Q5QHG5 · LAP1_TRIRU

Function

function

Extracellular aminopeptidase which contributes to pathogenicity.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

137350100150200250300350
TypeIDPosition(s)Description
Binding site176Zn2+ 1 (UniProtKB | ChEBI)
Binding site195Zn2+ 1 (UniProtKB | ChEBI)
Binding site195Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site234Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site261Zn2+ 1 (UniProtKB | ChEBI)
Binding site343Zn2+ 2 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionaminopeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetalloexopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Leucine aminopeptidase 1
  • EC number
  • Alternative names
    • Leucyl aminopeptidase 1 (LAP1)

Gene names

    • Name
      LAP1

Organism names

Accessions

  • Primary accession
    Q5QHG5

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

Type
IDPosition(s)Description
Signal1-18
ChainPRO_000038410019-373Leucine aminopeptidase 1
Glycosylation196N-linked (GlcNAc...) asparagine
Glycosylation288N-linked (GlcNAc...) asparagine
Disulfide bond310↔314
Glycosylation348N-linked (GlcNAc...) asparagine

Keywords

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    373
  • Mass (Da)
    40,635
  • Last updated
    2005-01-04 v1
  • Checksum
    7754DE880535DF81
MKLLSVLALSATATSVLGASIPVDARAEKFLIELAPGETRWVTEEEKWELKRKGQDFFDITDEEVGFTAAVAQPAIAYPTSIRHANAVNAMIATLSKENMQRDLTKLSSFQTAYYKVDFGKQSATWLQEQVQAAINTAGANRYGAKVASFRHNFAQHSIIATIPGRSPEVVVVGAHQDSINQRSPMTGRAPGADDNGSGSVTILEALRGVLRDQTILQGKAANTIEFHWYAGEEAGLLGSQAIFANYKQTGKKVKGMLNQDMTGYIKGMVDKGLKVSFGIITDNVNANLTKFVRMVITKYCSIPTIDTRCGYACSDHASANRNGYPSAMVAESPIDLLDPHLHTDSDNISYLDFDHMIEHAKLIVGFVTELAK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY496930
EMBL· GenBank· DDBJ
AAS76670.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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