C1AYU0 · C1AYU0_RHOOB

Function

Catalytic activity

  • Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
    EC:3.4.11.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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 Componentcytoplasm
Molecular Functionmetalloaminopeptidase activity
Molecular Functionpeptide binding
Molecular Functionzinc ion binding
Biological Processpeptide catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Aminopeptidase N
  • EC number
  • Alternative names
    • Alanine aminopeptidase
    • Lysyl aminopeptidase

Gene names

    • Name
      pepN
    • Ordered locus names
      ROP_16210

Organism names

Accessions

  • Primary accession
    C1AYU0

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain97-189Aminopeptidase N-like N-terminal
Domain231-444Peptidase M1 membrane alanine aminopeptidase
Domain512-820ERAP1-like C-terminal

Sequence similarities

Belongs to the peptidase M1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    835
  • Mass (Da)
    91,689
  • Last updated
    2009-05-26 v1
  • Checksum
    7AA1423D03444832
MSTANLTRAETAERSRAIEVLGYRVELDVLGAIDPDVGTFATTTTVEFTARTSTTWLDFLGAGVDSVTVNGAGVPVDYDGARIALAGLRESNVVTVTARGEYSRSGEGLHRFLDPADGRTYLYTQYEPADARRVFACFEQPDLKAPFTFVVTAPQEWEVISNQQVAERDDTAGGQVVTFAPTLPISTYITAVVAGPYHRVDAEWSGGDLTIPLGVLCRASLAQYLDADTIFEITRQGLGFFAEGFDYPYPFGKYDQVFVPEYNLGAMENPGCVTFTEAYVFRGAATDSQYEGRANTILHEMAHMWFGDLVTMVWWDDLWLKESFADYMGALANAEATRWTDAWVAFANRRKAWAYLQDQLPTTHPIVADIVDLEAAKLNFDGITYAKGASVLKQLVAYAGREAFFEGARRYFRAHAFGNTTLTDLLTELSATSGRDLTSWARAWLQTTGVSALSLERDADGRAAIVQTDPRPHRLGVGRFDFDGAGDLVCVQRIEVDLADPSTPIDLGDAPLVVLNDADLTYAKVRLDDRSLSTTEQSLDRVRDPLARGLIWSSLWNTTRDSELGAQRYLSMAQRFSPAESHLTLLSSVLANAPYAIEHYLPEPSRVAARREWLDHTWRALWDAPPASGSQLAWARAVAAAAEVDDSRAVNIRSLLDTDGQAPTGLSLDPDLRWAFRGALAATGHADDADLDGELRRDDTGSGRTAYLRATFSRPEPDVKAKAWESIFHDHTLSNDHLGAIIAGFRAGARHDLVAGFAAEYFASIRSVWESRSIEIARRIVVGLFPSETNLDAADGWLAGHTDAPAALRRLVVEQRDHLARDLRAQAFNSPDVTG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP011115
EMBL· GenBank· DDBJ
BAH49868.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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