AMPM_HELVI
ID AMPM_HELVI Reviewed; 1009 AA.
AC Q11000;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Membrane alanyl aminopeptidase;
DE EC=3.4.11.-;
DE AltName: Full=Aminopeptidase N-like protein;
DE AltName: Full=BTBP1;
DE AltName: Full=CryIA(C) receptor;
DE Flags: Precursor;
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 53-63.
RC TISSUE=Midgut;
RX PubMed=7592988; DOI=10.1074/jbc.270.45.27277;
RA Gill S.S., Cowles E.A., Francis V.;
RT "Identification, isolation, and cloning of a Bacillus thuringiensis CryIAc
RT toxin-binding protein from the midgut of the lepidopteran insect Heliothis
RT virescens.";
RL J. Biol. Chem. 270:27277-27282(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 -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; U35096; AAC46929.1; -; mRNA.
DR PIR; T18533; T18533.
DR AlphaFoldDB; Q11000; -.
DR SMR; Q11000; -.
DR MEROPS; M01.013; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.10.390.10; -; 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; 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..52
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:7592988"
FT /id="PRO_0000026745"
FT CHAIN 53..987
FT /note="Membrane alanyl aminopeptidase"
FT /id="PRO_0000026746"
FT PROPEP 988..1009
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026747"
FT REGION 955..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 338..342
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 460
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 987
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1009 AA; 113361 MW; CEBC1CB9D496AAA2 CRC64;
MAAIKLLVLS LACACVIAHS PIPPASRTIF LDERLEGGAF ENIDAFENIE LSNVVASPYR
LPTTTVPTHY KILWIIDIHQ PVQTYSGNVV ITLHATQAQV NEIVIHSDHM TLSSVVLRQG
DTVIPTTPTA QPEYHFLRVK LNDGYLAYNA DNAVLYTLSI DFTAPMRDDM YGIYNSWYRN
LPDDANVRWM ATTQFQATAA RYAFPCYDEP GFKAKFDVTI RRPVGYSSWF CTRQKGSGPS
TVAGYEEDEY HTTPTMSTYL LALIVSEYTS LPATNAAGEI LHEVIARPGA INNGQAVYAQ
RVGQALLAEM SDHTGFDFYA QDPNLKMTQA AIPDFGAGAM ENWGLLTYRE AYLLYDEQHT
NSYFKQIIAY ILSHEIAHMW FGNLVTNAWW DVLWLNEGFA RYYQYFLTAW VEDLGLATRF
INEQVHASLL SDSSIYAHPL TNPGVGSPAA VSAMFSTVTY NKGASIIRMT EHLLGFDVHR
TGLRNYLKDL AYKTAQPIDL FTALESAGNQ AGALSAYGSD FDFVKYYESW TEQPGHPVLN
VQINHQTGQM TITQRRFDID TGHSVQNRNY IIPITFTTGA NPSFDNTKPS HIISKGVTVI
DRGVVGDYWT IFNIQQTGFY RVNYDDYTWN LIVLALRGAD REKIHEYNRA QIVNDVFQFA
RSGLMTYQRA LNILSFLEFE TEYAPWVAAI TGFNWLRNRL VGKPQLDELN EKIVQWSSKV
MGELTYMPTE GEPFMRSYLR WQLAPVMCNL NVPACRAGAR AIFEDLRVFG HEVPVDSRNW
VYCNALRDGG AQEFNFLYNR FKSHNVYTEK IVLLQTLGCT SHVESLNTLL TDIVTPNQMI
RPQDYTTAFN TAVSGNEVNT RLVWNYIQAN LQLVFNAFAS PRTPLSYIAA RLRTVEEVVE
YQTWLNTTAI QSALGTNYNA IYGDSVATYN SILWVSTIED SLSTYLTNGN DVIEPSTSTT
STTAAPTTVT QPTITEPSTP TLPELTDSAM TSFASLFIIS LGAILHLIL
