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Protein

Beta-secretase 2

Gene

Bace2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves APP, between residues 690 and 691, leading 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. It has also been shown that it can cleave APP between residues 671 and 672 (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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061PROSITE-ProRule annotation
Active sitei299 – 2991PROSITE-ProRule annotation

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. membrane protein ectodomain proteolysis Source: UniProtKB
  2. negative regulation of amyloid precursor protein biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.041.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-secretase 2 (EC:3.4.23.45)
Alternative name(s):
Aspartyl protease 1
Short name:
ASP1
Short name:
Asp 1
Beta-site amyloid precursor protein cleaving enzyme 2
Short name:
Beta-site APP cleaving enzyme 2
Memapsin-1
Membrane-associated aspartic protease 1
Theta-secretase
Gene namesi
Name:Bace2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1860440. Bace2.

Subcellular locationi

Membrane By similarity; Single-pass type I membrane protein By similarity. Golgi apparatus By similarity. Endoplasmic reticulum By similarity. Endosome By similarity. Cell surface By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 469450ExtracellularSequence AnalysisAdd
BLAST
Transmembranei470 – 49021HelicalSequence AnalysisAdd
BLAST
Topological domaini491 – 51424CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB-SubCell
  2. endoplasmic reticulum Source: UniProtKB-SubCell
  3. endosome Source: UniProtKB-SubCell
  4. Golgi apparatus Source: UniProtKB
  5. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Propeptidei20 – 6243By similarityPRO_0000383646Add
BLAST
Chaini63 – 514452Beta-secretase 2PRO_0000383647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi229 ↔ 429By similarity
Disulfide bondi288 ↔ 453By similarity
Disulfide bondi340 ↔ 389By similarity
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Undergoes autoproteolytic cleavage.By similarity
Glycosylated.By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9JL18.

Expressioni

Gene expression databases

BgeeiQ9JL18.
GenevestigatoriQ9JL18.

Interactioni

Subunit structurei

Monomer. Interacts ith RTN3 and RTN4 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ9JL18.
SMRiQ9JL18. Positions 74-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG267436.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000036572.
InParanoidiQ9JL18.
KOiK07747.
OrthoDBiEOG7DNNVW.
PhylomeDBiQ9JL18.
TreeFamiTF329595.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009121. Pept_A1_BACE2.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR01817. BACE2.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JL18-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGALLRALLL LVLAQWLLSA VPALAPAPFT LPLQVAGATN HRASAVPGLG
60 70 80 90 100
TPELPRADGL ALALEPVRAT ANFLAMVDNL QGDSGRGYYL EMLIGTPPQK
110 120 130 140 150
VQILVDTGSS NFAVAGAPHS YIDTYFDSES SSTYHSKGFD VTVKYTQGSW
160 170 180 190 200
TGFVGEDLVT IPKGFNSSFL VNIATIFESE NFFLPGIKWN GILGLAYAAL
210 220 230 240 250
AKPSSSLETF FDSLVAQAKI PDIFSMQMCG AGLPVAGSGT NGGSLVLGGI
260 270 280 290 300
EPSLYKGDIW YTPIKEEWYY QIEILKLEIG GQNLNLDCRE YNADKAIVDS
310 320 330 340 350
GTTLLRLPQK VFDAVVEAVA RTSLIPEFSD GFWTGAQLAC WTNSETPWAY
360 370 380 390 400
FPKISIYLRD ENASRSFRIT ILPQLYIQPM MGAGFNYECY RFGISSSTNA
410 420 430 440 450
LVIGATVMEG FYVVFDRAQR RVGFAVSPCA EIEGTTVSEI SGPFSTEDIA
460 470 480 490 500
SNCVPAQALN EPILWIVSYA LMSVCGAILL VLILLLLLPL HCRHAPRDPE
510
VVNDESSLVR HRWK
Length:514
Mass (Da):55,800
Last modified:October 1, 2000 - v1
Checksum:iA70725F2C1DF5B47
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → P in BAC34931. (PubMed:16141072)Curated
Sequence conflicti11 – 111L → P in BAE38011. (PubMed:16141072)Curated
Sequence conflicti11 – 111L → P in BAC37384. (PubMed:16141072)Curated
Sequence conflicti37 – 371G → R in BAC34931. (PubMed:16141072)Curated
Sequence conflicti37 – 371G → R in BAE38011. (PubMed:16141072)Curated
Sequence conflicti37 – 371G → R in BAC37384. (PubMed:16141072)Curated
Sequence conflicti53 – 531E → G in BAC37384. (PubMed:16141072)Curated
Sequence conflicti369 – 3691I → T in BAC34931. (PubMed:16141072)Curated
Sequence conflicti488 – 4881L → V in AAD45964. (PubMed:10683441)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216310 mRNA. Translation: AAF36599.1.
AK052309 mRNA. Translation: BAC34931.1.
AK078770 mRNA. Translation: BAC37384.1.
AK165036 mRNA. Translation: BAE38011.1.
CH466602 Genomic DNA. Translation: EDL03663.1.
BC120773 mRNA. Translation: AAI20774.1.
BC131947 mRNA. Translation: AAI31948.1.
AF051150 mRNA. Translation: AAD45964.1.
CCDSiCCDS28359.1.
RefSeqiNP_062390.3. NM_019517.4.
UniGeneiMm.97885.

Genome annotation databases

EnsembliENSMUST00000047275; ENSMUSP00000043918; ENSMUSG00000040605.
GeneIDi56175.
KEGGimmu:56175.
UCSCiuc008ade.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216310 mRNA. Translation: AAF36599.1.
AK052309 mRNA. Translation: BAC34931.1.
AK078770 mRNA. Translation: BAC37384.1.
AK165036 mRNA. Translation: BAE38011.1.
CH466602 Genomic DNA. Translation: EDL03663.1.
BC120773 mRNA. Translation: AAI20774.1.
BC131947 mRNA. Translation: AAI31948.1.
AF051150 mRNA. Translation: AAD45964.1.
CCDSiCCDS28359.1.
RefSeqiNP_062390.3. NM_019517.4.
UniGeneiMm.97885.

3D structure databases

ProteinModelPortaliQ9JL18.
SMRiQ9JL18. Positions 74-456.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA01.041.

Proteomic databases

MaxQBiQ9JL18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047275; ENSMUSP00000043918; ENSMUSG00000040605.
GeneIDi56175.
KEGGimmu:56175.
UCSCiuc008ade.2. mouse.

Organism-specific databases

CTDi25825.
MGIiMGI:1860440. Bace2.

Phylogenomic databases

eggNOGiNOG267436.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000036572.
InParanoidiQ9JL18.
KOiK07747.
OrthoDBiEOG7DNNVW.
PhylomeDBiQ9JL18.
TreeFamiTF329595.

Miscellaneous databases

ChiTaRSiBace2. mouse.
NextBioi311944.
PROiQ9JL18.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JL18.
GenevestigatoriQ9JL18.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009121. Pept_A1_BACE2.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR01817. BACE2.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of the mouse Asp1 gene, a homolog of the human ASP1 (Down Syndrome region aspartyl protease)."
    Choi D.K., Sugano S., Sakaki Y.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Eye, Heart and Testis.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain.
  5. "The gene encoding DRAP (BACE2), a glycosylated transmembrane protein of the aspartic protease family, maps to the down critical region."
    Acquati F., Accarino M.P., Nucci C., Fumagalli P., Jovine L., Ottolenghi S., Taramelli R.
    FEBS Lett. 468:59-64(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 260-514.

Entry informationi

Entry nameiBACE2_MOUSE
AccessioniPrimary (citable) accession number: Q9JL18
Secondary accession number(s): Q3TNS7
, Q8C5E9, Q8C793, Q9R1P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 1, 2000
Last modified: February 4, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.