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P79143 (AMPN_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

Short name=AP-N
Short name=cAPN
EC=3.4.11.2
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name=AP-M
Microsomal aminopeptidase
CD_antigen=CD13
Gene names
Name:ANPEP
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length191 AA.
Sequence statusFragment.
Protein existenceEvidence 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, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis By similarity. May serve as a receptor for bovine coronavirus (BCV) in a species-specific manner. Ref.1

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. Ref.1

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›191›191Aminopeptidase N
PRO_0000095079

Regions

Region‹1 – ›191›191Metalloprotease

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Disulfide bond113 ↔ 120 By similarity
Disulfide bond150 ↔ 186 By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1911

Sequences

Sequence LengthMass (Da)Tools
P79143 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 43C2378CAC657D8F

FASTA19121,994
        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 

« Hide

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] [Europe PMC] [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

EMBL
GenBank
DDBJ
X98239 mRNA. Translation: CAA66895.1.
UniGeneCfa.3774.

3D structure databases

ProteinModelPortalP79143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000017677.

Protein family/group databases

MEROPSM01.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0308.
HOGENOMHOG000106482.
InParanoidP79143.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_CANFA
AccessionPrimary (citable) accession number: P79143
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries