Primary Information | |
---|---|
BoMiProt ID | Bomi273 |
Protein Name | Aspartyl aminopeptidase |
Organism | Bos taurus |
Uniprot ID | Q2HJH1 |
Milk Fraction | Exosome |
Ref Sequence ID | NP_001039417.1 |
Aminoacid Length | 471 |
Molecular Weight | 51828 |
FASTA Sequence | Download |
Gene Name | DNPEP |
Gene ID | 506882 |
Protein Existence Status | Reviewed: Experimental evidence at protein level |
Secondary Information | |
Presence in other biological fluids/tissue/cells | kidney, lung, and immune cells; expressed in many organ systems with especially high activity in the brain and testis |
Protein Function | play an essential role in cellular metabolism that has remained conserved throughout evolution; regulation of the renin-angiotensin system |
Biochemical Properties | acidic residue specific aminopeptidases; belongs to the M18 metallopeptidase family; is a self-compartmentalized, binuclear zinc-containing enzyme that forms a tetrahedron-shaped homododecameric complex; cytosolic, although it also exists in a membrane-associated form in some tissues; inhibitors - Nonselective metal chelators, reducing agents, and a substrate analog, aspartic acid hydroxamate |
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | |
CATH | Matched CATH superfamily 3.40.630.10 2.30.250.10 |
Predicted Disorder Regions | NA |
DisProt Annotation | |
TM Helix Prediction | No TM helices |
PDB ID | 3VAR, 3VAT, |
Bibliography | 1. Chen, Y. et al. (2014) ‘Identification and Characterization of Novel Inhibitors of Mammalian Aspartyl Aminopeptidase’, Molecular Pharmacology, 86(2), pp. 231–242. doi: 10.1124/mol.114.093070. |