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}.
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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
//