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Q1KLR6 (BACE1_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-secretase 1

EC=3.4.23.46
Alternative name(s):
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
OrganismCavia porcellus (Guinea pig)
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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's 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.

Subcellular location

Membrane; Single-pass type I membrane protein. Golgi apparatustrans-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.

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.

Sequence similarities

Belongs to the peptidase A1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 4524 By similarity
PRO_0000245804
Chain46 – 473428Beta-secretase 1
PRO_0000245805

Regions

Topological domain22 – 429408Extracellular Potential
Transmembrane430 – 45021Helical; Potential
Topological domain451 – 47323Cytoplasmic Potential
Region451 – 47323Interaction with RTN3 By similarity

Sites

Active site901 By similarity
Active site2611 By similarity

Amino acid modifications

Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Disulfide bond188 ↔ 392 By similarity
Disulfide bond250 ↔ 415 By similarity
Disulfide bond302 ↔ 352 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1KLR6 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: F9583693A13F86E9

FASTA47352,576
        10         20         30         40         50         60 
MAPALPWLLL WVGSGVLPVH GTQDGIRLPL RSGLAGAPLG LRLPRETDEE PGRRGSFVEM 

        70         80         90        100        110        120 
VDNLRGKSGQ GYYVEMTVGS PPQTLNILVD TGSSNFAVGA APHPFLHRYY QRQRSSTYRD 

       130        140        150        160        170        180 
LRKGVYVPYT QGKWEGELGT DLVSIPHGPN VTVRANIAAI TESDKFFING SNWEGILGLA 

       190        200        210        220        230        240 
YAEIARLCGA GFPLNQSEAV ASVGGSMIIG GIDHSLYTGN LWYTPIRREW YYEVIIVRVE 

       250        260        270        280        290        300 
INGQDLKMDC KEYNYDKSIV DSGTTNLRLP KKVFEAAVKS IKAASSTEKF PDGFWLGEQL 

       310        320        330        340        350        360 
VCWQAGTTPW NIFPVISLYL MGEVTNQSFR ITILPQQYLR PVEDVATSQD DCYKFAISQS 

       370        380        390        400        410        420 
STGTVMGAVI MEGFYVVFDR ARKRIGFAVS ACHVHDEFRT ATVEGPFVTP DMEDCGYNIP 

       430        440        450        460        470 
QTDESTLMTI AYVMAAICAL FMLPLCLMVC QWRCLRCLRH QHDDFADDIS LLK 

« Hide

References

[1]"Beta-site amyloid precursor protein cleaving enzyme 1 (BACE1) mRNA from guinea pig."
Christensen S.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ471956 mRNA. Translation: ABF13340.1.
RefSeqNP_001166390.1. NM_001172919.1.

3D structure databases

ProteinModelPortalQ1KLR6.
SMRQ1KLR6. Positions 52-419.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1KLR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000012877; ENSCPOP00000011476; ENSCPOG00000012754.
GeneID100135485.

Organism-specific databases

CTD23621.

Phylogenomic databases

eggNOGroNOG14885.
GeneTreeENSGT00600000084334.
HOVERGENHBG059578.
InParanoidQ1KLR6.
OMASFVEMVD.
OrthoDBEOG4SF95Q.

Family and domain databases

InterProIPR009119. Pept_A1_BACE.
IPR009120. Pept_A1_BACE1.
IPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 2 hits.
[Graphical view]
PRINTSPR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBACE1_CAVPO
AccessionPrimary (citable) accession number: Q1KLR6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 30, 2006
Last modified: July 27, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families