AMPN_CHICK
ID AMPN_CHICK Reviewed; 972 AA.
AC O57579; A0A1D5NWZ2; D2KKL5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Aminopeptidase Ey {ECO:0000303|PubMed:9734335};
DE EC=3.4.11.20 {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
DE AltName: Full=Aminopeptidase N {ECO:0000312|EMBL:ACZ95799.1};
GN Name=ANPEP; Synonyms=APDE;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 224-234; 296-363;
RP 378-405; 496-526 AND 954-966.
RC TISSUE=Egg yolk {ECO:0000269|PubMed:9734335}, and
RC Liver {ECO:0000269|PubMed:9734335};
RX PubMed=9734335; DOI=10.1016/s0305-0491(98)00012-1;
RA Midorikawa T., Abe R., Yamagata Y., Nakajima T., Ichishima E.;
RT "Isolation and characterization of cDNA encoding chicken egg yolk
RT aminopeptidase Ey.";
RL Comp. Biochem. Physiol. 119:513-520(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic kidney {ECO:0000312|EMBL:ACZ95799.1};
RA Xin Y., Ping W., Bo M.X.;
RT "Soluble high-expression and biological function of chicken aminopeptidase
RT N.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RA Ichishima E., Yamagata Y., Chiba H., Sawaguchi K., Tanaka T.;
RT "Soluble and bound forms of aminopeptidase in hen's egg yolk.";
RL Agric. Biol. Chem. 53:1867-1872(1989).
RN [5]
RP SUBUNIT.
RA Tanaka T., Oshida K., Ichishima E.;
RT "Electron microscopic analysis of dimeric form of aminopeptidase Ey from
RT hen's egg yolk.";
RL Agric. Biol. Chem. 55:2179-2181(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7684960; DOI=10.1016/0305-0491(93)90175-5;
RA Tanaka T., Ichishima E.;
RT "Substrate specificity of aminopeptidase Ey from hen's (Gallus domesticus)
RT egg yolk.";
RL Comp. Biochem. Physiol. 105:105-110(1993).
RN [7]
RP COFACTOR.
RX PubMed=8288037; DOI=10.1016/0020-711x(93)90528-m;
RA Tanaka T., Ichishima E.;
RT "Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme.";
RL Int. J. Biochem. 25:1681-1688(1993).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8205380; DOI=10.1016/0305-0491(94)90181-3;
RA Tanaka T., Ichishima E.;
RT "Inactivation of chemotactic peptides by aminopeptidase Ey from hen's
RT (Gallus gallus domesticus) egg yolk.";
RL Comp. Biochem. Physiol. 107B:533-538(1994).
CC -!- FUNCTION: Broad specificity aminopeptidase. Degrades a variety of
CC peptides possessing various N-terminal amino acids including
CC hydrophobic, basic and acidic amino acids. Preferentially hydrolyzes
CC small peptides consisting of 4 or 5 amino acids. Hydrolyzes the N-
CC terminal Xaa-Pro bonds in the chicken brain peptide Leu-Pro-Leu-Arg-
CC PheNH2, the substance P fragment Arg-Pro-Lys-Pro and the bradykinin
CC fragment Arg-Pro-Pro-Gly-Phe. Hydrolyzes the N-formylated peptides
CC fMet-Leu-Phe, fMet-Ala-Gly-Ser-Glu and fMet-Nle-Leu-Phe-Nle-Tyr-Lys,
CC but does not hydrolyze peptides with acetylation or pyroglutamic acid
CC at N-terminus. Does not hydrolyze large peptides such as complete
CC substance P, bradykinin or schistoFLRFamide.
CC {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380,
CC ECO:0000269|Ref.4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Differs from other aminopeptidases in broad specificity for
CC amino acids in the P1 position and the ability to hydrolyze peptides
CC of four or five residues that contain Pro in the P1' position.;
CC EC=3.4.11.20; Evidence={ECO:0000269|PubMed:7684960,
CC ECO:0000269|PubMed:8205380};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:8288037};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:8288037};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for Leu-Pro-Leu-Arg-PheNH2 {ECO:0000269|PubMed:7684960,
CC ECO:0000269|PubMed:8205380};
CC KM=1.23 mM for fMet-Leu-Phe {ECO:0000269|PubMed:7684960,
CC ECO:0000269|PubMed:8205380};
CC KM=1.53 mM for fMet-Ala-Gly-Ser-Glu {ECO:0000269|PubMed:7684960,
CC ECO:0000269|PubMed:8205380};
CC KM=1.72 mM for fMet-Nle-Leu-Phe-Nle-Tyr-Lys
CC {ECO:0000269|PubMed:7684960, ECO:0000269|PubMed:8205380};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|Ref.4}; Single-pass
CC type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also
CC found as a soluble form. {ECO:0000269|Ref.4}.
CC -!- TISSUE SPECIFICITY: Detected in the plasma and granule fractions of egg
CC yolk (at protein level). {ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000255}.
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DR EMBL; D87992; BAA24263.1; -; mRNA.
DR EMBL; GU223212; ACZ95799.1; -; mRNA.
DR EMBL; AADN04000131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_990192.1; NM_204861.1.
DR RefSeq; XP_015147557.1; XM_015292071.1.
DR AlphaFoldDB; O57579; -.
DR SMR; O57579; -.
DR STRING; 9031.ENSGALP00000040682; -.
DR MEROPS; M01.016; -.
DR PaxDb; O57579; -.
DR Ensembl; ENSGALT00000064511; ENSGALP00000044885; ENSGALG00000027501.
DR GeneID; 395667; -.
DR KEGG; gga:395667; -.
DR CTD; 290; -.
DR VEuPathDB; HostDB:geneid_395667; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000154876; -.
DR InParanoid; O57579; -.
DR OMA; KWFIFNI; -.
DR OrthoDB; 110058at2759; -.
DR PhylomeDB; O57579; -.
DR BRENDA; 3.4.11.20; 1306.
DR SABIO-RK; O57579; -.
DR PRO; PR:O57579; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000027501; Expressed in liver and 11 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CHAIN 2..972
FT /note="Aminopeptidase Ey"
FT /id="PRO_0000394749"
FT TOPO_DOM 2..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..972
FT /note="Extracellular"
FT REGION 33..72
FT /note="Cytosolic Ser/Thr-rich junction"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT REGION 37..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..967
FT /note="Metalloprotease"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT COMPBIAS 37..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 392
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 355..359
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 414
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 480
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P15144"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 764..771
FT /evidence="ECO:0000250"
FT DISULFID 801..837
FT /evidence="ECO:0000250"
FT CONFLICT 56..60
FT /note="Missing (in Ref. 1; BAA24263 and 2; ACZ95799)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="T -> K (in Ref. 2; ACZ95799)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="V -> A (in Ref. 2; ACZ95799)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> T (in Ref. 2; ACZ95799)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="D -> N (in Ref. 1; BAA24263 and 2; ACZ95799)"
FT /evidence="ECO:0000305"
FT CONFLICT 675..678
FT /note="QQVS -> HNVN (in Ref. 1; BAA24263)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="Q -> H (in Ref. 1; BAA24263)"
FT /evidence="ECO:0000305"
SQ 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
