
DR   Pfam; PF01764; Lipase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Signal; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:1879699,
FT                   ECO:0000269|PubMed:8458423"
FT   CHAIN           27..302
FT                   /note="Mono- and diacylglycerol lipase"
FT                   /id="PRO_0000017760"
FT   PROPEP          303..305
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000017761"
FT   ACT_SITE        171
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:7656005"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:7656005"
FT   ACT_SITE        285
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000305|PubMed:7656005"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        62..67
FT                   /evidence="ECO:0000269|PubMed:8458423"
FT   DISULFID        129..132
FT                   /evidence="ECO:0000269|PubMed:8458423"
FT   CONFLICT        89
FT                   /note="T -> V (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   305 AA;  32948 MW;  42C2A16203DBA1AA CRC64;
     MRLSFFTALS AVASLGYALP GKLQSRDVST SELDQFEFWV QYAAASYYEA DYTAQVGDKL
     SCSKGNCPEV EATGATVSYD FSDSTITDTA GYIAVDHTNS AVVLAFRGSY SVRNWVADAT
     FVHTNPGLCD GCLAELGFWS SWKLVRDDII KELKEVVAQN PNYELVVVGH SLGAAVATLA
     ATDLRGKGYP SAKLYAYASP RVGNAALAKY ITAQGNNFRF THTNDPVPKL PLLSMGYVHV
     SPEYWITSPN NATVSTSDIK VIDGDVSFDG NTGTGLPLLT DFEAHIWYFV QVDAGKGPGL
     PFKRV