ID   AMPN_HELAM              Reviewed;          10 AA.
AC   P81731;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Aminopeptidase N;
DE            Short=AP-N;
DE            EC=3.4.11.2;
DE   AltName: Full=CryIA(C) receptor;
DE   Flags: Fragment;
OS   Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Helicoverpa.
OX   NCBI_TaxID=29058;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   TISSUE=Larval midgut;
RX   PubMed=11683359; DOI=10.1007/s002840010297;
RA   Ingle S.S., Trivedi N., Prasad R., Kuruvilla J., Rao K.K., Chhatpar H.S.;
RT   "Aminopeptidase-N from the Helicoverpa armigera (Hubner) brush border
RT   membrane vesicles as a receptor of Bacillus thuringiensis crylac delta-
RT   endotoxin.";
RL   Curr. Microbiol. 43:255-259(2001).
CC   -!- FUNCTION: Acts as a receptor for B.thuringiensis Cry1Ac delta-
CC       endotoxin. {ECO:0000269|PubMed:11683359}.
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         Evidence={ECO:0000269|PubMed:11683359};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by the zinc-chelators 2,2-dipyridyl and
CC       1,10-phenanthroline. {ECO:0000269|PubMed:11683359}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Metalloprotease;
KW   Protease; Zinc.
FT   CHAIN           1..>10
FT                   /note="Aminopeptidase N"
FT                   /id="PRO_0000095086"
FT   NON_TER         10
SQ   SEQUENCE   10 AA;  1093 MW;  05042EB87B11F1BB CRC64;
     GMYTHEGSDP
//