P79143 · AMPN_CANLF
- ProteinAminopeptidase N
- GeneANPEP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids975 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 358-362 | substrate | ||||
Sequence: GAMEN | ||||||
Binding site | 394 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 395 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 398 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 417 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 483 | Transition state stabilizer | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular space | |
Cellular Component | plasma membrane | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | virus receptor activity | |
Molecular Function | zinc ion binding | |
Biological Process | angiogenesis | |
Biological Process | cell differentiation | |
Biological Process | peptide catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAminopeptidase N
- EC number
- Short namesAP-N; cAPN
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionP79143
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Note: Also found as a soluble form.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-11 | Cytoplasmic | ||||
Sequence: MAKGFYISKAL | ||||||
Transmembrane | 12-32 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: GILAIVLGIAAVSTIIALSVV | ||||||
Topological domain | 33-975 | Extracellular | ||||
Sequence: YAQEKNKNAESSPVSSPVSSPVSSPVSPTNPSTTAATTLAQSKPWNHYRLPKTLIPSSYNVTLRPYLTPNSNGLYTFKGSSTVRFTCKESTSMIIIHSKKLNYTNIQGQRVALRGVGGSQAPAIDRTELVEVTEYLVVHLREPLQVNSQYEMDSKFEGELADDLAGFYRSEYTENGVKKVLATTQMQAADARKSFPCFDEPAMKATFNITLIHPSNLVALSNMLPRGPSVPFTEEPNWNVTEFETTPIMSTYLLAYIVSEFKNVQENTPSNVLIRIWARPSAMDQGHGNYALRVTGPILDFFSRHYDTPYPLNKSDQIALPDFNAGAMENWGLVTYRESALLYDPQSSSIGNKERVVTVIAHELAHQWFGNLVTLEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLIVLNEVYRVMAVDALASSHPLSSPASEVNTPAQISEVFDSISYSKGASVLRMLSSFLTEDLFKKGVASYLHTFAYQNTIYLDLWNHLQWALGNQTAINLPYTVNAIMDRWILQMGFPVVTVDTTTGTLSQKHFLLDPQSNVTRPSKFNYLWIIPISSVKSGTQQAHYWMPDNAKVQNDLFKTTGDEWVLLNLNVTGYYLVNYDQNNWKKIHTQLQTDLSVIPVINRAQVIHDTFDLASAQIVPVTLALNSTLFLNQETEYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLRKQVTPLFNHFEKITQNWTDHPQTLTEQYNEINAVSTACTYGVPKCKDLVSTLFAEWRKNPQNNPIYPNLRSTVYCNAIAQGGEEEWNFVWEQFRNTSLVNEADKLRSALACSTQVWILNRYLSYTLNPEFIRKQDVISTLSSIASNVIGQSLAWDFIQSNWKKLFEDYGTGSFSFSNLIQAVTRRFSTEFELQQLEQFKANNMDTGFGSGTRALEQALEKTKANIKWVKENKEAVLQWFRENSQ |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000095079 | 1-975 | Aminopeptidase N | |||
Sequence: MAKGFYISKALGILAIVLGIAAVSTIIALSVVYAQEKNKNAESSPVSSPVSSPVSSPVSPTNPSTTAATTLAQSKPWNHYRLPKTLIPSSYNVTLRPYLTPNSNGLYTFKGSSTVRFTCKESTSMIIIHSKKLNYTNIQGQRVALRGVGGSQAPAIDRTELVEVTEYLVVHLREPLQVNSQYEMDSKFEGELADDLAGFYRSEYTENGVKKVLATTQMQAADARKSFPCFDEPAMKATFNITLIHPSNLVALSNMLPRGPSVPFTEEPNWNVTEFETTPIMSTYLLAYIVSEFKNVQENTPSNVLIRIWARPSAMDQGHGNYALRVTGPILDFFSRHYDTPYPLNKSDQIALPDFNAGAMENWGLVTYRESALLYDPQSSSIGNKERVVTVIAHELAHQWFGNLVTLEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLIVLNEVYRVMAVDALASSHPLSSPASEVNTPAQISEVFDSISYSKGASVLRMLSSFLTEDLFKKGVASYLHTFAYQNTIYLDLWNHLQWALGNQTAINLPYTVNAIMDRWILQMGFPVVTVDTTTGTLSQKHFLLDPQSNVTRPSKFNYLWIIPISSVKSGTQQAHYWMPDNAKVQNDLFKTTGDEWVLLNLNVTGYYLVNYDQNNWKKIHTQLQTDLSVIPVINRAQVIHDTFDLASAQIVPVTLALNSTLFLNQETEYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLRKQVTPLFNHFEKITQNWTDHPQTLTEQYNEINAVSTACTYGVPKCKDLVSTLFAEWRKNPQNNPIYPNLRSTVYCNAIAQGGEEEWNFVWEQFRNTSLVNEADKLRSALACSTQVWILNRYLSYTLNPEFIRKQDVISTLSSIASNVIGQSLAWDFIQSNWKKLFEDYGTGSFSFSNLIQAVTRRFSTEFELQQLEQFKANNMDTGFGSGTRALEQALEKTKANIKWVKENKEAVLQWFRENSQ | ||||||
Glycosylation | 134 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 182 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 240 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 271 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 425 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 430 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 533 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 580 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 633 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 689 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 747 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 769↔776 | |||||
Sequence: CTYGVPKC | ||||||
Disulfide bond | 806↔842 | |||||
Sequence: CNAIAQGGEEEWNFVWEQFRNTSLVNEADKLRSALAC | ||||||
Glycosylation | 826 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Sulfated.
N- and O-glycosylated.
May undergo proteolysis and give rise to a soluble form.
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 33-74 | Cytosolic Ser/Thr-rich junction | ||||
Sequence: YAQEKNKNAESSPVSSPVSSPVSSPVSPTNPSTTAATTLAQS | ||||||
Region | 41-68 | Disordered | ||||
Sequence: AESSPVSSPVSSPVSSPVSPTNPSTTAA | ||||||
Region | 75-975 | Metalloprotease | ||||
Sequence: KPWNHYRLPKTLIPSSYNVTLRPYLTPNSNGLYTFKGSSTVRFTCKESTSMIIIHSKKLNYTNIQGQRVALRGVGGSQAPAIDRTELVEVTEYLVVHLREPLQVNSQYEMDSKFEGELADDLAGFYRSEYTENGVKKVLATTQMQAADARKSFPCFDEPAMKATFNITLIHPSNLVALSNMLPRGPSVPFTEEPNWNVTEFETTPIMSTYLLAYIVSEFKNVQENTPSNVLIRIWARPSAMDQGHGNYALRVTGPILDFFSRHYDTPYPLNKSDQIALPDFNAGAMENWGLVTYRESALLYDPQSSSIGNKERVVTVIAHELAHQWFGNLVTLEWWNDLWLNEGFASYVEYLGADYAEPTWNLKDLIVLNEVYRVMAVDALASSHPLSSPASEVNTPAQISEVFDSISYSKGASVLRMLSSFLTEDLFKKGVASYLHTFAYQNTIYLDLWNHLQWALGNQTAINLPYTVNAIMDRWILQMGFPVVTVDTTTGTLSQKHFLLDPQSNVTRPSKFNYLWIIPISSVKSGTQQAHYWMPDNAKVQNDLFKTTGDEWVLLNLNVTGYYLVNYDQNNWKKIHTQLQTDLSVIPVINRAQVIHDTFDLASAQIVPVTLALNSTLFLNQETEYMPWEAALSSLSYFKLMFDRSEVYGPMKNYLRKQVTPLFNHFEKITQNWTDHPQTLTEQYNEINAVSTACTYGVPKCKDLVSTLFAEWRKNPQNNPIYPNLRSTVYCNAIAQGGEEEWNFVWEQFRNTSLVNEADKLRSALACSTQVWILNRYLSYTLNPEFIRKQDVISTLSSIASNVIGQSLAWDFIQSNWKKLFEDYGTGSFSFSNLIQAVTRRFSTEFELQQLEQFKANNMDTGFGSGTRALEQALEKTKANIKWVKENKEAVLQWFRENSQ |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length975
- Mass (Da)110,257
- Last updated2017-03-15 v2
- Checksum921D2446A2F84725
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAEX03002325 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
X98239 EMBL· GenBank· DDBJ | CAA66895.1 EMBL· GenBank· DDBJ | mRNA |