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Reviewed, UniProtKB/Swiss-Prot P81731 (AMPN_HELAM)

Last modified October 13, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aminopeptidase N
      Short name=AP-N
    EC=3.4.11.2
Alternative name(s):
    CryIA(C) receptor
OrganismHelicoverpa armigera (Cotton bollworm) (Heliothis armigera)
Taxonomic identifier29058 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeHeliothinaeHelicoverpa

Protein attributes

Sequence length10 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts as a receptor for B.thuringiensis Cry1Ac delta-endotoxin. Ref.1

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. Ref.1

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by the zinc-chelators 2,2-dipyridyl and 1,10-phenanthroline. Ref.1

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›10›10Aminopeptidase N
PRO_0000095086

Experimental info

Non-terminal residue101

Sequences

Sequence LengthMass (Da)Tools
P81731-1 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 05042EB87B11F1BB

FASTA101,093
        10 
GMYTHEGSDP 

« Hide

References

[1]"Aminopeptidase-N from the Helicoverpa armigera (Hubner) brush border membrane vesicles as a receptor of Bacillus thuringiensis crylac delta-endotoxin."
Ingle S.S., Trivedi N., Prasad R., Kuruvilla J., Rao K.K., Chhatpar H.S.
Curr. Microbiol. 43:255-259(2001) [PubMed: 11683359] [Abstract]
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
Tissue: Larval midgut.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.4.11.2. 39282.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_HELAM
AccessionPrimary (citable) accession number: P81731
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: October 13, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents