LipidDB ID

LipidDB-9606-00059

Entry Name

UniProt Accession

P56817; A0M8W7; B0YIU9; E9PE65; H7BXJ9; Q9BYB9; Q9BYC0; Q9BYC1; Q9UJT5; Q9ULS1;

Theoretical PI

5.24

Molecular Weight

55710.74

Genbank Protein ID

AAF04142.1; AAF18982.1; AAF17079.1; AAF26367.1; AAK38374.1; AAK38375.1; BAB40931.1; BAB40932.1; BAB40933.1; BAA86463.2; AAY16982.1; ACA05927.1; EAW67313.1; AAH65492.1; AAF13715.1;

Genbank Nucleotide ID

AF190725; AF201468; AF200343; AF204943; AF338816; AF338817; AB050436; AB050437; AB050438; AB032975; DQ007053; EF444940; AP000892; CH471065; BC065492; AF200193;

Protein Name

Beta-secretase 1

Protein Synonyms/Alias

3.4.23.46; Aspartyl protease 2; ASP2; Asp 2; Beta-site amyloid precursor protein cleaving enzyme 1; Beta-site APP cleaving enzyme 1; Memapsin-2; Membrane-associated aspartic protease 2;

Gene Name

BACE1

Gene Synonyms/Alias

BACE; KIAA1149;

Created Date

30-MAY-2000

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Vetrivel KS, Meckler X, Chen Y, Nguyen PD, Seidah NG, Vassar R, Wong PC,Fukata M, Kounnas MZ, Thinakaran G. Alzheimer disease Abeta production in theabsence of S-palmitoylation-dependent targeting of BACE1 to lipid rafts. J BiolChem. 2009 Feb 6;284(6):3793-803. doi: 10.1074/jbc.M808920200. Epub 2008 Dec 12.[PMID:19074428]
[2] Sidera C, Parsons R, Austen B. Post-translational processing of beta-secretasein Alzheimer's disease. Proteomics. 2005 Apr;5(6):1533-43.[PMID:15789346]

Functional Description

Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads 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.

Sequence Annotation

Topological domain: 22 457 Extracellular.
Transmembrane: 458 478 Helical.
Topological domain: 479 501 Cytoplasmic.
Region: 479 501 Interaction with RTN3.
Active site: 93 93
Active site: 289 289
Modified residue: 126 126 N6-acetyllysine.
Modified residue: 275 275 N6-acetyllysine.
Modified residue: 279 279 N6-acetyllysine.
Modified residue: 285 285 N6-acetyllysine.
Modified residue: 299 299 N6-acetyllysine.
Modified residue: 300 300 N6-acetyllysine.
Modified residue: 307 307 N6-acetyllysine.

Protein Length

501 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0030424; C:axon; IEA:Ensembl
GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW
GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW
GO:0005768; C:endosome; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0016021; C:integral component of membrane; NAS:UniProtKB
GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB
GO:0005770; C:late endosome; IDA:UniProtKB
GO:0005771; C:multivesicular body; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005802; C:trans-Golgi network; IDA:UniProtKB
GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB
GO:0001540; F:beta-amyloid binding; IPI:Alzheimers_University_of_Toronto
GO:0008798; F:beta-aspartyl-peptidase activity; TAS:ProtInc
GO:0019899; F:enzyme binding; IPI:UniProtKB
GO:0050435; P:beta-amyloid metabolic process; IDA:UniProtKB
GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB
GO:0006508; P:proteolysis; IDA:UniProtKB

Interpro

InterPro; IPR001461; Aspartic_peptidase
InterPro; IPR001969; Aspartic_peptidase_AS
InterPro; IPR009119; Pept_A1_BACE
InterPro; IPR009120; Pept_A1_BACE1
InterPro; IPR021109; Peptidase_aspartic_dom

Pfam

Pfam; PF00026; Asp;

SMART

PROSITE

PROSITE; PS00141; ASP_PROTEASE;

PRINTS

PRINTS; PR01816; BACE1;
PRINTS; PR01815; BACEFAMILY;
PRINTS; PR00792; PEPSIN;