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Aminopeptidase Ey (EC 3.4.11.20) (Aminopeptidase N)

 AMPN_CHICK              Reviewed;         972 AA.
O57579; A0A1D5NWZ2; D2KKL5;
15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 2.
25-APR-2018, entry version 95.
RecName: Full=Aminopeptidase Ey {ECO:0000303|PubMed:9734335};
EC=3.4.11.20 {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
AltName: Full=Aminopeptidase N {ECO:0000312|EMBL:ACZ95799.1};
Name=ANPEP; Synonyms=APDE;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 224-234; 296-363;
378-405; 496-526 AND 954-966.
TISSUE=Egg yolk {ECO:0000269|PubMed:9734335}, and
Liver {ECO:0000269|PubMed:9734335};
PubMed=9734335; DOI=10.1016/S0305-0491(98)00012-1;
Midorikawa T., Abe R., Yamagata Y., Nakajima T., Ichishima E.;
"Isolation and characterization of cDNA encoding chicken egg yolk
aminopeptidase Ey.";
Comp. Biochem. Physiol. 119:513-520(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryonic kidney {ECO:0000312|EMBL:ACZ95799.1};
Xin Y., Ping W., Bo M.X.;
"Soluble high-expression and biological function of chicken
aminopeptidase N.";
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl;
PubMed=15592404; DOI=10.1038/nature03154;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
Ichishima E., Yamagata Y., Chiba H., Sawaguchi K., Tanaka T.;
"Soluble and bound forms of aminopeptidase in hen's egg yolk.";
Agric. Biol. Chem. 53:1867-1872(1989).
[5]
SUBUNIT.
Tanaka T., Oshida K., Ichishima E.;
"Electron microscopic analysis of dimeric form of aminopeptidase Ey
from hen's egg yolk.";
Agric. Biol. Chem. 55:2179-2181(1991).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7684960;
Tanaka T., Ichishima E.;
"Substrate specificity of aminopeptidase Ey from hen's (Gallus
domesticus) egg yolk.";
Comp. Biochem. Physiol. 105:105-110(1993).
[7]
COFACTOR.
PubMed=8288037; DOI=10.1016/0020-711X(93)90528-M;
Tanaka T., Ichishima E.;
"Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme.";
Int. J. Biochem. 25:1681-1688(1993).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8205380;
Tanaka T., Ichishima E.;
"Inactivation of chemotactic peptides by aminopeptidase Ey from hen's
(Gallus gallus domesticus) egg yolk.";
Comp. Biochem. Physiol. 107B:533-538(1994).
-!- 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. {ECO:0000269|PubMed:7684960,
ECO:0000269|PubMed:8205380, ECO:0000269|Ref.4}.
-!- 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. {ECO:0000269|PubMed:7684960,
ECO:0000269|PubMed:8205380}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:8288037};
Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:8288037};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.58 mM for Leu-Pro-Leu-Arg-PheNH2
{ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
KM=1.23 mM for fMet-Leu-Phe {ECO:0000269|PubMed:7684960,
ECO:0000269|PubMed:8205380};
KM=1.53 mM for fMet-Ala-Gly-Ser-Glu {ECO:0000269|PubMed:7684960,
ECO:0000269|PubMed:8205380};
KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys
{ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
-!- SUBUNIT: Homodimer. {ECO:0000269|Ref.5}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.4}; Single-
pass type II membrane protein {ECO:0000250|UniProtKB:P15144}.
Note=Also found as a soluble form. {ECO:0000269|Ref.4}.
-!- TISSUE SPECIFICITY: Detected in the plasma and granule fractions
of egg yolk (at protein level). {ECO:0000269|Ref.4}.
-!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000255}.
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EMBL; D87992; BAA24263.1; -; mRNA.
EMBL; GU223212; ACZ95799.1; -; mRNA.
EMBL; AADN04000131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_990192.1; NM_204861.1.
RefSeq; XP_015147557.1; XM_015292071.1.
UniGene; Gga.48091; -.
UniGene; Gga.48118; -.
ProteinModelPortal; O57579; -.
SMR; O57579; -.
STRING; 9031.ENSGALP00000008315; -.
MEROPS; M01.016; -.
PaxDb; O57579; -.
PRIDE; O57579; -.
Ensembl; ENSGALT00000064511; ENSGALP00000044885; ENSGALG00000027501.
Ensembl; ENSGALT00000084741; ENSGALP00000062702; ENSGALG00000027501.
GeneID; 395667; -.
KEGG; gga:395667; -.
CTD; 290; -.
GeneTree; ENSGT00760000119082; -.
HOVERGEN; HBG006616; -.
InParanoid; O57579; -.
KO; K11140; -.
OMA; NNPIHPN; -.
PhylomeDB; O57579; -.
SABIO-RK; O57579; -.
PRO; PR:O57579; -.
Proteomes; UP000000539; Chromosome 10.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
GO; GO:0042277; F:peptide binding; IBA:GO_Central.
GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
CDD; cd09601; M1_APN_2; 1.
InterPro; IPR024571; ERAP1-like_C_dom.
InterPro; IPR034016; M1_APN-typ.
InterPro; IPR001930; Peptidase_M1.
InterPro; IPR014782; Peptidase_M1_N.
PANTHER; PTHR11533; PTHR11533; 1.
Pfam; PF11838; ERAP1_C; 1.
Pfam; PF01433; Peptidase_M1; 1.
PRINTS; PR00756; ALADIPTASE.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Aminopeptidase; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P15144}.
CHAIN 2 972 Aminopeptidase Ey.
/FTId=PRO_0000394749.
TOPO_DOM 2 10 Cytoplasmic. {ECO:0000255}.
TRANSMEM 11 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 972 Extracellular.
REGION 33 72 Cytosolic Ser/Thr-rich junction.
{ECO:0000250|UniProtKB:P15144}.
REGION 73 967 Metalloprotease.
{ECO:0000250|UniProtKB:P15144}.
REGION 355 359 Substrate binding.
{ECO:0000250|UniProtKB:P15144}.
ACT_SITE 392 392 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 391 391 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 395 395 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 414 414 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
SITE 480 480 Transition state stabilizer.
{ECO:0000250|UniProtKB:P15144}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 584 584 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 684 684 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 742 742 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 785 785 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 764 771 {ECO:0000250}.
DISULFID 801 837 {ECO:0000250}.
CONFLICT 56 60 Missing (in Ref. 1; BAA24263 and 2;
ACZ95799). {ECO:0000305}.
CONFLICT 248 248 T -> K (in Ref. 2; ACZ95799).
{ECO:0000305}.
CONFLICT 255 255 V -> A (in Ref. 2; ACZ95799).
{ECO:0000305}.
CONFLICT 538 538 S -> T (in Ref. 2; ACZ95799).
{ECO:0000305}.
CONFLICT 614 614 D -> N (in Ref. 1; BAA24263 and 2;
ACZ95799). {ECO:0000305}.
CONFLICT 675 678 QQVS -> HNVN (in Ref. 1; BAA24263).
{ECO:0000305}.
CONFLICT 923 923 Q -> H (in Ref. 1; BAA24263).
{ECO:0000305}.
SEQUENCE 972 AA; 109132 MW; 701F1BC0BCE1F852 CRC64;
MAAGFFISKS VGIVGIVLAL GAVATIIALS VVYAQEKNKS SGGSGGSDTT STTTASTTTT
STTTASTTAA PNNPWNRWRL PTALKPESYE VTLQPFLTPD DNNMYIFKGN SSVVFLCEEA
TDLILIHSNK LNYTLQGGFH ASLHAVNGST PPTISNTWLE TNTQYLVLQL AGPLQQGQHY
RLFSIFTGEL ADDLAGFYRS EYTEGNVTKV VATTQMQAPD ARKAFPCFDE PAMKAVFTVT
MIHPSDHTAI SNMPVHSTYQ LQMDGQSWNV TQFDPTPRMS TYLLAFIVSQ FDYVENNTGK
VQIRIWGRPA AIAEGQGEYA LEKTGPILSF FERHYNTAYP LPKSDQVGLP DFNAGAMENW
GLVTYRENSL LYDNAYSSIG NKERVVTVIA HELAHQWFGN LVTLRWWNDL WLNEGFASYV
EYLGADSAEP TWDIKDLMVL NELYTVMATD ALTTSHPLTF REDEINTPAQ ISEVFDSIAY
SKGASVLRML SDFLTEDVFK EGLQSYLHDF SYNNTVYTDL WDHLQEAVNK NSVPLPDSIG
AIMDRWTLQM GFPVVTVNTL TGSVQQSHFL LDSNSTVERP SVFNYTWIVP ITWMTPSRTG
DRYWLVDVSA TNSDFSVGSS TWLLLNLNVS GYFRVNYNQE NWDQLLQQLS NNHQAIPVIN
RAQIIDDAFN LARAQQVSVT LALNTTRFLS GETAYMPWQA ALNNLQYFQL MFDRSEVFGA
MTKYIQKQVT PLFEYYRTAT NNWTAIPSAL MDQYNEINAI STACSYGIAE CQQLATALYQ
QWRQNVSNNP IAPNLRSAIY CSAVATGGEE VWDFIWERFL EAPVVSEADK LRTALTCSTE
TWILQRYLQY TIDPTKIRKQ DATSTINSIA SNVVGQPLAW DFIRSNWRTL FGQYGGGSFS
FSRLISAVTQ RFNTEFELKQ LEQFKADNQD IGFGSGTRAL EQALERTRTN INWVKENKEV
VHAWFRAETA SS


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