ID AMPM_MANSE Reviewed; 990 AA.
AC Q11001;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 13-SEP-2023, entry version 98.
DE RecName: Full=Membrane alanyl aminopeptidase;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase N-like protein;
DE AltName: Full=CryIA(C) receptor;
DE Flags: Precursor; Fragment;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Midgut;
RX PubMed=7629076; DOI=10.1074/jbc.270.30.17765;
RA Knight P.J.K., Knowles B.H., Ellar D.J.;
RT "Molecular cloning of an insect aminopeptidase N that serves as a receptor
RT for Bacillus thuringiensis CryIA(c) toxin.";
RL J. Biol. Chem. 270:17765-17770(1995).
CC -!- FUNCTION: Binds to the B.thuringiensis toxin, CryIA(C).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Midgut brush-border membrane.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; X89081; CAA61452.1; -; mRNA.
DR EMBL; AB007039; BAA32476.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11001; -.
DR SMR; Q11001; -.
DR MEROPS; M01.013; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 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; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF284; 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; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Protease; Signal; Zinc.
FT SIGNAL <1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..35
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026748"
FT CHAIN 36..968
FT /note="Membrane alanyl aminopeptidase"
FT /id="PRO_0000026749"
FT PROPEP 969..990
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026750"
FT ACT_SITE 358
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 321..325
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 444
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 968
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 990 AA; 111294 MW; EDF6E63C398C11D8 CRC64;
FTIFLGVALL QGVLTLSPIP VPEEEWAEFS RMLRDPSYRL PTTTRPRHYA VTLTPYFDVV
PAGVSGLTTF SFDGEVTIYI SPTQANVNEI VLHCNDLTIQ SLRVTYVSGN SEVDITATGQ
TFTCEMPYSF LRIRTSTPLV MNQEYIIRST FRGNLQTNMR GFYRSWYVDR TGKRWMATTQ
FQPGHARQAF PCYDEPGFKA TFDITMNREA DFSPTISNMP IRATTTLTNG RISETFFTTP
LTSTYLLAFI VSHYQVISNN NNAARPFRIY ARNNVGSQGD WSLEMGEKLL LAMENYTAIP
YYTMAQNLDM KQAAIPDFSA GAMENWGLLT YREALILYDP LNSNHHYRQR VANIVSHEIA
HMWFGNLVTC AWWDNLWLNE GFARFSQYYL TATVDPELGY EIRFIPEQLQ VAMFSDSVDS
AHALTDTSVN DPVAVSAHFS TITYARGAAI LRMTQHLLSY DTFVKGLRQY LRARQFDVAE
PYHLFSALDA AAAEDNALAA YRGITIDAYF RTWSEKAGHP LLSVTVDHES GRMTLVQARW
ERNTGVSRFP GLWHIPITWT RAGAPDFENL KPSQVMTGQS LVIDRGTRGQ EWVIFNKQVS
GFYRVNYDNT TWGLITRALR SANRTVIHEL SRSQIVDDVF QLARSGVMSY QRALNILSYL
RFEDAYAPWL SAISGFNWVI RRFAHDAANL QTLQNQIIGL SEAVVARLGF TEVSGGTYMT
DLQRLHVMQF LCNVGHQQCI DAGRQNFLNW RNGSFIPANM RPWVYCTGLR YGSAEDFNYF
WNRYIVEDLS NEKVVMLEAA GCTRDQASLE KFLNAIVSGN DDVRPQDHSS ALSSAITSND
VNTMRAFDWL TKNVDQITRT LGSITSPLNT ITSRLLTEAQ MTQVQTWLDA NRNTIGAAYN
TGVNGIATSR ANLQWSANRM SEFLRFFETG FVDDVPSEAT TVAPPAETTV TPSTFPPTVA
PATTPAPGSG NIAALSVVSL LVTLAINMVA
//
