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P91885 (AMPN_MANSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

Short name=AP-N
EC=3.4.11.2
Alternative name(s):
Apn2
Microsomal aminopeptidase
Gene names
Name:APN2
OrganismManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifier7130 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-anchorGPI-anchor.

Sequence similarities

Belongs to the peptidase M1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – ?Aminopeptidase NPRO_0000026741
Propeptide? – 942Removed in mature form PotentialPRO_0000026742

Regions

Region304 – 3085Substrate binding By similarity

Sites

Active site3411Proton acceptor By similarity
Metal binding3401Zinc; catalytic By similarity
Metal binding3441Zinc; catalytic By similarity
Metal binding3631Zinc; catalytic By similarity
Site4251Transition state stabilizer By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation6011N-linked (GlcNAc...) Potential
Glycosylation6781N-linked (GlcNAc...) Potential
Disulfide bond711 ↔ 718 By similarity
Disulfide bond747 ↔ 783 By similarity

Sequences

Sequence LengthMass (Da)Tools
P91885 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: EFD4D906600E17B9

FASTA942106,780
        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 

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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] [Europe PMC] [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

ProteinModelPortalP91885.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM01.030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_MANSE
AccessionPrimary (citable) accession number: P91885
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: February 19, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries