SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9JL18

- BACE2_MOUSE

UniProt

Q9JL18 - BACE2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Beta-secretase 2
Gene
Bace2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

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 – 1061 By similarity
Active sitei299 – 2991 By similarity

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB
Complete GO annotation...

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; 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 – 469450Extracellular Reviewed prediction
Add
BLAST
Transmembranei470 – 49021Helical; Reviewed prediction
Add
BLAST
Topological domaini491 – 51424Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. cell surface Source: UniProtKB-SubCell
  3. endoplasmic reticulum Source: UniProtKB-SubCell
  4. endosome Source: UniProtKB-SubCell
  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 – 1919 Reviewed prediction
Add
BLAST
Propeptidei20 – 6243 By similarity
PRO_0000383646Add
BLAST
Chaini63 – 514452Beta-secretase 2
PRO_0000383647Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Undergoes autoproteolytic cleavage By similarity.
Glycosylated By similarity.

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Expressioni

Gene expression databases

BgeeiQ9JL18.
GenevestigatoriQ9JL18.

Interactioni

Subunit structurei

Monomer. Interacts ith RTN3 and RTN4 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ9JL18.
SMRiQ9JL18. Positions 72-455.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG267436.
GeneTreeiENSGT00710000106265.
HOGENOMiHOG000036572.
InParanoidiQ8C793.
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

MGALLRALLL LVLAQWLLSA VPALAPAPFT LPLQVAGATN HRASAVPGLG    50
TPELPRADGL ALALEPVRAT ANFLAMVDNL QGDSGRGYYL EMLIGTPPQK 100
VQILVDTGSS NFAVAGAPHS YIDTYFDSES SSTYHSKGFD VTVKYTQGSW 150
TGFVGEDLVT IPKGFNSSFL VNIATIFESE NFFLPGIKWN GILGLAYAAL 200
AKPSSSLETF FDSLVAQAKI PDIFSMQMCG AGLPVAGSGT NGGSLVLGGI 250
EPSLYKGDIW YTPIKEEWYY QIEILKLEIG GQNLNLDCRE YNADKAIVDS 300
GTTLLRLPQK VFDAVVEAVA RTSLIPEFSD GFWTGAQLAC WTNSETPWAY 350
FPKISIYLRD ENASRSFRIT ILPQLYIQPM MGAGFNYECY RFGISSSTNA 400
LVIGATVMEG FYVVFDRAQR RVGFAVSPCA EIEGTTVSEI SGPFSTEDIA 450
SNCVPAQALN EPILWIVSYA LMSVCGAILL VLILLLLLPL HCRHAPRDPE 500
VVNDESSLVR HRWK 514
Length:514
Mass (Da):55,800
Last modified:October 1, 2000 - v1
Checksum:iA70725F2C1DF5B47
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → P in BAC34931. 1 Publication
Sequence conflicti11 – 111L → P in BAE38011. 1 Publication
Sequence conflicti11 – 111L → P in BAC37384. 1 Publication
Sequence conflicti37 – 371G → R in BAC34931. 1 Publication
Sequence conflicti37 – 371G → R in BAE38011. 1 Publication
Sequence conflicti37 – 371G → R in BAC37384. 1 Publication
Sequence conflicti53 – 531E → G in BAC37384. 1 Publication
Sequence conflicti369 – 3691I → T in BAC34931. 1 Publication
Sequence conflicti488 – 4881L → V in AAD45964. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS28359.1.
RefSeqi NP_062390.3. NM_019517.4.
UniGenei Mm.97885.

3D structure databases

ProteinModelPortali Q9JL18.
SMRi Q9JL18. Positions 72-455.
ModBasei Search...

Protein family/group databases

MEROPSi A01.041.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047275 ; ENSMUSP00000043918 ; ENSMUSG00000040605 .
GeneIDi 56175.
KEGGi mmu:56175.
UCSCi uc008ade.2. mouse.

Organism-specific databases

CTDi 25825.
MGIi MGI:1860440. Bace2.

Phylogenomic databases

eggNOGi NOG267436.
GeneTreei ENSGT00710000106265.
HOGENOMi HOG000036572.
InParanoidi Q8C793.
KOi K07747.
OrthoDBi EOG7DNNVW.
PhylomeDBi Q9JL18.
TreeFami TF329595.

Miscellaneous databases

ChiTaRSi BACE2. mouse.
NextBioi 311944.
PROi Q9JL18.
SOURCEi Search...

Gene expression databases

Bgeei Q9JL18.
Genevestigatori Q9JL18.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR009119. Pept_A1_BACE.
IPR009121. Pept_A1_BACE2.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR01817. BACE2.
PR01815. BACEFAMILY.
PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 93 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