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P56818

- BACE1_MOUSE

UniProt

P56818 - BACE1_MOUSE

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Protein

Beta-secretase 1

Gene
Bace1, Bace
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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.

Catalytic activityi

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

Enzyme regulationi

Inhibited by RTN3 and RTN4 By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931 By similarity
Active sitei289 – 2891 By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB
  2. endopeptidase activity Source: MGI
  3. protein binding Source: MGI

GO - Biological processi

  1. beta-amyloid metabolic process Source: UniProtKB
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.46. 3474.

Protein family/group databases

MEROPSiA01.004.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Bace1
Synonyms:Bace
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1346542. Bace1.

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 457436Extracellular Reviewed predictionAdd
BLAST
Transmembranei458 – 47821Helical; Reviewed predictionAdd
BLAST
Topological domaini479 – 50123Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. axon Source: MGI
  2. cell surface Source: UniProtKB-SubCell
  3. cytoplasmic vesicle Source: MGI
  4. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  5. endoplasmic reticulum Source: UniProtKB-SubCell
  6. endosome Source: UniProtKB
  7. Golgi apparatus Source: UniProtKB
  8. integral component of plasma membrane Source: Ensembl
  9. membrane Source: MGI
  10. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Mice show a higher mortality rate early in life.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121 Reviewed predictionAdd
BLAST
Propeptidei22 – 4524 Reviewed predictionPRO_0000025941Add
BLAST
Chaini46 – 501456Beta-secretase 1PRO_0000025942Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi153 – 1531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi172 – 1721N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi216 ↔ 420 By similarity
Glycosylationi223 – 2231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi278 ↔ 443 By similarity
Disulfide bondi330 ↔ 380 By similarity
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Glycosylated By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP56818.

PTM databases

PhosphoSiteiP56818.

Expressioni

Tissue specificityi

Brain.

Gene expression databases

ArrayExpressiP56818.
BgeeiP56818.
CleanExiMM_BACE1.
GenevestigatoriP56818.

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.

Protein-protein interaction databases

BioGridi204741. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP56818.
SMRiP56818. Positions 58-453.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni479 – 50123Interaction with RTN3 By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the peptidase A1 family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71700.
GeneTreeiENSGT00710000106265.
HOGENOMiHOG000036572.
HOVERGENiHBG059578.
InParanoidiP56818.
KOiK04521.
OMAiPDMEDCG.
OrthoDBiEOG7DNNVW.
PhylomeDBiP56818.
TreeFamiTF329595.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009120. Pept_A1_BACE1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56818-1 [UniParc]FASTAAdd to Basket

« Hide

MAPALHWLLL WVGSGMLPAQ GTHLGIRLPL RSGLAGPPLG LRLPRETDEE    50
SEEPGRRGSF VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA 100
VGAAPHPFLH RYYQRQLSST YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH 150
GPNVTVRANI AAITESDKFF INGSNWEGIL GLAYAEIARP DDSLEPFFDS 200
LVKQTHIPNI FSLQLCGAGF PLNQTEALAS VGGSMIIGGI DHSLYTGSLW 250
YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK 300
VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG 350
EVTNQSFRIT ILPQQYLRPV EDVATSQDDC YKFAVSQSST GTVMGAVIME 400
GFYVVFDRAR KRIGFAVSAC HVHDEFRTAA VEGPFVTADM EDCGYNIPQT 450
DESTLMTIAY VMAAICALFM LPLCLMVCQW RCLRCLRHQH DDFADDISLL 500
K 501
Length:501
Mass (Da):55,748
Last modified:August 14, 2001 - v2
Checksum:iC085A013145E474E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS23135.1.
RefSeqiNP_001139419.1. NM_001145947.1.
NP_035922.4. NM_011792.5.
UniGeneiMm.24044.

Genome annotation databases

EnsembliENSMUST00000034591; ENSMUSP00000034591; ENSMUSG00000032086.
GeneIDi23821.
KEGGimmu:23821.
UCSCiuc009pgh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS23135.1.
RefSeqi NP_001139419.1. NM_001145947.1.
NP_035922.4. NM_011792.5.
UniGenei Mm.24044.

3D structure databases

ProteinModelPortali P56818.
SMRi P56818. Positions 58-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204741. 4 interactions.

Chemistry

ChEMBLi CHEMBL4593.

Protein family/group databases

MEROPSi A01.004.

PTM databases

PhosphoSitei P56818.

Proteomic databases

PRIDEi P56818.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034591 ; ENSMUSP00000034591 ; ENSMUSG00000032086 .
GeneIDi 23821.
KEGGi mmu:23821.
UCSCi uc009pgh.2. mouse.

Organism-specific databases

CTDi 23621.
MGIi MGI:1346542. Bace1.

Phylogenomic databases

eggNOGi NOG71700.
GeneTreei ENSGT00710000106265.
HOGENOMi HOG000036572.
HOVERGENi HBG059578.
InParanoidi P56818.
KOi K04521.
OMAi PDMEDCG.
OrthoDBi EOG7DNNVW.
PhylomeDBi P56818.
TreeFami TF329595.

Enzyme and pathway databases

BRENDAi 3.4.23.46. 3474.

Miscellaneous databases

ChiTaRSi BACE1. mouse.
NextBioi 303471.
PROi P56818.
SOURCEi Search...

Gene expression databases

ArrayExpressi P56818.
Bgeei P56818.
CleanExi MM_BACE1.
Genevestigatori P56818.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009120. Pept_A1_BACE1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR01816. BACE1.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  7. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiBACE1_MOUSE
AccessioniPrimary (citable) accession number: P56818
Secondary accession number(s): Q544D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 14, 2001
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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