Q8VCT3 · AMPB_MOUSE
- ProteinAminopeptidase B
- GeneRnpep
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids650 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg0-Leu-enkephalin, Arg0-Met-enkephalin and Arg-1-Lys0-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity).
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 298-302 | substrate | ||||
Sequence: GGMEN | ||||||
Binding site | 325 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 326 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 329 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 348 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 414 | Transition state stabilizer | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | external side of plasma membrane | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | plasma membrane | |
Cellular Component | secretory granule | |
Molecular Function | aminopeptidase activity | |
Molecular Function | cobalt ion binding | |
Molecular Function | copper ion binding | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | zinc ion binding | |
Biological Process | negative regulation of blood pressure | |
Biological Process | protein processing | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAminopeptidase B
- EC number
- Short namesAP-B
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8VCT3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000095089 | 1-650 | Aminopeptidase B | |||
Sequence: MESGGPGNYSAAARRPLHSAQAVDVASASSFRAFEILHLHLDLRAEFGPPGPGPGSRGLSGTATLELRCLLPEGASELRLDSHSCLEVTAATLRRGQPGDQQAPAEPVPFHTQPFSHYGQALCVAFRQPCGAADRFELELTYRVGEGPGVCWLAPEQTAGKKKPFVYTQGQAVLNRAFFPCFDTPAVKCTYSALIEVPDGFTAVMSADTWEKRGPNKFFFQMSHPIPSYLIALAIGDLASAEVGPRSRVWAEPCLIEAAKEEYSGVIEEFLATGEKLFGPYVWGRYDLLFMPPSFPFGGMENPCLTFVTPCLLAGDRSLADVIIHEISHSWFGNLVTNANWGEFWLNEGFTMYAQRRISTILFGAAYTCLEAATGRALLRQHMNVSGEENPLNKLRVKIEPGVDPDDTYNETPYEKGYCFVSYLAHLVGDQDQFDKFLKAYVDEFKFQSILAEDFLEFYLEYFPELKKKGVDSIPGFEFDRWLNTPGWPPYLPDLSPGDSLMKPAEELAELWVTSEPDMQAIEAVAISTWKTYQLVYFLDKILQKSPLPPGNVKKLGETYPKISNAQNAELRLRWGQIILKNDYQEEFQKVKDFLQSQGKQKYTLPLYHAMMGGSEMARTLAKDTFAATASQLHSNVVNYVQQILAPKDS | ||||||
Modified residue | 446 | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length650
- Mass (Da)72,416
- Last updated2011-07-27 v2
- Checksum95138D47E57E3C61
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E9PYF1 | E9PYF1_MOUSE | Rnpep | 611 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 11 | in Ref. 3; AAH19200 | ||||
Sequence: A → G | ||||||
Sequence conflict | 127 | in Ref. 3; AAH19200 | ||||
Sequence: R → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK159195 EMBL· GenBank· DDBJ | BAE34890.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159445 EMBL· GenBank· DDBJ | BAE35089.1 EMBL· GenBank· DDBJ | mRNA | ||
AK159625 EMBL· GenBank· DDBJ | BAE35239.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466520 EMBL· GenBank· DDBJ | EDL39584.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC019200 EMBL· GenBank· DDBJ | AAH19200.1 EMBL· GenBank· DDBJ | mRNA |