AMPM_BOMMO
ID AMPM_BOMMO Reviewed; 26 AA.
AC P81495;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Membrane alanyl aminopeptidase;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase N-like protein;
DE AltName: Full=CryIA(A) receptor;
DE Flags: Fragments;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=Kinshu X Showa; TISSUE=Midgut;
RX PubMed=9219522; DOI=10.1111/j.1432-1033.1997.t01-1-00652.x;
RA Yaoi K., Kadotani T., Kuwana H., Shinkawa A., Takahashi T., Iwahana H.,
RA Sato R.;
RT "Aminopeptidase N from Bombyx mori as a candidate for the receptor of
RT Bacillus thuringiensis Cry1Aa toxin.";
RL Eur. J. Biochem. 246:652-657(1997).
CC -!- FUNCTION: Binds to the B.thuringiensis toxin, CryIA(A).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- TISSUE SPECIFICITY: Midgut brush-border membrane.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR AlphaFoldDB; P81495; -.
DR MEROPS; M01.A13; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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; Reference proteome; Zinc.
FT CHAIN 1..>26
FT /note="Membrane alanyl aminopeptidase"
FT /id="PRO_0000095099"
FT NON_CONS 15..16
FT /evidence="ECO:0000305"
FT NON_TER 26
SQ SEQUENCE 26 AA; 2857 MW; D61382774BE787A7 CRC64;
DPAFRLPTTT RPRHYQAAIP DFSAGA