Reviewed,
UniProtKB/Swiss-Prot P81731 (AMPN_HELAM)
Last modified
October 13, 2009.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aminopeptidase N Short name=AP-N EC=3.4.11.2 Alternative name(s): CryIA(C) receptor |
| Organism | Helicoverpa armigera (Cotton bollworm) (Heliothis armigera) |
| Taxonomic identifier | 29058 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Noctuoidea › Noctuidae › Heliothinae › Helicoverpa |
Protein attributes
| Sequence length | 10 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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
| Keywords | |
|---|---|
| Ligand | Zinc |
| Molecular function | Aminopeptidase Hydrolase Metalloprotease Protease |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activityInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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 | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.4.11.2. 39282. |
Family and domain databases | |
| InterPro | IPR006025. Pept_M_Zn_BS. [Graphical view] |
| PROSITE | PS00142. ZINC_PROTEASE. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPN_HELAM | ||||||||
| Accession | Primary (citable) accession number: P81731 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


