GenomeNet

Database: UniProt
Entry: A0A0R4J0I8_MOUSE
LinkDB: A0A0R4J0I8_MOUSE
Original site: A0A0R4J0I8_MOUSE 
ID   A0A0R4J0I8_MOUSE        Unreviewed;       514 AA.
AC   A0A0R4J0I8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Beta-site APP-cleaving enzyme 2 {ECO:0000313|Ensembl:ENSMUSP00000043918.7};
GN   Name=Bace2 {ECO:0000313|Ensembl:ENSMUSP00000043918.7,
GN   ECO:0000313|MGI:MGI:1860440};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000043918.7, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000043918.7, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000043918.7,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000043918.7}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000043918.7};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000256|ARBA:ARBA00004240}. Endosome
CC       {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; NP_062390.3; NM_019517.5.
DR   AlphaFoldDB; A0A0R4J0I8; -.
DR   SMR; A0A0R4J0I8; -.
DR   ProteomicsDB; 359545; -.
DR   Antibodypedia; 4410; 603 antibodies from 38 providers.
DR   DNASU; 56175; -.
DR   Ensembl; ENSMUST00000047275.8; ENSMUSP00000043918.7; ENSMUSG00000040605.8.
DR   GeneID; 56175; -.
DR   KEGG; mmu:56175; -.
DR   AGR; MGI:1860440; -.
DR   CTD; 25825; -.
DR   MGI; MGI:1860440; Bace2.
DR   VEuPathDB; HostDB:ENSMUSG00000040605; -.
DR   GeneTree; ENSGT00940000159548; -.
DR   OMA; KEWYYQV; -.
DR   OrthoDB; 603414at2759; -.
DR   PhylomeDB; A0A0R4J0I8; -.
DR   BioGRID-ORCS; 56175; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Bace2; mouse.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000040605; Expressed in pyloric antrum and 157 other cell types or tissues.
DR   ExpressionAtlas; A0A0R4J0I8; baseline and differential.
DR   GO; GO:0031045; C:dense core granule; IEA:Ensembl.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0033162; C:melanosome membrane; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0032438; P:melanosome organization; IEA:Ensembl.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR   GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   CDD; cd05473; beta_secretase_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR009119; BACE.
DR   InterPro; IPR009121; BACE2.
DR   InterPro; IPR033874; Memapsin-like.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR   PANTHER; PTHR47965:SF40; BETA-SECRETASE 2; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR01817; BACE2.
DR   PRINTS; PR01815; BACEFAMILY.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR609121-2};
KW   Glycoprotein {ECO:0000256|PIRSR:PIRSR609121-3};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU000454};
KW   Proteomics identification {ECO:0007829|MaxQB:A0A0R4J0I8,
KW   ECO:0007829|ProteomicsDB:A0A0R4J0I8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..514
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006451978"
FT   TRANSMEM        463..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..425
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        106
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-3"
FT   DISULFID        229..429
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT   DISULFID        288..453
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
FT   DISULFID        340..389
FT                   /evidence="ECO:0000256|PIRSR:PIRSR609121-2"
SQ   SEQUENCE   514 AA;  55883 MW;  2A3055EF6AA90230 CRC64;
     MGALLRALLL PVLAQWLLSA VPALAPAPFT LPLQVARATN HRASAVPGLG TPELPRADGL
     ALALEPVRAT ANFLAMVDNL QGDSGRGYYL EMLIGTPPQK VQILVDTGSS NFAVAGAPHS
     YIDTYFDSES SSTYHSKGFD VTVKYTQGSW TGFVGEDLVT IPKGFNSSFL VNIATIFESE
     NFFLPGIKWN GILGLAYAAL AKPSSSLETF FDSLVAQAKI PDIFSMQMCG AGLPVAGSGT
     NGGSLVLGGI EPSLYKGDIW YTPIKEEWYY QIEILKLEIG GQNLNLDCRE YNADKAIVDS
     GTTLLRLPQK VFDAVVEAVA RTSLIPEFSD GFWTGAQLAC WTNSETPWAY FPKISIYLRD
     ENASRSFRIT ILPQLYIQPM MGAGFNYECY RFGISSSTNA LVIGATVMEG FYVVFDRAQR
     RVGFAVSPCA EIEGTTVSEI SGPFSTEDIA SNCVPAQALN EPILWIVSYA LMSVCGAILL
     VLILLLLLPL HCRHAPRDPE VVNDESSLVR HRWK
//
DBGET integrated database retrieval system