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P79171 (AMPN_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 105. 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=fAPN
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
Synonyms:APN
OrganismFelis catus (Cat) (Felis silvestris catus) [Reference proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. In case of feline coronavirus (FCoV) infection, serves as a receptor for FCoV spike glycoprotein. It is as well a receptor for other serogroup I coronaviruses, like canine coronavirus (CCoV), porcine transmissible gastroenteritis virus (TGEV), and human coronavirus 229E (HCoV-229E). Also serves as a receptor for infectious bronchitis virus (IBV, Arkansas 99 serotype) in serogroup III. Ref.1 Ref.2 Ref.3 Ref.4

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 FCoV, CCoV, TGEV and HCoV-229E spike glycoprotein. Ref.1

Subcellular location

Membrane; Single-pass type II membrane protein.

Post-translational modification

Sulfated By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 967966Aminopeptidase N
PRO_0000095080

Regions

Topological domain2 – 87Cytoplasmic
Transmembrane9 – 3224Helical; Signal-anchor for type II membrane protein; Potential
Topological domain33 – 967935Extracellular
Region33 – 6634Cytosolic Ser/Thr-rich junction
Region67 – 967901Metalloprotease
Region351 – 3555Substrate binding By similarity
Region670 – 840171Interaction with FCoV and TGEV spike glycoprotein

Sites

Active site3881Proton acceptor By similarity
Metal binding3871Zinc; catalytic By similarity
Metal binding3911Zinc; catalytic By similarity
Metal binding4101Zinc; catalytic By similarity
Site4761Transition state stabilizer By similarity

Amino acid modifications

Modified residue1751Sulfotyrosine Potential
Modified residue4181Sulfotyrosine Potential
Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation3381N-linked (GlcNAc...) Potential
Glycosylation6261N-linked (GlcNAc...) Potential
Glycosylation6821N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Disulfide bond762 ↔ 769 By similarity
Disulfide bond799 ↔ 835 By similarity

Experimental info

Sequence conflict1051N → S in AAD09272. Ref.2
Sequence conflict1441H → Q in AAD09272. Ref.2
Sequence conflict1781N → K in AAD09272. Ref.2
Sequence conflict2151E → D in AAD09272. Ref.2
Sequence conflict2361I → T in AAD09272. Ref.2
Sequence conflict2581Missing in AAD09272. Ref.2
Sequence conflict5811N → K in AAD09272. Ref.2
Sequence conflict5931S → N in AAD09272. Ref.2
Sequence conflict6231L → V in AAD09272. Ref.2
Sequence conflict7301L → S in AAD09272. Ref.2
Sequence conflict735 – 7373ERV → RKS in AAD09272. Ref.2
Sequence conflict7471T → A in AAD09272. Ref.2
Sequence conflict8291L → F in AAD09272. Ref.2
Sequence conflict9491L → I in AAD09272. Ref.2
Sequence conflict9671S → SK in AAD09272. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P79171 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 119BDAA34F5B5E89

FASTA967109,424
        10         20         30         40         50         60 
MAKGFYISKP VGILAILLGV AAVCTIIALS VVYSQEKNRS TESSTAASTA APTGPTTTVA 

        70         80         90        100        110        120 
TTLDQSKPWN VYRLPKTLIP DSYNVTLRPY LTPNNKGLYV FTGTNIVRFT CKESTNIVII 

       130        140        150        160        170        180 
HSKRLNYTSH QGHMVALSGV GGFHPQPVIV RTELVELTEY LVVHLQEPLV AGRQYEMNSE 

       190        200        210        220        230        240 
FQGELADDLA GFYRSEYMEN GVKKVLATTH MQATEARKSF PCFDEPAMKA TFNITIIHPN 

       250        260        270        280        290        300 
NLVALSNMLP RGPSVPFGED PTWKVTEFET TPIMSTYLLA YIVSEFSYVE TRAPSGVLIR 

       310        320        330        340        350        360 
IWARPSAINQ GHGDYALKVT GPILDFFSQH YDTPYPLNKS DQIALPDFNA GAMENWGLVT 

       370        380        390        400        410        420 
YRESALLYDR QSSSSGNQER VVTVIAHELA HQWFGNLVTL EWWNDLWLNE GFASYVEYLG 

       430        440        450        460        470        480 
ADFAEPTWNL KDLMVLNDVY RVMAVDALAS SHPLSTPASE INTPAQISEV FDSISYSKGA 

       490        500        510        520        530        540 
SVLRMLSNFL TEDLFKMGIA SYLHTYKYGN TIYLNLWEHL QQVVDKQPTI KLPDTVSAIM 

       550        560        570        580        590        600 
DRWILQMGFP VITVDTQTGT ISQQHFLLDP QSVVTRPSQF NYLWIVPISS VRSGSPQAHY 

       610        620        630        640        650        660 
WLPGVEKAQN DLFKTTANDW VLLNLNVTGY YLVNYDNENW KKIQTQLQTD LSVIPVINRA 

       670        680        690        700        710        720 
QVIHDAFNLA SAQKVPVTLA LNNTLFLIQE TEYMPWQAAL SSLSYFKLMF DRSEVYGPMK 

       730        740        750        760        770        780 
RYLKKQVTPL FNHFERVTKN WTDHPQTLMD QYSEINAVST ACSYGVPECE KLAATLFAQW 

       790        800        810        820        830        840 
KKNPQNNPIH PNLRSTVYCN AIAQGGEEEW NFVWEQFLKA ELVNEADKLR GALACSNQVW 

       850        860        870        880        890        900 
ILNRFLSYTL DPNLIRKQDV TSTLSSISSN VVGQTLVWDF VQSNWKKLFQ DYGTGSFSFS 

       910        920        930        940        950        960 
NLIQAVTRRF STEFELQQLE QFKKNNMDTG FGSATRALEQ ALEKTKANLK WVKENKDVVL 


RWFTENS 

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References

[1]"Feline aminopeptidase N serves as a receptor for feline, canine, porcine, and human coronaviruses in serogroup I."
Tresnan D.B., Levis R., Holmes K.V.
J. Virol. 70:8669-8674(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FCOV SPIKE GLYCOPROTEIN, CHARACTERIZATION OF CORONAVIRUS RECEPTOR FUNCTION.
[2]"Molecular analysis of the coronavirus-receptor function of aminopeptidase N."
Kolb A.F., Hegyi A., Maile J., Heister A., Hagemann M., Siddell S.G.
Adv. Exp. Med. Biol. 440:61-67(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR FIPV INFECTION.
[3]"Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N."
Hegyi A., Kolb A.F.
J. Gen. Virol. 79:1387-1391(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR FIPV; TGEV AND HCV-229E INFECTION.
[4]"The role of feline aminopeptidase N as a receptor for infectious bronchitis virus."
Miguel B., Pharr G.T., Wang C.
Arch. Virol. 147:2047-2056(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF IBV RECEPTOR FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58920 mRNA. Translation: AAC48686.1.
U96104 mRNA. Translation: AAD09272.1.
RefSeqNP_001009252.2. NM_001009252.2.

3D structure databases

ProteinModelPortalP79171.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM01.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493785.
KEGGfca:493785.

Organism-specific databases

CTD290.

Phylogenomic databases

eggNOGCOG0308.
HOVERGENHBG006616.
KOK11140.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_FELCA
AccessionPrimary (citable) accession number: P79171
Secondary accession number(s): O97783
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 105 of the entry and version 3 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