A1C948 · LAP1_ASPCL

Function

function

Extracellular aminopeptidase that allows assimilation of proteinaceous substrates.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site.

138850100150200250300350
TypeIDPosition(s)Description
Binding site188Zn2+ 1 (UniProtKB | ChEBI)
Binding site207Zn2+ 1 (UniProtKB | ChEBI)
Binding site207Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site246Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site273Zn2+ 1 (UniProtKB | ChEBI)
Binding site355Zn2+ 2 (UniProtKB | ChEBI); catalytic

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
    • ORF names
      ACLA_054190

Organism names

Accessions

  • Primary accession
    A1C948

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-19
PropeptidePRO_000041238820-88
ChainPRO_000041238989-388Leucine aminopeptidase 1
Glycosylation106N-linked (GlcNAc...) asparagine
Glycosylation180N-linked (GlcNAc...) asparagine
Glycosylation232N-linked (GlcNAc...) asparagine
Disulfide bond322↔326

Keywords

PTM databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase M28 family. M28E subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    388
  • Mass (Da)
    42,675
  • Last updated
    2007-01-23 v1
  • Checksum
    A9D8C684FAE1C66D
MRVLAAIALGATGLRGALAAVVPQEVLGTNPHIHHEQEKYLIELAPYQTRWVTEEEKWALKLDGVNFIDITEEHNTGFYPTLNSASYVKYPLKMQYADEVVALNKNLSTANMKANLEHFTSFHTRYYKSQTGIESATWLASQVEKVITESGAANHGATVERFAHPWGQFSIIARIPGQTNKTVVLGAHQDSINLFLPSILAAPGADDDGSGTVTILEALRGLLQSGSVAQGNATNTIEFHWYSAEEGGMLGSQAVFSSYKKNRREVKAMLQQDMTGYTKGALDAGAKEAVGIMIDYVDQGLTRFVKEIVTTYCSLGYVETKCGYACSDHTSASKYGYPAAMATESEMENTNRKIHTTDDQIKYLSFDHMLEHAKLTLGFAYELAFAPF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS027048
EMBL· GenBank· DDBJ
EAW13372.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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