Beta-secretase 2

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Beta-site APP-cleaving enzyme 2
Protein BACE2 PDB 2ewy.png
PDB rendering based on 2ewy.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols BACE2 ; AEPLC; ALP56; ASP1; ASP21; BAE2; CEAP1; DRAP
External IDs OMIM605668 MGI1860440 HomoloGene22696 ChEMBL: 2525 GeneCards: BACE2 Gene
EC number
RNA expression pattern
PBB GE BACE2 217867 x at tn.png
More reference expression data
Species Human Mouse
Entrez 25825 56175
Ensembl ENSG00000182240 ENSMUSG00000040605
UniProt Q9Y5Z0 Q9JL18
RefSeq (mRNA) NM_012105 NM_019517
RefSeq (protein) NP_036237 NP_062390
Location (UCSC) Chr 21:
42.54 – 42.65 Mb
Chr 16:
97.36 – 97.44 Mb
PubMed search [1] [2]

Beta-secretase 2 is an enzyme that in humans is encoded by the BACE2 gene.[1][2][3]

BACE2 is a close homolog of BACE1, a protease known to be an important enzyme involved in the cellular pathways that some believe lead to Alzheimer's disease. The physiological function and role of BACE2 in Alzheimer's disease is unknown.


Cerebral deposition of amyloid beta peptide is an early and critical feature of Alzheimer's disease and a frequent complication of Down syndrome. Amyloid beta peptide is generated by proteolytic cleavage of amyloid precursor protein by 2 proteases, one of which is the protein encoded by this gene. This gene localizes to the 'Down critical region' of chromosome 21. The encoded protein, a member of the peptidase A1 protein family, is a type I integral membrane glycoprotein and aspartic protease. Three transcript variants encoding different isoforms have been described for this gene.[3] It has been reported that BACE2 is the main protease that mediates the release of the amyloidogenic ectodomain of Pmel17 in melanocytes. [4]


BACE2 has been shown to interact with GGA1[5] and GGA2.[5]


  1. ^ Solans A, Estivill X, de La Luna S (Sep 2000). "A new aspartyl protease on 21q22.3, BACE2, is highly similar to Alzheimer's amyloid precursor protein beta-secretase". Cytogenet Cell Genet 89 (3-4): 177–84. doi:10.1159/000015608. PMID 10965118. 
  2. ^ Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML (Jun 2000). "The DNA sequence of human chromosome 21". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953. 
  3. ^ a b "Entrez Gene: BACE2 beta-site APP-cleaving enzyme 2". 
  4. ^ BACE2 processes PMEL to form the melanosome amyloid matrix in pigment cells Pubmed
  5. ^ a b He, Xiangyuan; Chang Wan-Pin; Koelsch Gerald; Tang Jordan (Jul 2002). "Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: implications on the endocytosis mechanism of memapsin 2". FEBS Lett. (Netherlands) 524 (1-3): 183–7. doi:10.1016/S0014-5793(02)03052-1. ISSN 0014-5793. PMID 12135764. 

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