Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P79098

- AMPN_BOVIN

UniProt

P79098 - AMPN_BOVIN

Protein

Aminopeptidase N

Gene

ANPEP

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. May serve as a receptor for bovine coronavirus (BCV) in a species-specific manner.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 bindingi385 – 3851Zinc; catalyticPROSITE-ProRule annotation
    Active sitei386 – 3861Proton acceptorPROSITE-ProRule annotation
    Metal bindingi389 – 3891Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi408 – 4081Zinc; catalyticPROSITE-ProRule annotation
    Sitei474 – 4741Transition 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

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Angiogenesis, Differentiation

    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:
    bAPN
    Alternative name(s):
    Alanyl aminopeptidase
    Aminopeptidase M
    Short name:
    AP-M
    Microsomal aminopeptidase
    CD_antigen: CD13
    Gene namesi
    Name:ANPEP
    Synonyms:APN
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: 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 – 965964Aminopeptidase NPRO_0000095078Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
    Modified residuei173 – 1731SulfotyrosineSequence Analysis
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Modified residuei416 – 4161SulfotyrosineSequence Analysis
    Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi624 – 6241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi680 – 6801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi738 – 7381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi760 ↔ 767By similarity
    Disulfide bondi797 ↔ 833By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Sulfation

    Proteomic databases

    PRIDEiP79098.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP79098.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 87CytoplasmicBy similarity
    Topological domaini33 – 965933ExtracellularBy similarityAdd
    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 – 6533Cytosolic Ser/Thr-rich junctionAdd
    BLAST
    Regioni66 – 965900MetalloproteaseAdd
    BLAST
    Regioni349 – 3535Substrate bindingBy similarity

    Domaini

    Amino acids 647-837 are essential to mediate susceptibility to infection with TGEV (in human/bovine chimeric studies).

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG006616.
    InParanoidiP79098.
    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.

    P79098-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKGFYISKA LGILAILLGV AAVATIIALS VVYAQEKNKN AERGTAAPTS    50
    PTGPTTTSAT TLDQSKPWNR YRLPTTLLPD SYRVTLRPYL TPNNNGLYIF 100
    TGSSTVRFTC KEPTDVIIIH SKKLNYTQHS GHLAALKGVG DTQAPEIDRT 150
    ELVLLTEYLV VHLKSSLEAG KTYEMETTFQ GELADDLAGF YRSEYMDGNV 200
    KKVLATTQMQ STDARKSFPC FDEPAMKATF NITLIHPKDL TALSNMPPKG 250
    PSVPFDGDSN WSVTEFETTP VMSTYLLAYI VSEFTSVESV APNDVQIRIW 300
    ARPKATADNH GLYALNVTGP ILNFFANHYN TAYPLPKSDQ IALPDFNAGA 350
    MENWGLVTYR ENALLYDPQS SSSSNKERVV TVIAHELAHQ WFGNLVTLAW 400
    WNDLWLNEGF ASYVEYLGAD YAEPTWNLKD LMVPNDVYSV MAVDALVTSH 450
    PLTTPANEVN TPAQISEMFD TISYSKGASV IRMLSNFLTE DLFKKGLASY 500
    LQTFAYQNTT YLNLWEHLQM AVENQLSIRL PDTVSAIMDR WTLQMGFPVI 550
    TVDTNTGTIS QKHFLLDPNS TVTRPSQFNY LWIVPISSIR NGQPQEHYWL 600
    RGEERNQNEL FKAAADDWVL LNINVTGYYQ VNYDENNWKK IQNQLMSRRE 650
    NIPVINRAQV IYDSFNLASA HMVPVTLALN NTLFLKNEME YMPWQAAVSS 700
    LNYFKLMFDR TEVYGPMQNY LKNQVEPIFL YFENLTKNWT EIPENLMDQY 750
    SEINAISTAC SNGLPKCEEL AKTLFNQWMN NPNVNPIDPN LRSTIYCNAI 800
    AQGGQEEWDF AWNQLQQAEL VNEADKLRSA LACTNHVWLL NRYLSYTLNP 850
    DLIRKQDATS TITSIASNVI GQSLAWDFIR SNWKKLFEDY GGGSFSFSNL 900
    IQGVTRRFST EFELQQLEEF KENNMDVGFG SGTRALEQAL EKTKANINWV 950
    KENKEVVLNW FKDHS 965
    Length:965
    Mass (Da):109,276
    Last modified:January 23, 2007 - v4
    Checksum:iC730910D173879A8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC105142 mRNA. Translation: AAI05143.1.
    X98240 mRNA. Translation: CAA66896.1.
    RefSeqiNP_001068612.1. NM_001075144.1.
    UniGeneiBt.27994.

    Genome annotation databases

    GeneIDi404191.
    KEGGibta:404191.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC105142 mRNA. Translation: AAI05143.1 .
    X98240 mRNA. Translation: CAA66896.1 .
    RefSeqi NP_001068612.1. NM_001075144.1.
    UniGenei Bt.27994.

    3D structure databases

    ProteinModelPortali P79098.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2010632.

    Protein family/group databases

    MEROPSi M01.001.

    Proteomic databases

    PRIDEi P79098.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 404191.
    KEGGi bta:404191.

    Organism-specific databases

    CTDi 290.

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.
    InParanoidi P79098.
    KOi K11140.

    Miscellaneous databases

    NextBioi 20817619.

    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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.
    2. "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] OF 648-838, IDENTIFICATION OF RECEPTOR FUNCTIONAL DOMAINS FOR BCV INFECTION.
      Tissue: Intestine.

    Entry informationi

    Entry nameiAMPN_BOVIN
    AccessioniPrimary (citable) accession number: P79098
    Secondary accession number(s): Q3MHR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 4 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