P79143 · AMPN_CANLF

Function

function

Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (By similarity).
(Microbial infection) Probable receptor for canine coronavirus (CCoV).

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 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site, site.

TypeIDPosition(s)Description
Binding site358-362substrate
Binding site394Zn2+ (UniProtKB | ChEBI); catalytic
Active site395Proton acceptor
Binding site398Zn2+ (UniProtKB | ChEBI); catalytic
Binding site417Zn2+ (UniProtKB | ChEBI); catalytic
Site483Transition state stabilizer

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentextracellular space
Cellular Componentplasma membrane
Molecular Functionmetalloaminopeptidase activity
Molecular Functionpeptide binding
Molecular Functionvirus receptor activity
Molecular Functionzinc ion binding
Biological Processangiogenesis
Biological Processcell differentiation
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
  • Short names
    AP-N; cAPN
  • Alternative names
    • Alanyl aminopeptidase
    • Aminopeptidase M (AP-M)
    • Microsomal aminopeptidase
  • CD Antigen Name
    • CD13

Gene names

    • Name
      ANPEP

Organism names

Accessions

  • Primary accession
    P79143
  • Secondary accessions
    • F1PCB5

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type II membrane protein
Note: Also found as a soluble form.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-11Cytoplasmic
Transmembrane12-32Helical; Signal-anchor for type II membrane protein
Topological domain33-975Extracellular

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, modified residue, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00000950791-975Aminopeptidase N
Glycosylation134N-linked (GlcNAc...) asparagine
Modified residue182Sulfotyrosine
Glycosylation240N-linked (GlcNAc...) asparagine
Glycosylation271N-linked (GlcNAc...) asparagine
Modified residue425Sulfotyrosine
Modified residue430Sulfotyrosine
Glycosylation533N-linked (GlcNAc...) asparagine
Glycosylation580N-linked (GlcNAc...) asparagine
Glycosylation633N-linked (GlcNAc...) asparagine
Glycosylation689N-linked (GlcNAc...) asparagine
Glycosylation747N-linked (GlcNAc...) asparagine
Disulfide bond769↔776
Disulfide bond806↔842
Glycosylation826N-linked (GlcNAc...) asparagine

Post-translational modification

Sulfated.
N- and O-glycosylated.
May undergo proteolysis and give rise to a soluble form.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

(Microbial infection) Interacts with CCoV spike glycoprotein.
Homodimer. Interacts with SLC6A19 (By similarity).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region33-74Cytosolic Ser/Thr-rich junction
Region41-68Disordered
Region75-975Metalloprotease

Domain

Amino acids 1-191 are essential to mediate susceptibility to infection with CCV (in canine/human chimeric studies).

Sequence similarities

Belongs to the peptidase M1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    975
  • Mass (Da)
    110,257
  • Last updated
    2017-03-15 v2
  • Checksum
    921D2446A2F84725
MAKGFYISKALGILAIVLGIAAVSTIIALSVVYAQEKNKNAESSPVSSPVSSPVSSPVSPTNPSTTAATTLAQSKPWNHYRLPKTLIPSSYNVTLRPYLTPNSNGLYTFKGSSTVRFTCKESTSMIIIHSKKLNYTNIQGQRVALRGVGGSQAPAIDRTELVEVTEYLVVHLREPLQVNSQYEMDSKFEGELADDLAGFYRSEYTENGVKKVLATTQMQAADARKSFPCFDEPAMKATFNITLIHPSNLVALSNMLPRGPSVPFTEEPNWNVTEFETTPIMSTYLLAYIVSEFKNVQENTPSNVLIRIWARPSAMDQGHGNYALRVTGPILDFFSRHYDTPYPLNKSDQIALPDFNAGAMENWGLVTYRESALLYDPQSSSIGNKERVVTVIAHELAHQWFGNLVTLEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLIVLNEVYRVMAVDALASSHPLSSPASEVNTPAQISEVFDSISYSKGASVLRMLSSFLTEDLFKKGVASYLHTFAYQNTIYLDLWNHLQWALGNQTAINLPYTVNAIMDRWILQMGFPVVTVDTTTGTLSQKHFLLDPQSNVTRPSKFNYLWIIPISSVKSGTQQAHYWMPDNAKVQNDLFKTTGDEWVLLNLNVTGYYLVNYDQNNWKKIHTQLQTDLSVIPVINRAQVIHDTFDLASAQIVPVTLALNSTLFLNQETEYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLRKQVTPLFNHFEKITQNWTDHPQTLTEQYNEINAVSTACTYGVPKCKDLVSTLFAEWRKNPQNNPIYPNLRSTVYCNAIAQGGEEEWNFVWEQFRNTSLVNEADKLRSALACSTQVWILNRYLSYTLNPEFIRKQDVISTLSSIASNVIGQSLAWDFIQSNWKKLFEDYGTGSFSFSNLIQAVTRRFSTEFELQQLEQFKANNMDTGFGSGTRALEQALEKTKANIKWVKENKEAVLQWFRENSQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAEX03002325
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
X98239
EMBL· GenBank· DDBJ
CAA66895.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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