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O57579

- AMPN_CHICK

UniProt

O57579 - AMPN_CHICK

Protein

Aminopeptidase N

Gene

ANPEP

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Broad specificity aminopeptidase. Degrades a variety of peptides possessing various N-terminal amino acids including hydrophobic, basic and acidic amino acids. Preferentially hydrolyzes small peptides consisting of 4 or 5 amino acids. Hydrolyzes the N-terminal Xaa-Pro bonds in the chicken brain peptide Leu-Pro-Leu-Arg-PheNH2, the substance P fragment Arg-Pro-Lys-Pro and the bradykinin fragment Arg-Pro-Pro-Gly-Phe. Hydrolyzes the N-formylated peptides fMet-Leu-Phe, fMet-Ala-Gly-Ser-Glu and fMet-Nle-Leu-Phe-Nle-Tyr-Lys, but does not hydrolyze peptides with acetylation or pyroglutamic acid at N-terminus. Does not hydrolyze large peptides such as complete substance P, bradykinin or schistoFLRFamide.3 Publications

    Catalytic activityi

    Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyze peptides of four or five residues that contain Pro in the P1' position.2 Publications
    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.1 Publication

    Kineticsi

    1. KM=0.58 mM for Leu-Pro-Leu-Arg-PheNH22 Publications
    2. KM=1.23 mM for fMet-Leu-Phe2 Publications
    3. KM=1.53 mM for fMet-Ala-Gly-Ser-Glu2 Publications
    4. KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi386 – 3861Zinc; catalyticBy similarityPROSITE-ProRule annotation
    Active sitei387 – 3871Proton acceptorPROSITE-ProRule annotation
    Metal bindingi390 – 3901Zinc; catalyticBy similarityPROSITE-ProRule annotation
    Metal bindingi409 – 4091Zinc; catalyticBy similarityPROSITE-ProRule annotation
    Sitei475 – 4751Transition state stabilizerBy similarity

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM01.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase NImported (EC:3.4.11.2)
    Alternative name(s):
    Aminopeptidase EyImported (EC:3.4.11.20)
    Gene namesi
    Name:ANPEP
    Synonyms:APDE
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication
    Note: A soluble form has also been detected.1 PublicationSequence Analysis

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 967967Aminopeptidase NPRO_0000394749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi264 – 2641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi508 – 5081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi579 – 5791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi609 – 6091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi679 – 6791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi737 – 7371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi759 ↔ 766By similarity
    Glycosylationi780 – 7801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi796 ↔ 832By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO57579.
    PRIDEiO57579.

    Expressioni

    Tissue specificityi

    Detected in the plasma and granule fractions of egg yolk (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000008315.

    Structurei

    3D structure databases

    ProteinModelPortaliO57579.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010CytoplasmicSequence Analysis
    Topological domaini32 – 967936ExtracellularAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 6735Cytosolic Ser/Thr-rich junctionBy similarityAdd
    BLAST
    Regioni68 – 967900MetalloproteaseBy similarityAdd
    BLAST
    Regioni350 – 3545Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Sequence Analysis

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOVERGENiHBG006616.
    KOiK11140.
    PhylomeDBiO57579.

    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.

    O57579-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAGFFISKS VGIVGIVLAL GAVATIIALS VVYAQEKNKS SGGSGGSDTT    50
    STTTASTTTA STTAAPNNPW NRWRLPTALK PESYEVTLQP FLTPDDNNMY 100
    IFKGNSSVVF LCEEATDLIL IHSNKLNYTL QGGFHASLHA VNGSTPPTIS 150
    NTWLETNTQY LVLQLAGPLQ QGQHYRLFSI FTGELADDLA GFYRSEYTEG 200
    NVTKVVATTQ MQAPDARKAF PCFDEPAMKA VFTVTMIHPS DHTAISNMPV 250
    HSTYQLQMDG QSWNVTQFDP TPRMSTYLLA FIVSQFDYVE NNTGKVQIRI 300
    WGRPAAIAEG QGEYALEKTG PILSFFERHY NTAYPLPKSD QVGLPDFNAG 350
    AMENWGLVTY RENSLLYDNA YSSIGNKERV VTVIAHELAH QWFGNLVTLR 400
    WWNDLWLNEG FASYVEYLGA DSAEPTWDIK DLMVLNELYT VMATDALTTS 450
    HPLTFREDEI NTPAQISEVF DSIAYSKGAS VLRMLSDFLT EDVFKEGLQS 500
    YLHDFSYNNT VYTDLWDHLQ EAVNKNSVPL PDSIGAIMDR WTLQMGFPVV 550
    TVNTLTGSVQ QSHFLLDSNS TVERPSVFNY TWIVPITWMT PSRTGDRYWL 600
    VDVSATNSNF SVGSSTWLLL NLNVSGYFRV NYNQENWDQL LQQLSNNHQA 650
    IPVINRAQII DDAFNLARAH NVNVTLALNT TRFLSGETAY MPWQAALNNL 700
    QYFQLMFDRS EVFGAMTKYI QKQVTPLFEY YRTATNNWTA IPSALMDQYN 750
    EINAISTACS YGIAECQQLA TALYQQWRQN VSNNPIAPNL RSAIYCSAVA 800
    TGGEEVWDFI WERFLEAPVV SEADKLRTAL TCSTETWILQ RYLQYTIDPT 850
    KIRKQDATST INSIASNVVG QPLAWDFIRS NWRTLFGQYG GGSFSFSRLI 900
    SAVTQRFNTE FELKQLEHFK ADNQDIGFGS GTRALEQALE RTRTNINWVK 950
    ENKEVVHAWF RAETASS 967
    Length:967
    Mass (Da):108,671
    Last modified:June 1, 1998 - v1
    Checksum:i5CDF5C77A5BD9D1C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti243 – 2431T → K in ACZ95799. 1 PublicationCurated
    Sequence conflicti250 – 2501V → A in ACZ95799. 1 PublicationCurated
    Sequence conflicti533 – 5331S → T in ACZ95799. 1 PublicationCurated
    Sequence conflicti670 – 6734HNVN → QQVS in ACZ95799. 1 PublicationCurated
    Sequence conflicti918 – 9181H → Q in ACZ95799. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87992 mRNA. Translation: BAA24263.1.
    GU223212 mRNA. Translation: ACZ95799.1.
    RefSeqiNP_990192.1. NM_204861.1.
    UniGeneiGga.48091.
    Gga.48118.

    Genome annotation databases

    GeneIDi395667.
    KEGGigga:395667.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87992 mRNA. Translation: BAA24263.1 .
    GU223212 mRNA. Translation: ACZ95799.1 .
    RefSeqi NP_990192.1. NM_204861.1.
    UniGenei Gga.48091.
    Gga.48118.

    3D structure databases

    ProteinModelPortali O57579.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000008315.

    Protein family/group databases

    MEROPSi M01.016.

    Proteomic databases

    PaxDbi O57579.
    PRIDEi O57579.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 395667.
    KEGGi gga:395667.

    Organism-specific databases

    CTDi 290.

    Phylogenomic databases

    eggNOGi COG0308.
    HOVERGENi HBG006616.
    KOi K11140.
    PhylomeDBi O57579.

    Miscellaneous databases

    NextBioi 20815739.
    PROi O57579.

    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. "Isolation and characterization of cDNA encoding chicken egg yolk aminopeptidase Ey."
      Midorikawa T., Abe R., Yamagata Y., Nakajima T., Ichishima E.
      Comp. Biochem. Physiol. 119:513-520(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 219-229; 296-363; 378-405; 496-526 AND 954-966.
      Tissue: Egg yolk1 Publication and Liver1 Publication.
    2. "Soluble high-expression and biological function of chicken aminopeptidase N."
      Xin Y., Ping W., Bo M.X.
      Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryonic kidneyImported.
    3. "Soluble and bound forms of aminopeptidase in hen's egg yolk."
      Ichishima E., Yamagata Y., Chiba H., Sawaguchi K., Tanaka T.
      Agric. Biol. Chem. 53:1867-1872(1989)
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Electron microscopic analysis of dimeric form of aminopeptidase Ey from hen's egg yolk."
      Tanaka T., Oshida K., Ichishima E.
      Agric. Biol. Chem. 55:2179-2181(1991)
      Cited for: SUBUNIT.
    5. "Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus) egg yolk."
      Tanaka T., Ichishima E.
      Comp. Biochem. Physiol. 105:105-110(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme."
      Tanaka T., Ichishima E.
      Int. J. Biochem. 25:1681-1688(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    7. "Inactivation of chemotactic peptides by aminopeptidase Ey from hen's (Gallus gallus domesticus) egg yolk."
      Tanaka T., Ichishima E.
      Comp. Biochem. Physiol. 107B:533-538(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiAMPN_CHICK
    AccessioniPrimary (citable) accession number: O57579
    Secondary accession number(s): D2KKL5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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