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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Zn2+1 PublicationNote: 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; catalyticPROSITE-ProRule annotationBy similarity
    Active sitei387 – 3871Proton acceptorPROSITE-ProRule annotation
    Metal bindingi390 – 3901Zinc; catalyticPROSITE-ProRule annotationBy similarity
    Metal bindingi409 – 4091Zinc; catalyticPROSITE-ProRule annotationBy similarity
    Sitei475 – 4751Transition state stabilizerBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKO57579.

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539 Componenti: Unplaced

    Subcellular locationi

    • Cell membrane 1 Publication; Single-pass type II membrane protein 1 Publication

    • Note: A soluble form has also been detected.Sequence Analysis1 Publication

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010CytoplasmicSequence Analysis
    Transmembranei11 – 3121Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST
    Topological domaini32 – 967936ExtracellularAdd
    BLAST

    GO - Cellular componenti

    Complete GO annotation...

    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...

    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.
    InParanoidiO57579.
    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

            10         20         30         40         50
    MAAGFFISKS VGIVGIVLAL GAVATIIALS VVYAQEKNKS SGGSGGSDTT
    60 70 80 90 100
    STTTASTTTA STTAAPNNPW NRWRLPTALK PESYEVTLQP FLTPDDNNMY
    110 120 130 140 150
    IFKGNSSVVF LCEEATDLIL IHSNKLNYTL QGGFHASLHA VNGSTPPTIS
    160 170 180 190 200
    NTWLETNTQY LVLQLAGPLQ QGQHYRLFSI FTGELADDLA GFYRSEYTEG
    210 220 230 240 250
    NVTKVVATTQ MQAPDARKAF PCFDEPAMKA VFTVTMIHPS DHTAISNMPV
    260 270 280 290 300
    HSTYQLQMDG QSWNVTQFDP TPRMSTYLLA FIVSQFDYVE NNTGKVQIRI
    310 320 330 340 350
    WGRPAAIAEG QGEYALEKTG PILSFFERHY NTAYPLPKSD QVGLPDFNAG
    360 370 380 390 400
    AMENWGLVTY RENSLLYDNA YSSIGNKERV VTVIAHELAH QWFGNLVTLR
    410 420 430 440 450
    WWNDLWLNEG FASYVEYLGA DSAEPTWDIK DLMVLNELYT VMATDALTTS
    460 470 480 490 500
    HPLTFREDEI NTPAQISEVF DSIAYSKGAS VLRMLSDFLT EDVFKEGLQS
    510 520 530 540 550
    YLHDFSYNNT VYTDLWDHLQ EAVNKNSVPL PDSIGAIMDR WTLQMGFPVV
    560 570 580 590 600
    TVNTLTGSVQ QSHFLLDSNS TVERPSVFNY TWIVPITWMT PSRTGDRYWL
    610 620 630 640 650
    VDVSATNSNF SVGSSTWLLL NLNVSGYFRV NYNQENWDQL LQQLSNNHQA
    660 670 680 690 700
    IPVINRAQII DDAFNLARAH NVNVTLALNT TRFLSGETAY MPWQAALNNL
    710 720 730 740 750
    QYFQLMFDRS EVFGAMTKYI QKQVTPLFEY YRTATNNWTA IPSALMDQYN
    760 770 780 790 800
    EINAISTACS YGIAECQQLA TALYQQWRQN VSNNPIAPNL RSAIYCSAVA
    810 820 830 840 850
    TGGEEVWDFI WERFLEAPVV SEADKLRTAL TCSTETWILQ RYLQYTIDPT
    860 870 880 890 900
    KIRKQDATST INSIASNVVG QPLAWDFIRS NWRTLFGQYG GGSFSFSRLI
    910 920 930 940 950
    SAVTQRFNTE FELKQLEHFK ADNQDIGFGS GTRALEQALE RTRTNINWVK
    960
    ENKEVVHAWF RAETASS
    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 (Ref. 2) Curated
    Sequence conflicti250 – 2501V → A in ACZ95799 (Ref. 2) Curated
    Sequence conflicti533 – 5331S → T in ACZ95799 (Ref. 2) Curated
    Sequence conflicti670 – 6734HNVN → QQVS in ACZ95799 (Ref. 2) Curated
    Sequence conflicti918 – 9181H → Q in ACZ95799 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D87992 mRNA. Translation: BAA24263.1.
    GU223212 mRNA. Translation: ACZ95799.1.
    RefSeqiNP_990192.1. NM_204861.1.
    UniGeneiGga.48091.
    Gga.48118.

    3D structure databases

    ProteinModelPortaliO57579.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000008315.

    Protein family/group databases

    MEROPSiM01.016.

    Proteomic databases

    PaxDbiO57579.
    PRIDEiO57579.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi395667.
    KEGGigga:395667.

    Organism-specific databases

    CTDi290.

    Phylogenomic databases

    eggNOGiCOG0308.
    HOVERGENiHBG006616.
    InParanoidiO57579.
    KOiK11140.
    PhylomeDBiO57579.

    Enzyme and pathway databases

    SABIO-RKO57579.

    Miscellaneous databases

    NextBioi20815739.
    PROiO57579.

    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]
    ProtoNetiSearch...

    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: May 27, 2015
    This is version 80 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.