LOCUS       NP_062077                501 aa            linear   ROD 18-MAR-2025
DEFINITION  beta-secretase 1 precursor [Rattus norvegicus].
ACCESSION   NP_062077
VERSION     NP_062077.1
DBSOURCE    REFSEQ: accession NM_019204.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 501)
  AUTHORS   Velazquez Toledano,J., Bello,M., Correa Basurto,J., Guerrero
            Gonzalez,I., Pacheco-Yepez,J. and Rosales Hernandez,M.C.
  TITLE     Determining Structural Changes for Ligand Recognition between Human
            and Rat Phosphorylated BACE1 in Silico and Its Phosphorylation by
            GSK3beta at Thr252 by in Vitro Studies
  JOURNAL   ACS Chem Neurosci 15 (3), 629-644 (2024)
   PUBMED   38227464
  REMARK    GeneRIF: Determining Structural Changes for Ligand Recognition
            between Human and Rat Phosphorylated BACE1 in Silico and Its
            Phosphorylation by GSK3beta at Thr252 by in Vitro Studies.
REFERENCE   2  (residues 1 to 501)
  AUTHORS   Wang,X., Li,M. and Hu,Y.
  TITLE     miR-29c-3p Attenuates beta-Amyloid-Induced Neurotoxicity in
            Alzheimer's Disease Through Regulating beta-Site Amyloid Precursor
            Protein-Cleaving Enzyme 1
  JOURNAL   Physiol Res 72 (6), 833-841 (2023)
   PUBMED   38215068
  REMARK    GeneRIF: miR-29c-3p Attenuates beta-Amyloid-Induced Neurotoxicity
            in Alzheimer's Disease Through Regulating beta-Site Amyloid
            Precursor Protein-Cleaving Enzyme 1.
REFERENCE   3  (residues 1 to 501)
  AUTHORS   Qu,J., Xiong,X., Hujie,G., Ren,J., Yan,L. and Ma,L.
  TITLE     MicroRNA-132-3p alleviates neuron apoptosis and impairments of
            learning and memory abilities in Alzheimer's disease by
            downregulation of HNRNPU stabilized BACE1
  JOURNAL   Cell Cycle 20 (21), 2309-2320 (2021)
   PUBMED   34585626
  REMARK    GeneRIF: MicroRNA-132-3p alleviates neuron apoptosis and
            impairments of learning and memory abilities in Alzheimer's disease
            by downregulation of HNRNPU stabilized BACE1.
REFERENCE   4  (residues 1 to 501)
  AUTHORS   Babusikova,E., Dobrota,D., Turner,A.J. and Nalivaeva,N.N.
  TITLE     Effect of Global Brain Ischemia on Amyloid Precursor Protein
            Metabolism and Expression of Amyloid-Degrading Enzymes in Rat
            Cortex: Role in Pathogenesis of Alzheimer's Disease
  JOURNAL   Biochemistry (Mosc) 86 (6), 680-692 (2021)
   PUBMED   34225591
  REMARK    GeneRIF: Effect of Global Brain Ischemia on Amyloid Precursor
            Protein Metabolism and Expression of Amyloid-Degrading Enzymes in
            Rat Cortex: Role in Pathogenesis of Alzheimer's Disease.
REFERENCE   5  (residues 1 to 501)
  AUTHORS   De Pietri Tonelli,D., Mihailovich,M., Di Cesare,A., Codazzi,F.,
            Grohovaz,F. and Zacchetti,D.
  TITLE     Translational regulation of BACE-1 expression in neuronal and
            non-neuronal cells
  JOURNAL   Nucleic Acids Res 32 (5), 1808-1817 (2004)
   PUBMED   15034149
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 501)
  AUTHORS   Rogers,G.W. Jr., Edelman,G.M. and Mauro,V.P.
  TITLE     Differential utilization of upstream AUGs in the beta-secretase
            mRNA suggests that a shunting mechanism regulates translation
  JOURNAL   Proc Natl Acad Sci U S A 101 (9), 2794-2799 (2004)
   PUBMED   14981268
REFERENCE   7  (residues 1 to 501)
  AUTHORS   Yan,R., Han,P., Miao,H., Greengard,P. and Xu,H.
  TITLE     The transmembrane domain of the Alzheimer's beta-secretase (BACE1)
            determines its late Golgi localization and access to beta -amyloid
            precursor protein (APP) substrate
  JOURNAL   J Biol Chem 276 (39), 36788-36796 (2001)
   PUBMED   11466313
REFERENCE   8  (residues 1 to 501)
  AUTHORS   Lin,X., Koelsch,G., Wu,S., Downs,D., Dashti,A. and Tang,J.
  TITLE     Human aspartic protease memapsin 2 cleaves the beta-secretase site
            of beta-amyloid precursor protein
  JOURNAL   Proc Natl Acad Sci U S A 97 (4), 1456-1460 (2000)
   PUBMED   10677483
REFERENCE   9  (residues 1 to 501)
  AUTHORS   Vassar,R., Bennett,B.D., Babu-Khan,S., Kahn,S., Mendiaz,E.A.,
            Denis,P., Teplow,D.B., Ross,S., Amarante,P., Loeloff,R., Luo,Y.,
            Fisher,S., Fuller,J., Edenson,S., Lile,J., Jarosinski,M.A.,
            Biere,A.L., Curran,E., Burgess,T., Louis,J.C., Collins,F.,
            Treanor,J., Rogers,G. and Citron,M.
  TITLE     Beta-secretase cleavage of Alzheimer's amyloid precursor protein by
            the transmembrane aspartic protease BACE
  JOURNAL   Science 286 (5440), 735-741 (1999)
   PUBMED   10531052
REFERENCE   10 (residues 1 to 501)
  AUTHORS   Urmoneit,B., Reinsch,C., Turner,J., Czech,C., Beyreuther,K. and
            Dyrks,T.
  TITLE     Inhibition of beta A4 production by specific modulation of
            beta-secretase activity
  JOURNAL   J Mol Neurosci 6 (1), 23-32 (1995)
   PUBMED   8562317
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AF190727.1 and JAXUCZ010000008.1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF190727.1, SRR26643287.19966.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760389
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            regulatory uORF        :: PMID: 14981268
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..501
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="8"
                     /map="8q22"
     Protein         1..501
                     /product="beta-secretase 1 precursor"
                     /EC_number="3.4.23.46"
                     /note="ASP2; asp 2; memapsin-2; aspartyl protease 2;
                     membrane-associated aspartic protease 2; beta-site amyloid
                     precursor protein cleaving enzyme 1; beta-site APP
                     cleaving enzyme 1"
                     /calculated_mol_wt=53557
     sig_peptide     1..21
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2268
     mat_peptide     46..501
                     /product="Beta-secretase 1. /id=PRO_0000025944"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
                     /calculated_mol_wt=51014
     Region          72..437
                     /region_name="beta_secretase_like"
                     /note="Beta-secretase, aspartic-acid protease important in
                     the pathogenesis of Alzheimer's disease; cd05473"
                     /db_xref="CDD:133140"
     Site            order(72,93,95,132..134,171,189,259,289,291..293,368,382)
                     /site_type="active"
                     /note="inhibitor binding site [active]"
                     /db_xref="CDD:133140"
     Site            order(93..96,289..292)
                     /site_type="active"
                     /note="catalytic motif [active]"
                     /db_xref="CDD:133140"
     Site            order(93,289)
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:133140"
     Site            126
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            order(129..132,136..139)
                     /site_type="active"
                     /note="Active site flap [active]"
                     /db_xref="CDD:133140"
     Site            153
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            172
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            223
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            275
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            279
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            285
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            299
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            300
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            307
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P56817; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            354
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     Site            458..478
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
     Region          479..501
                     /region_name="Interaction with RTN3.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
     Region          496..500
                     /region_name="DXXLL.
                     /evidence=ECO:0000250|UniProtKB:P56817"
                     /note="propagated from UniProtKB/Swiss-Prot (P56819.1)"
     Site            498
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56818; propagated from
                     UniProtKB/Swiss-Prot (P56819.1)"
     CDS             1..501
                     /gene="Bace1"
                     /gene_synonym="Bace"
                     /coded_by="NM_019204.2:428..1933"
                     /db_xref="GeneID:29392"
                     /db_xref="RGD:2191"
ORIGIN      
        1 mapalrwlll wvgsgmlpaq gthlgirlpl rsglagpplg lrlpretdee peepgrrgsf
       61 vemvdnlrgk sgqgyyvemt vgsppqtlni lvdtgssnfa vgaaphpflh ryyqrqlsst
      121 yrdlrksvyv pytqgkwege lgtdlvsiph gpnvtvrani aaitesdkff ingsnwegil
      181 glayaeiarp ddslepffds lvkqthipni fslqlcgagf plnqtealas vggsmiiggi
      241 dhslytgslw ytpirrewyy eviivrvein gqdlkmdcke ynydksivds gttnlrlpkk
      301 vfeaavksik aasstekfpd gfwlgeqlvc wqagttpwni fpvislylmg evtnqsfrit
      361 ilpqqylrpv edvatsqddc ykfavsqsst gtvmgavime gfyvvfdrar krigfavsac
      421 hvhdefrtaa vegpfvtadm edcgynipqt destlmtiay vmaaicalfm lplclmvcqw
      481 rclrclrhqh ddfaddisll k
//
