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P81731

- AMPN_HELAM

UniProt

P81731 - AMPN_HELAM

Protein

Aminopeptidase N

Gene
N/A
Organism
Helicoverpa armigera (Cotton bollworm) (Heliothis armigera)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

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

    Catalytic activityi

    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.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

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

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminopeptidase N (EC:3.4.11.2)
    Short name:
    AP-N
    Alternative name(s):
    CryIA(C) receptor
    OrganismiHelicoverpa armigera (Cotton bollworm) (Heliothis armigera)
    Taxonomic identifieri29058 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaNoctuidaeHeliothinaeHelicoverpa

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›10›10Aminopeptidase NPRO_0000095086

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Sequencei

    Sequence statusi: Fragment.

    P81731-1 [UniParc]FASTAAdd to Basket

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    GMYTHEGSDP                                               10
    Length:10
    Mass (Da):1,093
    Last modified:May 30, 2000 - v1
    Checksum:i05042EB87B11F1BB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei10 – 101

    Cross-referencesi

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
      Tissue: Larval midgut.

    Entry informationi

    Entry nameiAMPN_HELAM
    AccessioniPrimary (citable) accession number: P81731
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 54 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3