Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. It has also been shown that it can cleave APP between residues 671 and 672 (PubMed:10591213, PubMed:11083922, PubMed:11423558, PubMed:15857888, PubMed:16816112). Involved in the proteolytic shedding of PMEL at early stages of melanosome biogenesis. Cleaves PMEL within the M-beta fragment to release the amyloidogenic PMEL luminal fragment containing M-alpha and a small portion of M-beta N-terminus. This is a prerequisite step for subsequent processing and assembly of PMEL fibrils into amyloid sheets (PubMed:23754390). Responsible also for the proteolytic processing of CLTRN in pancreatic beta cells (PubMed:21907142).
Undergoes autoproteolytic cleavage.
Glycosylated.
Belongs to the peptidase A1 family.
Brain. Present in neurons within the hippocampus, frontal cortex and temporal cortex (at protein level). Expressed at low levels in most peripheral tissues and at higher levels in colon, kidney, pancreas, placenta, prostate, stomach and trachea. Expressed at low levels in the brain. Found in spinal cord, medulla oblongata, substantia nigra and locus coruleus. Expressed in the ductal epithelium of both normal and malignant prostate.
AEPLC, ALP56, ASP21, CDA13, UNQ418/PRO852, BACE2, Beta-secretase 2, Aspartic-like protease 56 kDa, Aspartyl protease 1, Beta-site amyloid precursor protein cleaving enzyme 2, Down region aspartic protease, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase, ASP1, Asp 1, Beta-site APP cleaving enzyme 2, DRAP
Proteins
Neuroscience
56180Da
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ab5670