AMPN_PLUXY
ID AMPN_PLUXY Reviewed; 946 AA.
AC P91887;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Aminopeptidase N;
DE Short=AP-N;
DE EC=3.4.11.2;
DE AltName: Full=Apn1;
DE AltName: Full=Microsomal aminopeptidase;
DE Flags: Precursor;
GN Name=APN1;
OS Plutella xylostella (Diamondback moth) (Plutella maculipennis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Yponomeutoidea;
OC Plutellidae; Plutella.
OX NCBI_TaxID=51655;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X97878; CAA66467.1; -; mRNA.
DR AlphaFoldDB; P91887; -.
DR SMR; P91887; -.
DR MEROPS; M01.030; -.
DR BRENDA; 3.4.11.2; 4920.
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; Disulfide bond; Glycoprotein; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Metal-binding; Metalloprotease; Protease;
KW Signal; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..?
FT /note="Aminopeptidase N"
FT /id="PRO_0000026743"
FT PROPEP ?..946
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026744"
FT ACT_SITE 345
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 308..312
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 429
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 605
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 715..722
FT /evidence="ECO:0000250"
FT DISULFID 751..787
FT /evidence="ECO:0000250"
SQ SEQUENCE 946 AA; 106578 MW; 1DFD81A364067BFB CRC64;
MRLLICLTLL GLVCGNPVQL TDNSIALQNT YDNYVLPGES FPTFYDVQLF FDPEYEASFN
GTVAIRVVPR IATQEIVLHA MEMEILSIRA YSDLPSDDNL NENLFSSYTL ATDDTHLLKI
QFTRVLDALQ PITVEISYSA QYAPNMFGVY VSRYVENGAT VSLVTSQLQP TFARRAFPCY
DEPALKAVFR TTIYAPPAYN VVETNMPLRT DSLKSDRPGF TKHEFQDTLV MSSYLLAYLV
SKFDYISNEN NPTYDKSMKV FSRPGTQNTA EFALDFGQKN MVELEKYTEF PYAFPKIDKV
AVPDFAAGAM ENWGLVIYRE IALLVQEGVT TTSTLQGIGR IISHENTHQW FGNEVGPDSW
TYTWLNEGFA NFFESFATDL VLPEWRMMDQ FVINMQNVFQ SDAVLSVNPI TFEVRTPSQI
LGTFNSVAYQ KSGSVIRMMQ HFLTPEIFRK SLALYISRMS RKAAKPTDLF EAIQEVVDAS
DHSIRWRLSI IMNRWTQQGG FPVVTVRRSA PSAQSFVITQ RRFLTDSTQE SNTVWNVPLN
WVLSTDVNFN DTRPMAWLPP QLAAEAVQVP GLQNAEWFIV NKQQTGYYRV NYDPENWRAL
AKVLNDTHEI IHLLNRAQLI DDSFNLARNG RLDYSLAFDL SRYLVQERDY IPWAAANAAF
NYLNSVLSGS SVHPLFQEYL LFLTAPLYQR LGFNAATGEE HVTPFHRNII LNINCLHGNE
DCVSTAETLL QNFRDNPTQT LNPDIQTTVF CSGLRGGDVD NFNFLWARYT ATQDSSEQSI
LLNALGCTSN ADRRDFLFSQ VIASDSQVRE QDRHSVLVSA INSGPDNMNA ALDFVLENFA
NIQPNVQGLT GTTNILNAFA RTLTTQEHAN KIDEFSNKYA NVFTAGEMAS VAAIKENIAA
SITWNSQNAA TVEAWLRKNF GTDGASTVSA SITIIISAMV AIYNIL
