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P79171

- AMPN_FELCA

UniProt

P79171 - AMPN_FELCA

Protein

Aminopeptidase N

Gene

ANPEP

Organism
Felis catus (Cat) (Felis silvestris catus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.By similarity

    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; catalyticPROSITE-ProRule annotation
    Active sitei388 – 3881Proton acceptorPROSITE-ProRule annotation
    Metal bindingi391 – 3911Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi410 – 4101Zinc; catalyticPROSITE-ProRule annotation
    Sitei476 – 4761Transition state stabilizerBy 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

    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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
    Modified residuei175 – 1751SulfotyrosineSequence Analysis
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi338 – 3381N-linked (GlcNAc...)Sequence Analysis
    Modified residuei418 – 4181SulfotyrosineSequence Analysis
    Glycosylationi626 – 6261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi740 – 7401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi762 ↔ 769By similarity
    Disulfide bondi799 ↔ 835By 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.By similarity1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP79171.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87Cytoplasmic
    Topological domaini33 – 967935ExtracellularAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei9 – 3224Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051N → S in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti144 – 1441H → Q in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti178 – 1781N → K in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti215 – 2151E → D in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti236 – 2361I → T in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti258 – 2581Missing in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti581 – 5811N → K in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti593 – 5931S → N in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti623 – 6231L → V in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti730 – 7301L → S in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti735 – 7373ERV → RKS in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti747 – 7471T → A in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti829 – 8291L → F in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti949 – 9491L → I in AAD09272. (PubMed:9782265)Curated
    Sequence conflicti967 – 9671S → SK in AAD09272. (PubMed:9782265)Curated

    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: October 1, 2014
    This is version 108 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