Reviewed, UniProtKB/Swiss-Prot P91887 (AMPN_PLUXY)

Names and origin

Protein names

Recommended name:
    Aminopeptidase N
      Short name=AP-N
    EC=3.4.11.2
Alternative name(s):
    Apn1
    Microsomal aminopeptidase

Gene names

Name:

APN1

Organism

Plutella xylostella (Diamondback moth)

Taxonomic identifier

51655 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Yponomeutoidea › Plutellidae › Plutella

Protein attributes

Sequence length	946 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Sequence similarities	Belongs to the peptidase M1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	GPI-anchor Glycoprotein Lipoprotein
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Potential
	Chain	16 – ?		Aminopeptidase N		PRO_0000026743
	Propeptide	? – 946		Removed in mature form Potential		PRO_0000026744
Sites
	Active site	345	1	By similarity
	Active site	429	1	Proton donor Potential
	Metal binding	344	1	Zinc; catalytic By similarity
	Metal binding	348	1	Zinc; catalytic By similarity
	Metal binding	367	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	60	1	N-linked (GlcNAc...) Potential
	Glycosylation	550	1	N-linked (GlcNAc...) Potential
	Glycosylation	605	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P91887-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 1DFD81A364067BFB	FASTA	946	106,578
	10 20 30 40 50 60 MRLLICLTLL GLVCGNPVQL TDNSIALQNT YDNYVLPGES FPTFYDVQLF FDPEYEASFN 70 80 90 100 110 120 GTVAIRVVPR IATQEIVLHA MEMEILSIRA YSDLPSDDNL NENLFSSYTL ATDDTHLLKI 130 140 150 160 170 180 QFTRVLDALQ PITVEISYSA QYAPNMFGVY VSRYVENGAT VSLVTSQLQP TFARRAFPCY 190 200 210 220 230 240 DEPALKAVFR TTIYAPPAYN VVETNMPLRT DSLKSDRPGF TKHEFQDTLV MSSYLLAYLV 250 260 270 280 290 300 SKFDYISNEN NPTYDKSMKV FSRPGTQNTA EFALDFGQKN MVELEKYTEF PYAFPKIDKV 310 320 330 340 350 360 AVPDFAAGAM ENWGLVIYRE IALLVQEGVT TTSTLQGIGR IISHENTHQW FGNEVGPDSW 370 380 390 400 410 420 TYTWLNEGFA NFFESFATDL VLPEWRMMDQ FVINMQNVFQ SDAVLSVNPI TFEVRTPSQI 430 440 450 460 470 480 LGTFNSVAYQ KSGSVIRMMQ HFLTPEIFRK SLALYISRMS RKAAKPTDLF EAIQEVVDAS 490 500 510 520 530 540 DHSIRWRLSI IMNRWTQQGG FPVVTVRRSA PSAQSFVITQ RRFLTDSTQE SNTVWNVPLN 550 560 570 580 590 600 WVLSTDVNFN DTRPMAWLPP QLAAEAVQVP GLQNAEWFIV NKQQTGYYRV NYDPENWRAL 610 620 630 640 650 660 AKVLNDTHEI IHLLNRAQLI DDSFNLARNG RLDYSLAFDL SRYLVQERDY IPWAAANAAF 670 680 690 700 710 720 NYLNSVLSGS SVHPLFQEYL LFLTAPLYQR LGFNAATGEE HVTPFHRNII LNINCLHGNE 730 740 750 760 770 780 DCVSTAETLL QNFRDNPTQT LNPDIQTTVF CSGLRGGDVD NFNFLWARYT ATQDSSEQSI 790 800 810 820 830 840 LLNALGCTSN ADRRDFLFSQ VIASDSQVRE QDRHSVLVSA INSGPDNMNA ALDFVLENFA 850 860 870 880 890 900 NIQPNVQGLT GTTNILNAFA RTLTTQEHAN KIDEFSNKYA NVFTAGEMAS VAAIKENIAA 910 920 930 940 SITWNSQNAA TVEAWLRKNF GTDGASTVSA SITIIISAMV AIYNIL

References

[1]

"Cloning and characterization of Manduca sexta and Plutella xylostella midgut aminopeptidase N related to Bacillus thuringiensis toxin-binding proteins." Denolf P.H., Hendrickx K., van Damme J., Jansens S., Peferoen M., Degheele D., van Rie J. Eur. J. Biochem. 248:748-761(1997) [PubMed: 9342226] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Midgut.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X97878 mRNA. Translation: CAA66467.1.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M01.030.
Enzyme and pathway databases
BRENDA	3.4.11.2. 39095.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR001930. Peptidase_M1. IPR014782. Peptidase_M1_N. [Graphical view]
PANTHER	PTHR11533. Peptidase_M1. 1 hit.
Pfam	PF01433. Peptidase_M1. 1 hit. [Graphical view]
PRINTS	PR00756. ALADIPTASE.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMPN_PLUXY

Accession

Primary (citable) accession number: P91887

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	October 13, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)