AMPN_MANSE
ID AMPN_MANSE Reviewed; 942 AA.
AC P91885;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Aminopeptidase N;
DE Short=AP-N;
DE EC=3.4.11.2;
DE AltName: Full=Apn2;
DE AltName: Full=Microsomal aminopeptidase;
DE Flags: Precursor;
GN Name=APN2;
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], PROTEIN SEQUENCE OF 68-72; 187-199; 460-475;
RP 602-612; 693-703; 875-884 AND 893-908, 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).
RN [2]
RP SEQUENCE REVISION.
RA Denolf P.H.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Binds to CRY1AB5.
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; X97877; CAA66466.2; -; mRNA.
DR AlphaFoldDB; P91885; -.
DR SMR; P91885; -.
DR MEROPS; M01.030; -.
DR BRENDA; 3.4.11.2; 3173.
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; Disulfide bond;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW Metalloprotease; Protease; Signal; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..?
FT /note="Aminopeptidase N"
FT /id="PRO_0000026741"
FT PROPEP ?..942
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026742"
FT ACT_SITE 341
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
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 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT SITE 425
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 711..718
FT /evidence="ECO:0000250"
FT DISULFID 747..783
FT /evidence="ECO:0000250"
SQ SEQUENCE 942 AA; 106780 MW; EFD4D906600E17B9 CRC64;
MYSLIFLALI GAAFGVPLST NEDSTRNQNL AALYVLPQTS YPTFYDVRLF IDPGYTEAFH
GNVSIRIIPN INIDQITIHA MAMRIDSIRV VSDVNPNEDL FSDFTLATDD THLLTIRLTR
NITALQPHVI HIDYVAQYAD DMFGVYVSTY EENGRTVNLV TSQLQPTFAR RAFPCYDEPA
LKAVFRTTIY APAAYATVRS NTPERRDSLK PNEPGYVKHE FEDTLVMSTY LIAYLVSNFN
YIENSQNPIY PIPFRVYSRP GTQNTAEFAL EFGQQNMIAL EEYTEFPYAF PKIDKAAVPD
FAAGAMENWG LVIYREVALL VREGVTTTSV KQNIGRIICH ENTHMWFGNE VGPMSWTYTW
LNEGFANFFE NYATDFVRPQ WRMMDQFVIA MQNVFQSDAV LSVNPMTHPV YTPSQIIGTF
NAVAYQKSGS VIRMLQHFMT PEIFRRGLVI YIKANSRAAA APSDLYVALQ QALDESSHRI
PKPISTIMTE WSTQGGFPVL TVRRTAPNAD SVFVAQERYL TDRSLTSTDR WHVPVNWVIS
SNVNFSDTSP QAWILPTFPA TAVDVPGLSN ADWYIFNKQQ TGYYRVNYDV ENWVALARVL
NNSHEIIHVL NRAQIVDDAF NLARNGRLHY KNAFEISRYL EMEKDYIPWA AANPAFNYLD
IVLSGANSYN LYRYYLLNLT APMFEDLGFD VKSGEEFVTP YHRNIILDIN CRFGNQRCIS
RAQEILQAFK NNPNQRPNPD IQTLVYCSSL RAGNVENFNF LWNMYLGTSD SSEQSILLSA
LGCTSNAERR NFYLNQIIDD NSAVREQDRH SIAVSVINSS PEGMNVALDF VVENFHRIQP
RVQALTGTTN ILNTFARRLT TSAHNEKIDE LVRRHESIFS AGERASIAAI RENIAASIAW
SNSNAGIVEN WLKENYGPPS GAKSLTAGLL VLISLFVAIF NH
