Reviewed, UniProtKB/Swiss-Prot P91885 (AMPN_MANSE)

Names and origin

Protein names

Recommended name:
    Aminopeptidase N
      Short name=AP-N
    EC=3.4.11.2
Alternative name(s):
    Apn2
    Microsomal aminopeptidase

Gene names

Name:

APN2

Organism

Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)

Taxonomic identifier

7130 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Sphingidae › Sphinginae › Sphingini › Manduca

Protein attributes

Sequence length	942 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.
Subunit structure	Binds to CRY1AB5.
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
Technical term	Direct protein sequencing
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_0000026741
	Propeptide	? – 942		Removed in mature form Potential		PRO_0000026742
Sites
	Active site	341	1	By similarity
	Active site	425	1	Proton donor Potential
	Metal binding	340	1	Zinc; catalytic By similarity
	Metal binding	344	1	Zinc; catalytic By similarity
	Metal binding	363	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	62	1	N-linked (GlcNAc...) Potential
	Glycosylation	121	1	N-linked (GlcNAc...) Potential
	Glycosylation	544	1	N-linked (GlcNAc...) Potential
	Glycosylation	601	1	N-linked (GlcNAc...) Potential
	Glycosylation	678	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	P91885-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: EFD4D906600E17B9	FASTA	942	106,780
	10 20 30 40 50 60 MYSLIFLALI GAAFGVPLST NEDSTRNQNL AALYVLPQTS YPTFYDVRLF IDPGYTEAFH 70 80 90 100 110 120 GNVSIRIIPN INIDQITIHA MAMRIDSIRV VSDVNPNEDL FSDFTLATDD THLLTIRLTR 130 140 150 160 170 180 NITALQPHVI HIDYVAQYAD DMFGVYVSTY EENGRTVNLV TSQLQPTFAR RAFPCYDEPA 190 200 210 220 230 240 LKAVFRTTIY APAAYATVRS NTPERRDSLK PNEPGYVKHE FEDTLVMSTY LIAYLVSNFN 250 260 270 280 290 300 YIENSQNPIY PIPFRVYSRP GTQNTAEFAL EFGQQNMIAL EEYTEFPYAF PKIDKAAVPD 310 320 330 340 350 360 FAAGAMENWG LVIYREVALL VREGVTTTSV KQNIGRIICH ENTHMWFGNE VGPMSWTYTW 370 380 390 400 410 420 LNEGFANFFE NYATDFVRPQ WRMMDQFVIA MQNVFQSDAV LSVNPMTHPV YTPSQIIGTF 430 440 450 460 470 480 NAVAYQKSGS VIRMLQHFMT PEIFRRGLVI YIKANSRAAA APSDLYVALQ QALDESSHRI 490 500 510 520 530 540 PKPISTIMTE WSTQGGFPVL TVRRTAPNAD SVFVAQERYL TDRSLTSTDR WHVPVNWVIS 550 560 570 580 590 600 SNVNFSDTSP QAWILPTFPA TAVDVPGLSN ADWYIFNKQQ TGYYRVNYDV ENWVALARVL 610 620 630 640 650 660 NNSHEIIHVL NRAQIVDDAF NLARNGRLHY KNAFEISRYL EMEKDYIPWA AANPAFNYLD 670 680 690 700 710 720 IVLSGANSYN LYRYYLLNLT APMFEDLGFD VKSGEEFVTP YHRNIILDIN CRFGNQRCIS 730 740 750 760 770 780 RAQEILQAFK NNPNQRPNPD IQTLVYCSSL RAGNVENFNF LWNMYLGTSD SSEQSILLSA 790 800 810 820 830 840 LGCTSNAERR NFYLNQIIDD NSAVREQDRH SIAVSVINSS PEGMNVALDF VVENFHRIQP 850 860 870 880 890 900 RVQALTGTTN ILNTFARRLT TSAHNEKIDE LVRRHESIFS AGERASIAAI RENIAASIAW 910 920 930 940 SNSNAGIVEN WLKENYGPPS GAKSLTAGLL VLISLFVAIF NH

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], PROTEIN SEQUENCE OF 68-72; 187-199; 460-475; 602-612; 693-703; 875-884 AND 893-908, CHARACTERIZATION. Tissue: Midgut.

[2]

Denolf P.H. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97877 mRNA. Translation: CAA66466.2.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M01.030.
Enzyme and pathway databases
BRENDA	3.4.11.2. 15145.
Family and domain databases
InterPro	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_MANSE

Accession

Primary (citable) accession number: P91885

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 30, 2000
Last modified:	November 24, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)