Q68FS4 · AMPL_RAT

  • Protein
    Cytosol aminopeptidase
  • Gene
    Lap3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides (PubMed:12675513, PubMed:6108111).
The presence of Zn2+ ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme (By similarity).
For instance, in the presence of Mn2+, it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates (By similarity).
Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status (PubMed:12675513).

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds two metal ions per subunit. Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals: site 1 is occupied by Zn2+, Mn2+, Mg2+ or Co2+, while the tight binding site 2 can be occupied by only Zn2+ or Co2+. One Zn2+ ion is tightly bound to site 2 and essential for enzyme activity in vivo, while site 1 can be occupied by different metals to give different enzymatic activities. Mn2+ is required for Cys-Gly hydrolysis activity. A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain.

Activity regulation

Bimane-S-cysteinylglycine-hydrolyzing activity is inhibited by o-phenanthroline or bestatin, and is activated by the addition of zinc chloride.

Kinetics

Vmax pH TEMPERATURE[C] NOTES EVIDENCE
1.6 μmol/min/mgfor peptidase activity with S-benzyl-cysteine-p-nitroanilide
11.9 μmol/min/mgfor peptidase activity with Leucine-p-nitroanilide
9.4 μmol/min/mgfor peptidase activity with Alanine-p-nitroanilide

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site202Zn2+ 3 (UniProtKB | ChEBI); structural
Binding site203Zn2+ 3 (UniProtKB | ChEBI); structural
Binding site282substrate
Binding site282Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site287Mg2+ (UniProtKB | ChEBI); catalytic
Binding site287substrate
Binding site287Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site287Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site292substrate
Active site294
Binding site294substrate
Binding site303Zn2+ 3 (UniProtKB | ChEBI); structural
Binding site305substrate
Binding site305Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site364Mg2+ (UniProtKB | ChEBI); catalytic
Binding site364substrate
Binding site364Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site366Mg2+ (UniProtKB | ChEBI); catalytic
Binding site366Zn2+ 1 (UniProtKB | ChEBI); catalytic
Binding site366Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site368

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componenttrans-Golgi network
Molecular Functioncarboxypeptidase activity
Molecular Functionmanganese ion binding
Molecular Functionmetalloaminopeptidase activity
Molecular Functionpeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytosol aminopeptidase
  • EC number
  • Alternative names
    • Cysteinylglycine-S-conjugate dipeptidase
      (EC:3.4.13.23
      ) . EC:3.4.13.23 (UniProtKB | ENZYME | Rhea)
    • Leucine aminopeptidase 3
      (LAP-3)
    • Leucyl aminopeptidase
      (LAP
      )
    • Peptidase S
    • Proline aminopeptidase
      (EC:3.4.11.5
      ) . EC:3.4.11.5 (UniProtKB | ENZYME | Rhea)
    • Prolyl aminopeptidase

Gene names

    • Name
      Lap3

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q68FS4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002741461-519Cytosol aminopeptidase
Modified residue42Phosphoserine
Modified residue45N6-succinyllysine
Modified residue54Phosphoserine
Modified residue61N6-succinyllysine
Modified residue103N6-succinyllysine
Modified residue180Phosphoserine
Modified residue194Phosphoserine
Modified residue221N6-acetyllysine; alternate
Modified residue221N6-succinyllysine; alternate
Modified residue238Phosphoserine
Modified residue455N6-acetyllysine; alternate
Modified residue455N6-succinyllysine; alternate
Modified residue476N6-succinyllysine
Modified residue489N6-acetyllysine; alternate
Modified residue489N6-succinyllysine; alternate

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homohexamer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase M17 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative initiation.

Q68FS4-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    519
  • Mass (Da)
    56,150
  • Last updated
    2004-10-11 v1
  • Checksum
    0D4DFDC93D0CFF9D
MYLLPLPAAARVALRRLGVRGLWDRGLSTADMTKGLVLGIYSKDKDDDVPQFTSAGENFNKLVSGRLREMLNISGPPLKAGKTRTFYGLHQDFPSVVVVGLGKRSAGVDDQENWHEGKENIRAAVAAGCRQVQDLELPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKVAVSAKLHGSGDLEAWEKGVLFASGQNLARQLMESPANEMTPTRFAEVIEKNLKSASSKTEVHIRTKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYTGSPNATEAPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASVETGDRVWRMPLFEHYTRQVIDCQLADVNNLGKYRSAGACTAAAFLREFVTHTKWAHLDIAGVMTNKDEIPYLRKGMSGRPTRTLIEFLLRFSKDSS

Q68FS4-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6AG50A0A8I6AG50_RATLap3500

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0226331-31in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC079381
EMBL· GenBank· DDBJ
AAH79381.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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