Reviewed, UniProtKB/Swiss-Prot P79143 (AMPN_CANFA)

Names and origin

Protein names

Recommended name:
    Aminopeptidase N
      Short name=AP-N
      Short name=cAPN
    EC=3.4.11.2
Alternative name(s):
    Alanyl aminopeptidase
    Microsomal aminopeptidase
    Aminopeptidase M
      Short name=AP-M
    CD_antigen=CD13

Gene names

Name:

ANPEP

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	191 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types and in the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis By similarity. In case of canine coronavirus (CCoV), serves as a receptor for CCoV spike glycoprotein in a species-specific manner.
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	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Homodimer By similarity. Interacts with CCoV spike glycoprotein.
Subcellular location	Membrane; Single-pass type II membrane protein.
Domain	Amino acids 1-191 are essential to mediate susceptibility to infection with CCV (in canine/human chimeric studies). This region can confer susceptibility to infection with TGEV and FIPV (strain 79-1146) when substituted in corresponding human ANPEP region. Ref.1
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation Host-virus interaction
Cellular component	Membrane
Ligand	Zinc
Molecular function	Aminopeptidase Developmental protein Hydrolase Metalloprotease Protease
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›191	›191	Aminopeptidase N		PRO_0000095079
Regions
	Region	‹1 – ›191	›191	Metalloprotease
Amino acid modifications
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	91	1	N-linked (GlcNAc...) Potential
	Glycosylation	170	1	N-linked (GlcNAc...) Potential
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	191	1

Sequences

	Sequence		Length	Mass (Da)
	P79143-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 43C2378CAC657D8F	FASTA	191	21,994
	10 20 30 40 50 60 DLSVIPVINR AQVIHDTFDL ASAQIVPVTL ALNSTLFLNQ ETEYMPWEAA LSSLSYFKLM 70 80 90 100 110 120 FDRSEVYGPM KNYLRKQVTP LFNHFEKITQ NWTDHPQTLT EQYNEINAVS TACTYGVPKC 130 140 150 160 170 180 KDLVSTLFAE WRKNPQNNPI YPNLRSTVYC NAIAQGGEEE WNFVWEQFRN TSLVNEADKL 190 RSALACSTQV W

References

[1]

"Interspecies aminopeptidase-N chimeras reveal species-specific receptor recognition by canine coronavirus, feline infectious peritonitis virus, and transmissible gastroenteritis virus." Benbacer L., Kut E., Besnardeau L., Laude H., Delmas B. J. Virol. 71:734-737(1997) [PubMed: 8985407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CCOV SPIKE GLYCOPROTEIN, IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR CCOV INFECTION. Tissue: Small intestine.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X98239 mRNA. Translation: CAA66895.1.
UniGene	Cfa.3774
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P79143.
Protein family/group databases
MEROPS	M01.001.
Genome annotation databases
Ensembl	ENSCAFT00000019070; ENSCAFP00000017677; ENSCAFG00000012013; Canis familiaris. [Genome view] ENSCAFT00000019074; ENSCAFP00000017681; ENSCAFG00000012013; Canis familiaris. [Genome view]
Phylogenomic databases
HOVERGEN	P79143.
Enzyme and pathway databases
BRENDA	3.4.11.2. 463.
Family and domain databases
InterPro	IPR001930. Peptidase_M1. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMPN_CANFA

Accession

Primary (citable) accession number: P79143

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	May 1, 1997
Last modified:	October 13, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)