ID Q5XJ89_DANRE Unreviewed; 372 AA.
AC Q5XJ89; A0A8N7XJE1; B2GP45; F1QIH8;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 143.
DE SubName: Full=Beta-secretase 2 {ECO:0000313|Ensembl:ENSDARP00000065823, ECO:0000313|RefSeq:NP_001005991.1};
DE EC=3.4.23.45 {ECO:0000313|RefSeq:NP_001005991.1};
DE SubName: Full=Zgc:103530 {ECO:0000313|EMBL:AAH83415.1, ECO:0000313|EMBL:AAI64206.1};
GN Name=bace2 {ECO:0000313|Ensembl:ENSDARP00000065823,
GN ECO:0000313|RefSeq:NP_001005991.1,
GN ECO:0000313|ZFIN:ZDB-GENE-041010-68};
GN Synonyms=fi26d02 {ECO:0000313|RefSeq:NP_001005991.1}, wu:fi26d02
GN {ECO:0000313|RefSeq:NP_001005991.1}, zbace
GN {ECO:0000313|RefSeq:NP_001005991.1}, zgc:103530
GN {ECO:0000313|EMBL:AAH83415.1, ECO:0000313|RefSeq:NP_001005991.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI64206.1};
RN [1] {ECO:0000313|RefSeq:NP_001005991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10873463;
RA Sauder J.M., Arthur J.W., Dunbrack RL J.r.;
RT "Modeling of substrate specificity of the Alzheimer's disease amyloid
RT precursor protein beta-secretase.";
RL J. Mol. Biol. 300:241-248(2000).
RN [2] {ECO:0000313|EMBL:AAI64206.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000313|EMBL:AAH83415.1}, and PCR rescue
RC {ECO:0000313|EMBL:AAI64206.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000065823}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000065823};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [4] {ECO:0000313|RefSeq:NP_001005991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23527866;
RA Walter J.;
RT "Fishing for function--distinct roles of Bace1 and Bace2 in Zebrafish
RT development.";
RL J. Neurochem. 127:435-437(2013).
RN [5] {ECO:0000313|RefSeq:NP_001005991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23406323; DOI=10.1111/jnc.12198;
RA van Bebber F., Hruscha A., Willem M., Schmid B., Haass C.;
RT "Loss of Bace2 in zebrafish affects melanocyte migration and is distinct
RT from Bace1 knock out phenotypes.";
RL J. Neurochem. 127:471-481(2013).
RN [6] {ECO:0000313|Ensembl:ENSDARP00000065823, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000065823};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [7] {ECO:0000313|RefSeq:NP_001005991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [8] {ECO:0000313|RefSeq:NP_001005991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29804876;
RA Zhang Y.M., Zimmer M.A., Guardia T., Callahan S.J., Mondal C.,
RA Di Martino J., Takagi T., Fennell M., Garippa R., Campbell N.R.,
RA Bravo-Cordero J.J., White R.M.;
RT "Distant Insulin Signaling Regulates Vertebrate Pigmentation through the
RT Sheddase Bace2.";
RL Dev. Cell 45:580-594(2018).
RN [9] {ECO:0000313|RefSeq:NP_001005991.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {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 EMBL; CABZ01056409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01057324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU856515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC083415; AAH83415.1; -; mRNA.
DR EMBL; BC164206; AAI64206.1; -; mRNA.
DR RefSeq; NP_001005991.1; NM_001005991.2.
DR STRING; 7955.ENSDARP00000065823; -.
DR MEROPS; A01.041; -.
DR PaxDb; 7955-ENSDARP00000065823; -.
DR Ensembl; ENSDART00000065824; ENSDARP00000065823; ENSDARG00000044781.
DR Ensembl; ENSDART00000065824.6; ENSDARP00000065823.6; ENSDARG00000044781.7.
DR GeneID; 449818; -.
DR KEGG; dre:449818; -.
DR AGR; ZFIN:ZDB-GENE-041010-68; -.
DR CTD; 25825; -.
DR ZFIN; ZDB-GENE-041010-68; bace2.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_039009_0_0_1; -.
DR OMA; FGEMLLY; -.
DR OrthoDB; 603414at2759; -.
DR Proteomes; UP000000437; Chromosome 15.
DR Bgee; ENSDARG00000044781; Expressed in mature ovarian follicle and 23 other cell types or tissues.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0048484; P:enteric nervous system development; IMP:ZFIN.
DR GO; GO:0097324; P:melanocyte migration; IMP:ZFIN.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
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; IPR009120; BACE1.
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; PR01816; BACE1.
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 2: Evidence at transcript level;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001005991.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..372
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001005991.1"
FT /id="PRO_5035034097"
FT DOMAIN 80..372
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 98
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 372 AA; 40577 MW; D1A82CA210D593AB CRC64;
MRLYGLLLLS LTFWKSHSVF KIPLNIFAGK FNASVQLDLR PLQKNEAAAK SGLSLASDPA
GIVNFLDMIN NLKGDSGRGY YMQMIIGTPG QTLNILVDTG SSNFAVAAAA HPYITHYFNR
ALSSTYQSTE RAVAVKYTQG EWEGELGTDL ITIPEGPSGA ITINIAAILT SEGFFLPGIN
WQGILGLAYP LLARPDPSVE PFFNSVVRQT GIPDVFSLQM CGAGVPASTT GDPAGGSLIM
GGVEPTLHRG PIWYTPVLEE WYYQVEVLKL EVGDQNLNLD CKEYNSDKAI VDSGTTLLRL
PANVFTAVVD TIMQTSLIDD FSAGFFDGTK LACWMRGESP WRFFPKVSIY LRGTNTSQSF
RITILPQVRI VP
//
