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O57579

- AMPN_CHICK

UniProt

O57579 - AMPN_CHICK

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Protein

Aminopeptidase N

Gene
ANPEP, APDE
Organism
Gallus gallus (Chicken)
Status
Reviewed - 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.2 Publications

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-Phe1 Publication
  3. KM=1.53 mM for fMet-Ala-Gly-Ser-Glu1 Publication
  4. KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi386 – 3861Zinc; catalytic By similarityBy similarity
Active sitei387 – 3871Proton acceptor By similarityBy similarity
Metal bindingi390 – 3901Zinc; catalytic By similarityBy similarity
Metal bindingi409 – 4091Zinc; catalytic By similarityBy similarity
Sitei475 – 4751Transition state stabilizer By similarity

GO - Molecular functioni

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

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 N (EC:3.4.11.2)
Alternative name(s):
Aminopeptidase Ey (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; Single-pass type II membrane protein
Note: A soluble form has also been detected.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Cytoplasmic
Transmembranei11 – 3121Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini32 – 967936ExtracellularAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
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...) Reviewed prediction
Glycosylationi105 – 1051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Glycosylationi142 – 1421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi201 – 2011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi264 – 2641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi291 – 2911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi508 – 5081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi569 – 5691N-linked (GlcNAc...) Reviewed prediction
Glycosylationi579 – 5791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi609 – 6091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi623 – 6231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi673 – 6731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi679 – 6791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi737 – 7371N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi759 ↔ 766 By similarity
Glycosylationi780 – 7801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi796 ↔ 832 By 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 6735Cytosolic Ser/Thr-rich junction By similarityBy similarityAdd
BLAST
Regioni68 – 967900Metalloprotease By similarityBy similarityAdd
BLAST
Regioni350 – 3545Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

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

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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

Sequence conflict

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

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 yolk and Liver.
  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 kidney.
  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 14, 2014
This is version 74 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

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