Q5QHG5 · LAP1_TRIRU
- ProteinLeucine aminopeptidase 1
- GeneLAP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids373 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Extracellular aminopeptidase which contributes to pathogenicity.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Activity regulation
Activity is inhibited by EDTA, o-phenanthroline, bestatin and amastatin.
pH Dependence
Optimum pH is 7.0.
Temperature Dependence
Optimum temperatures are ranging from 40 to 50 degrees Celsius.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 176 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 195 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 195 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 234 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
Binding site | 261 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 343 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | aminopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metalloexopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLeucine aminopeptidase 1
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Trichophyton
Accessions
- Primary accessionQ5QHG5
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-18 | ||||
Chain | PRO_0000384100 | 19-373 | Leucine aminopeptidase 1 | ||
Glycosylation | 196 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 288 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 310↔314 | ||||
Glycosylation | 348 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Expression
Induction
Expression is strongly increased during growth on protein-rich medium. Expressed at even higher levels when keratin is present in the protein-rich medium.
Interaction
Subunit
Monomer.
Structure
Family & Domains
Sequence similarities
Belongs to the peptidase M28 family. M28E subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length373
- Mass (Da)40,635
- Last updated2005-01-04 v1
- Checksum7754DE880535DF81
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY496930 EMBL· GenBank· DDBJ | AAS76670.1 EMBL· GenBank· DDBJ | Genomic DNA |