O09175 · AMPB_RAT

Function

function

Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg0-Leu-enkephalin, Arg0-Met-enkephalin and Arg-1-Lys0-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4).

Catalytic activity

  • Release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys.
    EC:3.4.11.6 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site, site.

165050100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site298-302substrate
Binding site325Zn2+ (UniProtKB | ChEBI); catalytic
Active site326Proton acceptor
Binding site329Zn2+ (UniProtKB | ChEBI); catalytic
Binding site348Zn2+ (UniProtKB | ChEBI); catalytic
Site414Transition state stabilizer

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 Componentexternal side of plasma membrane
Cellular Componentextracellular region
Cellular Componentextracellular space
Cellular ComponentGolgi apparatus
Cellular Componentplasma membrane
Cellular Componentsecretory granule
Molecular Functionaminopeptidase activity
Molecular Functioncobalt ion binding
Molecular Functioncopper ion binding
Molecular Functionmetalloaminopeptidase activity
Molecular Functionpeptide binding
Molecular Functionzinc ion binding
Biological Processnegative regulation of blood pressure
Biological Processprotein processing
Biological Processproteolysis
Biological Processretina development in camera-type eye

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Aminopeptidase B
  • EC number
  • Short names
    AP-B
  • Alternative names
    • Arginine aminopeptidase
    • Arginyl aminopeptidase
    • Cytosol aminopeptidase IV

Gene names

    • Name
      Rnpep

Organism names

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

Accessions

  • Primary accession
    O09175
  • Secondary accessions
    • P97530

Proteomes

Organism-specific databases

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000950901-650Aminopeptidase B
Modified residue7Phosphoserine
Modified residue446N6-acetyllysine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed.

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Sequence similarities

Belongs to the peptidase M1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    650
  • Mass (Da)
    72,620
  • Last updated
    2002-07-11 v2
  • Checksum
    032BE2F4F50B58E0
MESSGPSSCHSAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLNGKATLELRCLLPEGASELRLDSHSCLEVMAATLLRGQPGDQQQLTEPVPFHTQPFSHYGQALCVVFPKPCCAAERFRLELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALVEVPDGFTAVMSASTWERRGPNKFFFQMSQPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYNGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMDVSGEENPLNKLRVKIEPGVDPDDTYNETPYEKGYCFVSYLAHLVGDQEQFDKFLKAYVDEFKFQSILAEDFLEFYLEYFPELKKKGVDSIPGFEFNRWLNTPGWPPYLPDLSPGDSLMKPAEELAELWAASEPDMQAIEAVAISTWKTYQLVYFLDKILQKSPLPPGNVKKLGETYPKISNAQNAELRLRWGQIILKNDHQEEFWKVKDFLQSQGKQKYTLPLYHAMMGGSEMARTLAKETFSATASQLHSNVVNYVQQILAPKGS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6GJU0A0A8I6GJU0_RATRnpep611
G3V6V1G3V6V1_RATRnpep650

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict47-48in Ref. 1; AAB52971
Sequence conflict74in Ref. 2; BAA13413
Sequence conflict250-251in Ref. 1; AAB52971
Sequence conflict627in Ref. 2; BAA13413

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U61696
EMBL· GenBank· DDBJ
AAB52971.1
EMBL· GenBank· DDBJ
mRNA
D87515
EMBL· GenBank· DDBJ
BAA13413.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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