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O57579 (AMPN_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

EC=3.4.11.2
Alternative name(s):
Aminopeptidase Ey
EC=3.4.11.20
Gene names
Name:ANPEP
Synonyms:APDE
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length967 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.5 Ref.7

Catalytic activity

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. Ref.5 Ref.7

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. Ref.5 Ref.7

Cofactor

Binds 1 zinc ion per subunit. Ref.6

Subunit structure

Homodimer. Ref.4

Subcellular location

Cell membrane; Single-pass type II membrane protein. Note: A soluble form has also been detected. Ref.3

Tissue specificity

Detected in the plasma and granule fractions of egg yolk (at protein level). Ref.3

Sequence similarities

Belongs to the peptidase M1 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.58 mM for Leu-Pro-Leu-Arg-PheNH2 Ref.5 Ref.7

KM=1.23 mM for fMet-Leu-Phe Ref.7

KM=1.53 mM for fMet-Ala-Gly-Ser-Glu Ref.7

KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys Ref.7

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 967967Aminopeptidase N
PRO_0000394749

Regions

Topological domain1 – 1010Cytoplasmic
Transmembrane11 – 3121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain32 – 967936Extracellular
Region33 – 6735Cytosolic Ser/Thr-rich junction By similarity UniProtKB P15144
Region68 – 967900Metalloprotease By similarity UniProtKB P15144
Region350 – 3545Substrate binding By similarity

Sites

Active site3871Proton acceptor By similarity UniProtKB Q10740
Metal binding3861Zinc; catalytic By similarity UniProtKB Q10740
Metal binding3901Zinc; catalytic By similarity UniProtKB Q10740
Metal binding4091Zinc; catalytic By similarity UniProtKB Q10740
Site4751Transition state stabilizer By similarity

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Glycosylation5791N-linked (GlcNAc...) Potential
Glycosylation6091N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Glycosylation6731N-linked (GlcNAc...) Potential
Glycosylation6791N-linked (GlcNAc...) Potential
Glycosylation7371N-linked (GlcNAc...) Potential
Glycosylation7801N-linked (GlcNAc...) Potential
Disulfide bond759 ↔ 766 By similarity
Disulfide bond796 ↔ 832 By similarity

Experimental info

Sequence conflict2431T → K in ACZ95799. Ref.2
Sequence conflict2501V → A in ACZ95799. Ref.2
Sequence conflict5331S → T in ACZ95799. Ref.2
Sequence conflict670 – 6734HNVN → QQVS in ACZ95799. Ref.2
Sequence conflict9181H → Q in ACZ95799. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O57579 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 5CDF5C77A5BD9D1C

FASTA967108,671
        10         20         30         40         50         60 
MAAGFFISKS VGIVGIVLAL GAVATIIALS VVYAQEKNKS SGGSGGSDTT STTTASTTTA 

        70         80         90        100        110        120 
STTAAPNNPW NRWRLPTALK PESYEVTLQP FLTPDDNNMY IFKGNSSVVF LCEEATDLIL 

       130        140        150        160        170        180 
IHSNKLNYTL QGGFHASLHA VNGSTPPTIS NTWLETNTQY LVLQLAGPLQ QGQHYRLFSI 

       190        200        210        220        230        240 
FTGELADDLA GFYRSEYTEG NVTKVVATTQ MQAPDARKAF PCFDEPAMKA VFTVTMIHPS 

       250        260        270        280        290        300 
DHTAISNMPV HSTYQLQMDG QSWNVTQFDP TPRMSTYLLA FIVSQFDYVE NNTGKVQIRI 

       310        320        330        340        350        360 
WGRPAAIAEG QGEYALEKTG PILSFFERHY NTAYPLPKSD QVGLPDFNAG AMENWGLVTY 

       370        380        390        400        410        420 
RENSLLYDNA YSSIGNKERV VTVIAHELAH QWFGNLVTLR WWNDLWLNEG FASYVEYLGA 

       430        440        450        460        470        480 
DSAEPTWDIK DLMVLNELYT VMATDALTTS HPLTFREDEI NTPAQISEVF DSIAYSKGAS 

       490        500        510        520        530        540 
VLRMLSDFLT EDVFKEGLQS YLHDFSYNNT VYTDLWDHLQ EAVNKNSVPL PDSIGAIMDR 

       550        560        570        580        590        600 
WTLQMGFPVV TVNTLTGSVQ QSHFLLDSNS TVERPSVFNY TWIVPITWMT PSRTGDRYWL 

       610        620        630        640        650        660 
VDVSATNSNF SVGSSTWLLL NLNVSGYFRV NYNQENWDQL LQQLSNNHQA IPVINRAQII 

       670        680        690        700        710        720 
DDAFNLARAH NVNVTLALNT TRFLSGETAY MPWQAALNNL QYFQLMFDRS EVFGAMTKYI 

       730        740        750        760        770        780 
QKQVTPLFEY YRTATNNWTA IPSALMDQYN EINAISTACS YGIAECQQLA TALYQQWRQN 

       790        800        810        820        830        840 
VSNNPIAPNL RSAIYCSAVA TGGEEVWDFI WERFLEAPVV SEADKLRTAL TCSTETWILQ 

       850        860        870        880        890        900 
RYLQYTIDPT KIRKQDATST INSIASNVVG QPLAWDFIRS NWRTLFGQYG GGSFSFSRLI 

       910        920        930        940        950        960 
SAVTQRFNTE FELKQLEHFK ADNQDIGFGS GTRALEQALE RTRTNINWVK ENKEVVHAWF 


RAETASS 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87992 mRNA. Translation: BAA24263.1.
GU223212 mRNA. Translation: ACZ95799.1.
RefSeqNP_990192.1. NM_204861.1.
UniGeneGga.48091.
Gga.48118.

3D structure databases

ProteinModelPortalO57579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000008315.

Protein family/group databases

MEROPSM01.016.

Proteomic databases

PaxDbO57579.
PRIDEO57579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395667.
KEGGgga:395667.

Organism-specific databases

CTD290.

Phylogenomic databases

eggNOGCOG0308.
HOVERGENHBG006616.
KOK11140.
PhylomeDBO57579.

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20815739.
PROO57579.

Entry information

Entry nameAMPN_CHICK
AccessionPrimary (citable) accession number: O57579
Secondary accession number(s): D2KKL5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries