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Protein

Beta-secretase 1

Gene

BACE1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.

Enzyme regulationi

Inhibited by RTN3 and RTN4.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei93PROSITE-ProRule annotation1
Active sitei289PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.004

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:BACE1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Organism-specific databases

VGNCiVGNC:26400 BACE1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 457ExtracellularSequence analysisAdd BLAST436
Transmembranei458 – 478HelicalSequence analysisAdd BLAST21
Topological domaini479 – 501CytoplasmicSequence analysisAdd BLAST23

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000024580222 – 45By similarityAdd BLAST24
ChainiPRO_000024580346 – 501Beta-secretase 1Add BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei126N6-acetyllysineBy similarity1
Glycosylationi153N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi172N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi216 ↔ 420By similarity
Glycosylationi223N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei275N6-acetyllysineBy similarity1
Disulfide bondi278 ↔ 443By similarity
Modified residuei279N6-acetyllysineBy similarity1
Modified residuei285N6-acetyllysineBy similarity1
Modified residuei299N6-acetyllysineBy similarity1
Modified residuei300N6-acetyllysineBy similarity1
Modified residuei307N6-acetyllysineBy similarity1
Disulfide bondi330 ↔ 380By similarity
Glycosylationi354N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi474S-palmitoyl cysteineBy similarity1
Lipidationi478S-palmitoyl cysteineBy similarity1
Lipidationi482S-palmitoyl cysteineBy similarity1
Lipidationi485S-palmitoyl cysteineBy similarity1
Modified residuei498PhosphoserineBy similarity1

Post-translational modificationi

N-Glycosylated.By similarity
Acetylated in the endoplasmic reticulum at Lys-126, Lys-275, Lys-279, Lys-285, Lys-299, Lys-300 and Lys-307. Acetylation by NAT8 and NAT8B is transient and deacetylation probably occurs in the Golgi. Acetylation regulates the maturation, the transport to the plasma membrane, the stability and the expression of the protein (By similarity).By similarity
Palmitoylation mediates lipid raft localization.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiQ2HJ40

Expressioni

Gene expression databases

BgeeiENSBTAG00000019365
ExpressionAtlasiQ2HJ40 baseline and differential

Interactioni

Subunit structurei

Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts with RTN3 and RTN4. Interacts with SNX6 (By similarity). Interacts with PCSK9 (By similarity). Interacts with NAT8 and NAT8B (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000039837

Structurei

3D structure databases

ProteinModelPortaliQ2HJ40
SMRiQ2HJ40
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 416Peptidase A1PROSITE-ProRule annotationAdd BLAST342

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni479 – 501Interaction with RTN3By similarityAdd BLAST23

Domaini

The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP (By similarity).By similarity

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1339 Eukaryota
ENOG410XNV7 LUCA
GeneTreeiENSGT00910000144168
HOGENOMiHOG000036572
HOVERGENiHBG059578
InParanoidiQ2HJ40
KOiK04521
OMAiPDMEDCG
OrthoDBiEOG091G0CNK
TreeFamiTF329595

Family and domain databases

CDDicd05473 beta_secretase_like, 1 hit
Gene3Di2.40.70.10, 2 hits
InterProiView protein in InterPro
IPR001461 Aspartic_peptidase_A1
IPR001969 Aspartic_peptidase_AS
IPR009119 BACE
IPR009120 BACE1
IPR033874 Memapsin-like
IPR033121 PEPTIDASE_A1
IPR021109 Peptidase_aspartic_dom_sf
PANTHERiPTHR13683 PTHR13683, 1 hit
PTHR13683:SF245 PTHR13683:SF245, 1 hit
PfamiView protein in Pfam
PF00026 Asp, 1 hit
PRINTSiPR01816 BACE1
PR01815 BACEFAMILY
PR00792 PEPSIN
SUPFAMiSSF50630 SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS00141 ASP_PROTEASE, 1 hit
PS51767 PEPTIDASE_A1, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2HJ40-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQALPWLLL WMGSGVLPAH GSQPGIRLPL RSGLGGAPLG LRLPRETDEE
60 70 80 90 100
SEEPGRRGSF VEMVDNLRGK SGQGYYVEMT LGSPPQTLNI LVDTGSSNFA
110 120 130 140 150
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH
160 170 180 190 200
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS
210 220 230 240 250
LVKQTHVPNL FSLQLCGAGF PLNQSEALAS VGGSMIIGGI DHSLYMGSLW
260 270 280 290 300
YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK
310 320 330 340 350
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG
360 370 380 390 400
EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAISQSST GTVMGAVIME
410 420 430 440 450
GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTPDM EDCGYNIPQT
460 470 480 490 500
DESTLMTIAY VMAAICALFM LPLCLMVCQW RCLRCLRHQH DDFADDISLL

K
Length:501
Mass (Da):55,725
Last modified:March 21, 2006 - v1
Checksum:i8E5EA730FC91C295
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC113325 mRNA Translation: AAI13326.1
RefSeqiNP_001039996.1, NM_001046531.1
UniGeneiBt.28273

Genome annotation databases

EnsembliENSBTAT00000040056; ENSBTAP00000039837; ENSBTAG00000019365
GeneIDi614333
KEGGibta:614333

Similar proteinsi

Entry informationi

Entry nameiBACE1_BOVIN
AccessioniPrimary (citable) accession number: Q2HJ40
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 21, 2006
Last modified: March 28, 2018
This is version 96 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health