Q7Q2T8 · AMPN_ANOGA
- ProteinAminopeptidase N
- GeneAPN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1020 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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
Note: Binds 1 zinc ion per subunit.
Biotechnology
Potential vaccine candidate (PubMed:26075520).
Antibodies against ANP1 prevent parasite P.falciparum development in the mosquito midgut (PubMed:26075520).
Antibodies against ANP1 prevent parasite P.falciparum development in the mosquito midgut (PubMed:26075520).
pH Dependence
Optimum pH is 6-7.5.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 199 | substrate | |||
Binding site | 330 | substrate | |||
Binding site | 331 | substrate | |||
Binding site | 333 | substrate | |||
Binding site | 366 | substrate | |||
Binding site | 366 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 367 | ||||
Binding site | 370 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 389 | substrate | |||
Binding site | 389 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Site | 452 | Transition state stabilizer | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular space | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | identical protein binding | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | metallopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | zinc ion binding | |
Biological Process | peptide catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAminopeptidase N
- EC number
- Short namesAnAPN1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Nematocera > Culicoidea > Culicidae > Anophelinae > Anopheles
Accessions
- Primary accessionQ7Q2T8
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, lipidation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-19 | ||||
Chain | PRO_5014588085 | 20-997 | Aminopeptidase N | ||
Disulfide bond | 736↔743 | ||||
Disulfide bond | 772↔808 | ||||
Lipidation | 997 | GPI-anchor amidated aspartate | |||
Propeptide | PRO_0000457487 | 998-1020 | Removed in mature form | ||
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q7Q2T8 | APN1 Q7Q2T8 | 2 | EBI-16161420, EBI-16161420 |
Protein-protein interaction databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,020
- Mass (Da)113,244
- Last updated2007-10-23 v4
- MD5 Checksum81AE84BB1BA6AADFBC8AAA53DD559AE6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAAB01008968 EMBL· GenBank· DDBJ | EAA13235.4 EMBL· GenBank· DDBJ | Genomic DNA |