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P79171

- AMPN_FELCA

UniProt

P79171 - AMPN_FELCA

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Protein

Aminopeptidase N

Gene
ANPEP, APN
Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

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.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi387 – 3871Zinc; catalytic By similarity
Active sitei388 – 3881Proton acceptor By similarity
Metal bindingi391 – 3911Zinc; catalytic By similarity
Metal bindingi410 – 4101Zinc; catalytic By similarity
Sitei476 – 4761Transition state stabilizer By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. virus receptor activity Source: UniProtKB-KW
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Developmental protein, Host cell receptor for virus entry, Hydrolase, Metalloprotease, Protease, Receptor

Keywords - Biological processi

Angiogenesis, Differentiation, Host-virus interaction

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Short name:
fAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:ANPEP
Synonyms:APN
OrganismiFelis catus (Cat) (Felis silvestris catus)
Taxonomic identifieri9685 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis
ProteomesiUP000011712: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 87Cytoplasmic
Transmembranei9 – 3224Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini33 – 967935ExtracellularAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 967966Aminopeptidase NPRO_0000095080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi84 – 841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi126 – 1261N-linked (GlcNAc...) Reviewed prediction
Modified residuei175 – 1751Sulfotyrosine Reviewed prediction
Glycosylationi233 – 2331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi338 – 3381N-linked (GlcNAc...) Reviewed prediction
Modified residuei418 – 4181Sulfotyrosine Reviewed prediction
Glycosylationi626 – 6261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi682 – 6821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi740 – 7401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi762 ↔ 769 By similarity
Disulfide bondi799 ↔ 835 By similarity

Post-translational modificationi

Sulfated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with FCoV, CCoV, TGEV and HCoV-229E spike glycoprotein.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP79171.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6634Cytosolic Ser/Thr-rich junctionAdd
BLAST
Regioni67 – 967901MetalloproteaseAdd
BLAST
Regioni351 – 3555Substrate binding By similarity
Regioni670 – 840171Interaction with FCoV and TGEV spike glycoproteinAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOVERGENiHBG006616.
KOiK11140.

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P79171-1 [UniParc]FASTAAdd to Basket

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MAKGFYISKP VGILAILLGV AAVCTIIALS VVYSQEKNRS TESSTAASTA    50
APTGPTTTVA TTLDQSKPWN VYRLPKTLIP DSYNVTLRPY LTPNNKGLYV 100
FTGTNIVRFT CKESTNIVII HSKRLNYTSH QGHMVALSGV GGFHPQPVIV 150
RTELVELTEY LVVHLQEPLV AGRQYEMNSE FQGELADDLA GFYRSEYMEN 200
GVKKVLATTH MQATEARKSF PCFDEPAMKA TFNITIIHPN NLVALSNMLP 250
RGPSVPFGED PTWKVTEFET TPIMSTYLLA YIVSEFSYVE TRAPSGVLIR 300
IWARPSAINQ GHGDYALKVT GPILDFFSQH YDTPYPLNKS DQIALPDFNA 350
GAMENWGLVT YRESALLYDR QSSSSGNQER VVTVIAHELA HQWFGNLVTL 400
EWWNDLWLNE GFASYVEYLG ADFAEPTWNL KDLMVLNDVY RVMAVDALAS 450
SHPLSTPASE INTPAQISEV FDSISYSKGA SVLRMLSNFL TEDLFKMGIA 500
SYLHTYKYGN TIYLNLWEHL QQVVDKQPTI KLPDTVSAIM DRWILQMGFP 550
VITVDTQTGT ISQQHFLLDP QSVVTRPSQF NYLWIVPISS VRSGSPQAHY 600
WLPGVEKAQN DLFKTTANDW VLLNLNVTGY YLVNYDNENW KKIQTQLQTD 650
LSVIPVINRA QVIHDAFNLA SAQKVPVTLA LNNTLFLIQE TEYMPWQAAL 700
SSLSYFKLMF DRSEVYGPMK RYLKKQVTPL FNHFERVTKN WTDHPQTLMD 750
QYSEINAVST ACSYGVPECE KLAATLFAQW KKNPQNNPIH PNLRSTVYCN 800
AIAQGGEEEW NFVWEQFLKA ELVNEADKLR GALACSNQVW ILNRFLSYTL 850
DPNLIRKQDV TSTLSSISSN VVGQTLVWDF VQSNWKKLFQ DYGTGSFSFS 900
NLIQAVTRRF STEFELQQLE QFKKNNMDTG FGSATRALEQ ALEKTKANLK 950
WVKENKDVVL RWFTENS 967
Length:967
Mass (Da):109,424
Last modified:January 23, 2007 - v3
Checksum:i119BDAA34F5B5E89
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051N → S in AAD09272. 1 Publication
Sequence conflicti144 – 1441H → Q in AAD09272. 1 Publication
Sequence conflicti178 – 1781N → K in AAD09272. 1 Publication
Sequence conflicti215 – 2151E → D in AAD09272. 1 Publication
Sequence conflicti236 – 2361I → T in AAD09272. 1 Publication
Sequence conflicti258 – 2581Missing in AAD09272. 1 Publication
Sequence conflicti581 – 5811N → K in AAD09272. 1 Publication
Sequence conflicti593 – 5931S → N in AAD09272. 1 Publication
Sequence conflicti623 – 6231L → V in AAD09272. 1 Publication
Sequence conflicti730 – 7301L → S in AAD09272. 1 Publication
Sequence conflicti735 – 7373ERV → RKS in AAD09272. 1 Publication
Sequence conflicti747 – 7471T → A in AAD09272. 1 Publication
Sequence conflicti829 – 8291L → F in AAD09272. 1 Publication
Sequence conflicti949 – 9491L → I in AAD09272. 1 Publication
Sequence conflicti967 – 9671S → SK in AAD09272. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58920 mRNA. Translation: AAC48686.1.
U96104 mRNA. Translation: AAD09272.1.
RefSeqiNP_001009252.2. NM_001009252.2.

Genome annotation databases

GeneIDi493785.
KEGGifca:493785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U58920 mRNA. Translation: AAC48686.1 .
U96104 mRNA. Translation: AAD09272.1 .
RefSeqi NP_001009252.2. NM_001009252.2.

3D structure databases

ProteinModelPortali P79171.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M01.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 493785.
KEGGi fca:493785.

Organism-specific databases

CTDi 290.

Phylogenomic databases

eggNOGi COG0308.
HOVERGENi HBG006616.
KOi K11140.

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAMPN_FELCA
AccessioniPrimary (citable) accession number: P79171
Secondary accession number(s): O97783
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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