Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity.
Expression analysis of BACE2 in brain and peripheral tissues.
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BACE and BACE2 define a membrane aspartic protease family.
"BACE and BACE2 are unique among aspartic proteases in that they possess a carboxyl-terminal extension with a predicted transmembrane region and together they define a new family."
BACE2 functions as an alternative alpha-secretase in cells.
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BACE2 localizes to ER, Golgi, TGN, endosomes and plasma membrane.
"BACE2 localizes in the endoplasmic reticulum, Golgi, trans-Golgi network, endosomes, and plasma membrane, and its cellular localization patterns depend on the presence of its transmembrane domain."
Antagonistic effects of beta-site amyloid precursor protein-cleaving enzymes 1 and 2 on beta-amyloid peptide production in cells.
Bace2 is a β cell-enriched protease that regulates pancreatic β cell function and mass.
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Bace2 is the TMEM27 sheddase in beta cells.
"Here we identified, through a siRNA screen, beta site amyloid precursor protein cleaving enzyme 2 (Bace2) as the sheddase of the proproliferative plasma membrane protein Tmem27 in murine and human β cells."
BACE2 processes PMEL to form the melanosome amyloid matrix in pigment cells.
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BACE2 cleaves PMEL to release the amyloidogenic luminal domain.
"By using biochemical and morphological analyses, combined with RNA silencing, pharmacologic inhibition, and BACE2 overexpression in a human melanocytic cell line, we show that BACE2 cleaves the integral membrane form of PMEL within the juxtamembrane domain, releasing the PMEL luminal domain into endosomal precursors for the formation of amyloid fibrils and downstream melanosome morphogenesis."
Identification of Human Islet Amyloid Polypeptide as a BACE2 Substrate.
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BACE2 cleaves human IAPP at two sites.
"Herein, we identify two distinct sites of the mature human IAPP sequence that are susceptible to BACE2-mediated proteolytic activity."
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
UniProt entry Q9Y5Z0 (BACE2_HUMAN)
Affinage mechanistic annotation for BACE2 (human)
Identification of BACE2 as an avid ß-amyloid-degrading protease.
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BACE2 is an avid Abeta-degrading protease in vitro.
"However, in vitro, BACE2 was also found to be a particularly avid AßDP, with a catalytic efficiency exceeding all known AßDPs except insulin-degrading enzyme (IDE)."
Prodomain processing of Asp1 (BACE2) is autocatalytic.
The Alzheimer's disease-linked protease BACE2 cleaves VEGFR3 and modulates its signaling.
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BACE2 sheds VEGFR3 from lymphatic endothelial cells.
"Inactivation of BACE2, but not BACE1, inhibited shedding of VEGFR3 from primary human lymphatic endothelial cells (LECs) and reduced release of the shed, soluble VEGFR3 (sVEGFR3) ectodomain into the blood of mice, nonhuman primates, and humans."