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Protein

Aminopeptidase Ey

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

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)DescriptionActionsGraphical viewLength
    Metal bindingi391Zinc; catalyticPROSITE-ProRule annotation1
    Active sitei392Proton acceptorPROSITE-ProRule annotation1
    Metal bindingi395Zinc; catalyticPROSITE-ProRule annotation1
    Metal bindingi414Zinc; catalyticPROSITE-ProRule annotation1
    Sitei480Transition state stabilizerBy similarity1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionAminopeptidase, Hydrolase, Metalloprotease, Protease
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKO57579.

    Protein family/group databases

    MEROPSiM01.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase Ey1 Publication (EC:3.4.11.202 Publications)
    Alternative name(s):
    Aminopeptidase NImported
    Gene namesi
    Name:ANPEP
    Synonyms:APDE
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
    Proteomesi
    • UP000000539 Componentsi: Chromosome 10, Unassembled WGS sequence, Unplaced

    Subcellular locationi

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

    • Note: Also found as a soluble form.1 Publication

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini2 – 10CytoplasmicSequence analysis9
    Transmembranei11 – 31Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini32 – 972ExtracellularAdd BLAST941

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity
    ChainiPRO_00003947492 – 972Aminopeptidase EyAdd BLAST971

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi110N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi132N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi147N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi206N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi269N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi513N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi574N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi584N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi628N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi684N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi742N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi764 ↔ 771By similarity
    Glycosylationi785N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi801 ↔ 837By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    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

    Structurei

    3D structure databases

    ProteinModelPortaliO57579.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni33 – 72Cytosolic Ser/Thr-rich junctionBy similarityAdd BLAST40
    Regioni73 – 967MetalloproteaseBy similarityAdd BLAST895
    Regioni355 – 359Substrate bindingBy similarity5

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Sequence analysis

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG006616.
    InParanoidiO57579.
    KOiK11140.
    PhylomeDBiO57579.

    Family and domain databases

    CDDicd09601. M1_APN_2. 1 hit.
    InterProiView protein in InterPro
    IPR024571. ERAP1-like_C_dom.
    IPR034016. M1_APN-typ.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiView protein in Pfam
    PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiView protein in PROSITE
    PS00142. ZINC_PROTEASE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    O57579-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAGFFISKS VGIVGIVLAL GAVATIIALS VVYAQEKNKS SGGSGGSDTT
    60 70 80 90 100
    STTTASTTTT STTTASTTAA PNNPWNRWRL PTALKPESYE VTLQPFLTPD
    110 120 130 140 150
    DNNMYIFKGN SSVVFLCEEA TDLILIHSNK LNYTLQGGFH ASLHAVNGST
    160 170 180 190 200
    PPTISNTWLE TNTQYLVLQL AGPLQQGQHY RLFSIFTGEL ADDLAGFYRS
    210 220 230 240 250
    EYTEGNVTKV VATTQMQAPD ARKAFPCFDE PAMKAVFTVT MIHPSDHTAI
    260 270 280 290 300
    SNMPVHSTYQ LQMDGQSWNV TQFDPTPRMS TYLLAFIVSQ FDYVENNTGK
    310 320 330 340 350
    VQIRIWGRPA AIAEGQGEYA LEKTGPILSF FERHYNTAYP LPKSDQVGLP
    360 370 380 390 400
    DFNAGAMENW GLVTYRENSL LYDNAYSSIG NKERVVTVIA HELAHQWFGN
    410 420 430 440 450
    LVTLRWWNDL WLNEGFASYV EYLGADSAEP TWDIKDLMVL NELYTVMATD
    460 470 480 490 500
    ALTTSHPLTF REDEINTPAQ ISEVFDSIAY SKGASVLRML SDFLTEDVFK
    510 520 530 540 550
    EGLQSYLHDF SYNNTVYTDL WDHLQEAVNK NSVPLPDSIG AIMDRWTLQM
    560 570 580 590 600
    GFPVVTVNTL TGSVQQSHFL LDSNSTVERP SVFNYTWIVP ITWMTPSRTG
    610 620 630 640 650
    DRYWLVDVSA TNSDFSVGSS TWLLLNLNVS GYFRVNYNQE NWDQLLQQLS
    660 670 680 690 700
    NNHQAIPVIN RAQIIDDAFN LARAQQVSVT LALNTTRFLS GETAYMPWQA
    710 720 730 740 750
    ALNNLQYFQL MFDRSEVFGA MTKYIQKQVT PLFEYYRTAT NNWTAIPSAL
    760 770 780 790 800
    MDQYNEINAI STACSYGIAE CQQLATALYQ QWRQNVSNNP IAPNLRSAIY
    810 820 830 840 850
    CSAVATGGEE VWDFIWERFL EAPVVSEADK LRTALTCSTE TWILQRYLQY
    860 870 880 890 900
    TIDPTKIRKQ DATSTINSIA SNVVGQPLAW DFIRSNWRTL FGQYGGGSFS
    910 920 930 940 950
    FSRLISAVTQ RFNTEFELKQ LEQFKADNQD IGFGSGTRAL EQALERTRTN
    960 970
    INWVKENKEV VHAWFRAETA SS
    Length:972
    Mass (Da):109,132
    Last modified:March 15, 2017 - v2
    Checksum:i701F1BC0BCE1F852
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti56 – 60Missing in BAA24263 (PubMed:9734335).Curated5
    Sequence conflicti56 – 60Missing in ACZ95799 (Ref. 2) Curated5
    Sequence conflicti248T → K in ACZ95799 (Ref. 2) Curated1
    Sequence conflicti255V → A in ACZ95799 (Ref. 2) Curated1
    Sequence conflicti538S → T in ACZ95799 (Ref. 2) Curated1
    Sequence conflicti614D → N in BAA24263 (PubMed:9734335).Curated1
    Sequence conflicti614D → N in ACZ95799 (Ref. 2) Curated1
    Sequence conflicti675 – 678QQVS → HNVN in BAA24263 (PubMed:9734335).Curated4
    Sequence conflicti923Q → H in BAA24263 (PubMed:9734335).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D87992 mRNA. Translation: BAA24263.1.
    GU223212 mRNA. Translation: ACZ95799.1.
    AADN04000131 Genomic DNA. No translation available.
    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.
    AADN04000131 Genomic DNA. No translation available.
    RefSeqiNP_990192.1. NM_204861.1.
    UniGeneiGga.48091.
    Gga.48118.

    3D structure databases

    ProteinModelPortaliO57579.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiM01.016.

    Proteomic databases

    PRIDEiO57579.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi395667.
    KEGGigga:395667.

    Organism-specific databases

    CTDi290.

    Phylogenomic databases

    HOVERGENiHBG006616.
    InParanoidiO57579.
    KOiK11140.
    PhylomeDBiO57579.

    Enzyme and pathway databases

    SABIO-RKO57579.

    Miscellaneous databases

    PROiO57579.

    Family and domain databases

    CDDicd09601. M1_APN_2. 1 hit.
    InterProiView protein in InterPro
    IPR024571. ERAP1-like_C_dom.
    IPR034016. M1_APN-typ.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiView protein in Pfam
    PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiView protein in PROSITE
    PS00142. ZINC_PROTEASE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAMPN_CHICK
    AccessioniPrimary (citable) accession number: O57579
    Secondary accession number(s): A0A1D5NWZ2, D2KKL5
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
    Last sequence update: March 15, 2017
    Last modified: March 15, 2017
    This is version 87 of the entry and version 2 of the sequence. See 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

    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 one 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.