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P56818

- BACE1_MOUSE

UniProt

P56818 - BACE1_MOUSE

Protein

Beta-secretase 1

Gene

Bace1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    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 amyloid precursor protein.

    Enzyme regulationi

    Inhibited by RTN3 and RTN4.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei93 – 931PROSITE-ProRule annotation
    Active sitei289 – 2891PROSITE-ProRule annotation

    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

    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.By similarity

    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

    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 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 4524Sequence AnalysisPRO_0000025941Add
    BLAST
    Chaini46 – 501456Beta-secretase 1PRO_0000025942Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-acetyllysineBy similarity
    Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 420By similarity
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Modified residuei275 – 2751N6-acetyllysineBy similarity
    Disulfide bondi278 ↔ 443By similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei285 – 2851N6-acetyllysineBy similarity
    Modified residuei299 – 2991N6-acetyllysineBy similarity
    Modified residuei300 – 3001N6-acetyllysineBy similarity
    Modified residuei307 – 3071N6-acetyllysineBy similarity
    Disulfide bondi330 ↔ 380By similarity
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis

    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

    Keywords - PTMi

    Acetylation, 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. Interacts with NAT8 and NAT8B By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204741. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP56818.
    SMRiP56818. Positions 58-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 457436ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini479 – 50123CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei458 – 47821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni479 – 50123Interaction with RTN3By 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.By similarity

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    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

    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: October 1, 2014
    This is version 131 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