|
|
||
|
|
|
|
|
UniProt functional annotation for Q16769 | ||
|
|
|
|
|
|
||
| UniProt code: Q16769. |
|
||
| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
|
||
|
||
| Function: | |
Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N- terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides. {ECO:0000269|PubMed:15063747, ECO:0000269|PubMed:18486145, ECO:0000269|PubMed:21288892}. |
|
||
| Catalytic activity: | |
Reaction=N-terminal L-glutaminyl-[peptide] = N-terminal 5-oxo-L-prolyl- [peptide] + NH4(+); Xref=Rhea:RHEA:23652, Rhea:RHEA-COMP:11736, Rhea:RHEA-COMP:11846, ChEBI:CHEBI:28938, ChEBI:CHEBI:64722, ChEBI:CHEBI:87215; EC=2.3.2.5; Evidence={ECO:0000269|PubMed:16135565, ECO:0000269|PubMed:18072935, ECO:0000269|PubMed:18486145, ECO:0000269|PubMed:21288892}; |
| Subcellular location: | |
Secreted {ECO:0000269|PubMed:18486145}. |
| Similarity: | |
Belongs to the glutaminyl-peptide cyclotransferase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.