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Q9JL18 (BACE2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 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 names
Name:Bace2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length514 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 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.

Catalytic activity

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

Subunit structure

Monomer. Interacts ith RTN3 and RTN4 By similarity.

Subcellular location

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

Post-translational modification

Undergoes autoproteolytic cleavage By similarity.

Glycosylated By similarity.

Sequence similarities

Belongs to the peptidase A1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Propeptide20 – 6243 By similarity
PRO_0000383646
Chain63 – 514452Beta-secretase 2
PRO_0000383647

Regions

Topological domain20 – 469450Extracellular Potential
Transmembrane470 – 49021Helical; Potential
Topological domain491 – 51424Cytoplasmic Potential

Sites

Active site1061 By similarity
Active site2991 By similarity

Amino acid modifications

Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation3621N-linked (GlcNAc...) Potential
Disulfide bond229 ↔ 429 By similarity
Disulfide bond288 ↔ 453 By similarity
Disulfide bond340 ↔ 389 By similarity

Experimental info

Sequence conflict111L → P in BAC34931. Ref.2
Sequence conflict111L → P in BAE38011. Ref.2
Sequence conflict111L → P in BAC37384. Ref.2
Sequence conflict371G → R in BAC34931. Ref.2
Sequence conflict371G → R in BAE38011. Ref.2
Sequence conflict371G → R in BAC37384. Ref.2
Sequence conflict531E → G in BAC37384. Ref.2
Sequence conflict3691I → T in BAC34931. Ref.2
Sequence conflict4881L → V in AAD45964. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9JL18 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A70725F2C1DF5B47

FASTA51455,800
        10         20         30         40         50         60 
MGALLRALLL LVLAQWLLSA VPALAPAPFT LPLQVAGATN HRASAVPGLG TPELPRADGL 

        70         80         90        100        110        120 
ALALEPVRAT ANFLAMVDNL QGDSGRGYYL EMLIGTPPQK VQILVDTGSS NFAVAGAPHS 

       130        140        150        160        170        180 
YIDTYFDSES SSTYHSKGFD VTVKYTQGSW TGFVGEDLVT IPKGFNSSFL VNIATIFESE 

       190        200        210        220        230        240 
NFFLPGIKWN GILGLAYAAL AKPSSSLETF FDSLVAQAKI PDIFSMQMCG AGLPVAGSGT 

       250        260        270        280        290        300 
NGGSLVLGGI EPSLYKGDIW YTPIKEEWYY QIEILKLEIG GQNLNLDCRE YNADKAIVDS 

       310        320        330        340        350        360 
GTTLLRLPQK VFDAVVEAVA RTSLIPEFSD GFWTGAQLAC WTNSETPWAY FPKISIYLRD 

       370        380        390        400        410        420 
ENASRSFRIT ILPQLYIQPM MGAGFNYECY RFGISSSTNA LVIGATVMEG FYVVFDRAQR 

       430        440        450        460        470        480 
RVGFAVSPCA EIEGTTVSEI SGPFSTEDIA SNCVPAQALN EPILWIVSYA LMSVCGAILL 

       490        500        510 
VLILLLLLPL HCRHAPRDPE VVNDESSLVR HRWK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS28359.1.
RefSeqNP_062390.3. NM_019517.4.
UniGeneMm.97885.

3D structure databases

ProteinModelPortalQ9JL18.
SMRQ9JL18. Positions 72-455.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSA01.041.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047275; ENSMUSP00000043918; ENSMUSG00000040605.
GeneID56175.
KEGGmmu:56175.
UCSCuc008ade.2. mouse.

Organism-specific databases

CTD25825.
MGIMGI:1860440. Bace2.

Phylogenomic databases

eggNOGNOG267436.
GeneTreeENSGT00710000106265.
HOGENOMHOG000036572.
InParanoidQ8C793.
KOK07747.
OrthoDBEOG7DNNVW.
PhylomeDBQ9JL18.
TreeFamTF329595.

Gene expression databases

BgeeQ9JL18.
GenevestigatorQ9JL18.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009121. Pept_A1_BACE2.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR01817. BACE2.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBACE2. mouse.
NextBio311944.
PROQ9JL18.
SOURCESearch...

Entry information

Entry nameBACE2_MOUSE
AccessionPrimary (citable) accession number: Q9JL18
Secondary accession number(s): Q3TNS7 expand/collapse secondary AC list , Q8C5E9, Q8C793, Q9R1P7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot