ID   AMPN_MANSE              Reviewed;         942 AA.
AC   P91885;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   02-SEP-2026, entry version 119.
DE   RecName: Full=Aminopeptidase N;
DE            Short=AP-N;
DE            EC=3.4.11.2;
DE   AltName: Full=Apn2;
DE   AltName: Full=Microsomal aminopeptidase;
DE   Flags: Precursor;
GN   Name=APN2;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 68-72; 187-199; 460-475;
RP   602-612; 693-703; 875-884 AND 893-908, AND CHARACTERIZATION.
RC   TISSUE=Midgut;
RX   PubMed=9342226; DOI=10.1111/j.1432-1033.1997.t01-1-00748.x;
RA   Denolf P.H., Hendrickx K., van Damme J., Jansens S., Peferoen M.,
RA   Degheele D., van Rie J.;
RT   "Cloning and characterization of Manduca sexta and Plutella xylostella
RT   midgut aminopeptidase N related to Bacillus thuringiensis toxin-binding
RT   proteins.";
RL   Eur. J. Biochem. 248:748-761(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Denolf P.H.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC         peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC         amino acids including Pro (slow action). When a terminal hydrophobic
CC         residue is followed by a prolyl residue, the two may be released as
CC         an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Binds to CRY1AB5.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; X97877; CAA66466.2; -; mRNA.
DR   AlphaFoldDB; P91885; -.
DR   SMR; P91885; -.
DR   MEROPS; M01.030; -.
DR   GlyCosmos; P91885; 5 sites, No reported glycans.
DR   EnsemblMetazoa; XM_030176857.2; XP_030032717.1; LOC115449131.
DR   OrthoDB; 10031169at2759; -.
DR   BRENDA; 3.4.11.2; 3173.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016285; F:alanyl aminopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:TreeGrafter.
DR   GO; GO:0042277; F:peptide binding; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043171; P:peptide catabolic process; IEA:TreeGrafter.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd09601; M1_APN-Q_like; 1.
DR   FunFam; 1.25.50.20:FF:000001; Aminopeptidase; 1.
DR   FunFam; 2.60.40.1910:FF:000008; Aminopeptidase; 1.
DR   FunFam; 1.10.390.10:FF:000013; Aminopeptidase N; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 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; IPR050344; Peptidase_M1_aminopeptidases.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF290; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
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; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Signal; Zinc.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..?
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000026741"
FT   PROPEP          ?..942
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026742"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         304..308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         340
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   SITE            425
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        601
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        678
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        711..718
FT                   /evidence="ECO:0000250"
FT   DISULFID        747..783
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   942 AA;  106780 MW;  EFD4D906600E17B9 CRC64;
     MYSLIFLALI GAAFGVPLST NEDSTRNQNL AALYVLPQTS YPTFYDVRLF IDPGYTEAFH
     GNVSIRIIPN INIDQITIHA MAMRIDSIRV VSDVNPNEDL FSDFTLATDD THLLTIRLTR
     NITALQPHVI HIDYVAQYAD DMFGVYVSTY EENGRTVNLV TSQLQPTFAR RAFPCYDEPA
     LKAVFRTTIY APAAYATVRS NTPERRDSLK PNEPGYVKHE FEDTLVMSTY LIAYLVSNFN
     YIENSQNPIY PIPFRVYSRP GTQNTAEFAL EFGQQNMIAL EEYTEFPYAF PKIDKAAVPD
     FAAGAMENWG LVIYREVALL VREGVTTTSV KQNIGRIICH ENTHMWFGNE VGPMSWTYTW
     LNEGFANFFE NYATDFVRPQ WRMMDQFVIA MQNVFQSDAV LSVNPMTHPV YTPSQIIGTF
     NAVAYQKSGS VIRMLQHFMT PEIFRRGLVI YIKANSRAAA APSDLYVALQ QALDESSHRI
     PKPISTIMTE WSTQGGFPVL TVRRTAPNAD SVFVAQERYL TDRSLTSTDR WHVPVNWVIS
     SNVNFSDTSP QAWILPTFPA TAVDVPGLSN ADWYIFNKQQ TGYYRVNYDV ENWVALARVL
     NNSHEIIHVL NRAQIVDDAF NLARNGRLHY KNAFEISRYL EMEKDYIPWA AANPAFNYLD
     IVLSGANSYN LYRYYLLNLT APMFEDLGFD VKSGEEFVTP YHRNIILDIN CRFGNQRCIS
     RAQEILQAFK NNPNQRPNPD IQTLVYCSSL RAGNVENFNF LWNMYLGTSD SSEQSILLSA
     LGCTSNAERR NFYLNQIIDD NSAVREQDRH SIAVSVINSS PEGMNVALDF VVENFHRIQP
     RVQALTGTTN ILNTFARRLT TSAHNEKIDE LVRRHESIFS AGERASIAAI RENIAASIAW
     SNSNAGIVEN WLKENYGPPS GAKSLTAGLL VLISLFVAIF NH
//