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Protein

Mono- and diacylglycerol lipase

Gene

mdlA

Organism
Penicillium camembertii
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes mono- and diacylglycerol but not triacylglycerol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei171 – 1711Nucleophile1 Publication
Active sitei225 – 2251Charge relay system1 Publication
Active sitei285 – 2851Charge relay system1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Protein family/group databases

ESTHERipenca-mdgli. Lipase_3.

Names & Taxonomyi

Protein namesi
Recommended name:
Mono- and diacylglycerol lipase (EC:3.1.1.-)
Short name:
MDGL
Gene namesi
Name:mdlA
OrganismiPenicillium camembertii
Taxonomic identifieri5075 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26262 PublicationsAdd
BLAST
Chaini27 – 302276Mono- and diacylglycerol lipasePRO_0000017760Add
BLAST
Propeptidei303 – 3053Removed in mature formPRO_0000017761

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 ↔ 671 Publication
Disulfide bondi129 ↔ 1321 Publication
Glycosylationi251 – 2511N-linked (GlcNAc...)

Post-translational modificationi

Multiple forms of this lipase are due to the presence of different carbohydrates, which may contribute to the stability of this lipase but not to the enzyme activity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIAX-ray2.10A27-305[»]
ProteinModelPortaliP61870.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61870.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamiPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61870-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSFFTALS AVASLGYALP GKLQSRDVST SELDQFEFWV QYAAASYYEA
60 70 80 90 100
DYTAQVGDKL SCSKGNCPEV EATGATVSYD FSDSTITDTA GYIAVDHTNS
110 120 130 140 150
AVVLAFRGSY SVRNWVADAT FVHTNPGLCD GCLAELGFWS SWKLVRDDII
160 170 180 190 200
KELKEVVAQN PNYELVVVGH SLGAAVATLA ATDLRGKGYP SAKLYAYASP
210 220 230 240 250
RVGNAALAKY ITAQGNNFRF THTNDPVPKL PLLSMGYVHV SPEYWITSPN
260 270 280 290 300
NATVSTSDIK VIDGDVSFDG NTGTGLPLLT DFEAHIWYFV QVDAGKGPGL

PFKRV
Length:305
Mass (Da):32,948
Last modified:June 7, 2004 - v1
Checksum:i42C2A16203DBA1AA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891T → V AA sequence (PubMed:8458423).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90315 Genomic DNA. Translation: BAA14345.1.
PIRiJQ1188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90315 Genomic DNA. Translation: BAA14345.1.
PIRiJQ1188.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TIAX-ray2.10A27-305[»]
ProteinModelPortaliP61870.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERipenca-mdgli. Lipase_3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP61870.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002921. Fungal_lipase-like.
IPR005592. Mono/diacylglycerol_lipase_N.
[Graphical view]
PfamiPF03893. Lipase3_N. 1 hit.
PF01764. Lipase_3. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDLA_PENCA
AccessioniPrimary (citable) accession number: P61870
Secondary accession number(s): P25234
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 13, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.