位置:首页 > 蛋白库 > MDLA_PENCY
MDLA_PENCY
ID   MDLA_PENCY              Reviewed;         305 AA.
AC   P61869; P25234;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Mono- and diacylglycerol lipase;
DE            Short=MDGL;
DE            EC=3.1.1.-;
DE   Flags: Precursor;
GN   Name=mdlA;
OS   Penicillium cyclopium.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PG37;
RA   Wu M.C., Li J.H., Qian Z.K., Min T.S., Sun C.R., Huang W.D.;
RT   "Cloning and structure of the mono- and diacylglycerol lipase-encoding gene
RT   from Penicillium cyclopium PG37.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF288219; AAF99710.1; -; Genomic_DNA.
DR   PIR; JQ1188; JQ1188.
DR   PDB; 5CH8; X-ray; 1.62 A; A=27-305.
DR   PDBsum; 5CH8; -.
DR   AlphaFoldDB; P61869; -.
DR   SMR; P61869; -.
DR   ESTHER; penca-mdgli; Lipase_3.
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; Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Signal; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..302
FT                   /note="Mono- and diacylglycerol lipase"
FT                   /id="PRO_0000017762"
FT   PROPEP          303..305
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000017763"
FT   ACT_SITE        171
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P61870"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P61870"
FT   ACT_SITE        285
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P61870"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        62..67
FT                   /evidence="ECO:0000250|UniProtKB:P61870"
FT   DISULFID        129..132
FT                   /evidence="ECO:0000250|UniProtKB:P61870"
FT   HELIX           30..45
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           49..52
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           68..72
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   TURN            97..100
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          101..107
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           112..118
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           136..159
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          164..170
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           172..185
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           205..214
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          217..222
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          243..246
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           256..258
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           270..274
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   HELIX           279..285
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:5CH8"
FT   TURN            292..295
FT                   /evidence="ECO:0007829|PDB:5CH8"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024