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O57579

- AMPN_CHICK

UniProt

O57579 - AMPN_CHICK

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Protein

Aminopeptidase N

Gene

ANPEP

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.

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; 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
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 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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
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

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

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
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. 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:
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 .
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.
InParanoidi O57579.
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: November 26, 2014
This is version 77 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