Beta-secretase 1 precursor - Mus musculus (Mouse)

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P56818 (BACE1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-secretase 1
EC=3.4.23.46

Alternative name(s):
Aspartyl protease 2
Short name=ASP2
Short name=Asp 2
Beta-site amyloid precursor protein cleaving enzyme 1
Short name=Beta-site APP cleaving enzyme 1
Memapsin-2
Membrane-associated aspartic protease 2

Gene names

Name:	Bace1
Synonyms:	Bace

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-\|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer amyloid precursor protein.
Enzyme regulation	Inhibited by RTN3 and RTN4 By similarity.
Subunit structure	Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4. Interacts with SNX6 By similarity. Interacts with PCSK9 By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein. Golgi apparatus › trans-Golgi network By similarity. Endoplasmic reticulum By similarity. Endosome By similarity. Cell surface By similarity. Cytoplasmic vesicle membrane By similarity. Note: Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface By similarity.
Tissue specificity	Brain.
Domain	The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP By similarity.
Post-translational modification	Glycosylated By similarity.
Disruption phenotype	Mice show a higher mortality rate early in life. Ref.7
Sequence similarities	Belongs to the peptidase A1 family.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle Endoplasmic reticulum Endosome Golgi apparatus Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	beta-amyloid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB axon Inferred from direct assay PubMed 11740561. Source: MGI cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic vesicle Inferred from direct assay PubMed 11740561. Source: MGI cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell endosome Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred from electronic annotation. Source: Compara membrane Inferred from direct assay PubMed 15886206. Source: MGI trans-Golgi network Inferred from electronic annotation. Source: Compara
Molecular_function	aspartic-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Propeptide

22 – 45

Potential

PRO_0000025941

Chain

46 – 501

456

Beta-secretase 1

PRO_0000025942

Regions

Topological domain

22 – 457

436

Extracellular Potential

Transmembrane

458 – 478

Helical; Potential

Topological domain

479 – 501

Cytoplasmic Potential

Region

479 – 501

Interaction with RTN3 By similarity

Sites

Active site

By similarity

Active site

289

By similarity

Amino acid modifications

Glycosylation

153

N-linked (GlcNAc...) Potential

Glycosylation

172

N-linked (GlcNAc...) Potential

Glycosylation

223

N-linked (GlcNAc...) Potential

Glycosylation

354

N-linked (GlcNAc...) Potential

Disulfide bond

216 ↔ 420

By similarity

Disulfide bond

278 ↔ 443

By similarity

Disulfide bond

330 ↔ 380

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P56818 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: C085A013145E474E
Show »

FASTA

501

55,748

        10         20         30         40         50         60 
MAPALHWLLL WVGSGMLPAQ GTHLGIRLPL RSGLAGPPLG LRLPRETDEE SEEPGRRGSF 

        70         80         90        100        110        120 
VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA VGAAPHPFLH RYYQRQLSST 

       130        140        150        160        170        180 
YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH GPNVTVRANI AAITESDKFF INGSNWEGIL 

       190        200        210        220        230        240 
GLAYAEIARP DDSLEPFFDS LVKQTHIPNI FSLQLCGAGF PLNQTEALAS VGGSMIIGGI 

       250        260        270        280        290        300 
DHSLYTGSLW YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK 

       310        320        330        340        350        360 
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG EVTNQSFRIT 

       370        380        390        400        410        420 
ILPQQYLRPV EDVATSQDDC YKFAVSQSST GTVMGAVIME GFYVVFDRAR KRIGFAVSAC 

       430        440        450        460        470        480 
HVHDEFRTAA VEGPFVTADM EDCGYNIPQT DESTLMTIAY VMAAICALFM LPLCLMVCQW 

       490        500 
RCLRCLRHQH DDFADDISLL K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE." Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A., Denis P., Teplow D.B., Ross S., Amarante P., Loeloff R., Luo Y., Fisher S., Fuller J., Edenson S., Lile J., Jarosinski M.A., Biere A.L., Curran E. Citron M. Science 286:735-741(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Bennett B.D., Vassar R., Citron M. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 6 AND 81-87.
[3]	"Membrane-anchored aspartyl protease with Alzheimer's disease beta-secretase activity." Yan R., Bienkowski M.J., Shuck M.E., Miao H., Tory M.C., Pauley A.M., Brashier J.R., Stratman N.C., Mathews W.R., Buhl A.E., Carter D.B., Tomasselli A.G., Parodi L.A., Heinrikson R.L., Gurney M.E. Nature 402:533-537(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Aorta, Head and Testis.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[6]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 301-307, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[7]	"Phenotypic and biochemical analyses of BACE1- and BACE2-deficient mice." Dominguez D., Tournoy J., Hartmann D., Huth T., Cryns K., Deforce S., Serneels L., Camacho I.E., Marjaux E., Craessaerts K., Roebroek A.J.M., Schwake M., D'Hooge R., Bach P., Kalinke U., Moechars D., Alzheimer C., Reiss K., Saftig P., De Strooper B. J. Biol. Chem. 280:30797-30806(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF190726 mRNA. Translation: AAF04143.2. AF200346 mRNA. Translation: AAF17082.1. AK014464 mRNA. Translation: BAB29370.1. AK033112 mRNA. Translation: BAC28156.1. AK041285 mRNA. Translation: BAC30889.1. BC048189 mRNA. Translation: AAH48189.1.
IPI	IPI00116121.
RefSeq	NP_001139419.1. NM_001145947.1. NP_035922.4. NM_011792.5.
UniGene	Mm.24044.
3D structure databases
ProteinModelPortal	P56818.
SMR	P56818. Positions 53-447.
ModBase	Search...
Protein family/group databases
MEROPS	A01.004.
PTM databases
PhosphoSite	P56818.
Proteomic databases
PRIDE	P56818.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034591; ENSMUSP00000034591; ENSMUSG00000032086.
GeneID	23821.
KEGG	mmu:23821.
UCSC	uc009pgh.2. mouse.
Organism-specific databases
CTD	23621.
MGI	MGI:1346542. Bace1.
Phylogenomic databases
eggNOG	NOG71700.
GeneTree	ENSGT00700000104165.
HOGENOM	HOG000036572.
HOVERGEN	HBG059578.
InParanoid	P56818.
KO	K04521.
OMA	PDMEDCG.
Enzyme and pathway databases
BRENDA	3.4.23.46. 3474.
Gene expression databases
ArrayExpress	P56818.
Bgee	P56818.
CleanEx	MM_BACE1.
Genevestigator	P56818.
GermOnline	ENSMUSG00000032086. Mus musculus.
Family and domain databases
Gene3D	2.40.70.10. 2 hits.
InterPro	IPR009119. Pept_A1_BACE. IPR009120. Pept_A1_BACE1. IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. [Graphical view]
PANTHER	PTHR13683. PTHR13683. 1 hit.
Pfam	PF00026. Asp. 1 hit. [Graphical view]
PRINTS	PR01816. BACE1. PR01815. BACEFAMILY. PR00792. PEPSIN.
SUPFAM	SSF50630. Pept_Aspartic. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4593.
ChiTaRS	BACE1. mouse.
NextBio	303471.
SOURCE	Search...

Entry information

Entry name

BACE1_MOUSE

Accession

Primary (citable) accession number: P56818
Secondary accession number(s): Q544D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 14, 2001
Last modified:	April 3, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents