BACE_STRPU
ID BACE_STRPU Reviewed; 540 AA.
AC W8W138; W4ZI74;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Beta-secretase {ECO:0000303|PubMed:24381583};
DE EC=3.4.23.- {ECO:0000305};
DE Flags: Precursor;
GN Name=BACE {ECO:0000312|EMBL:CCQ18550.1};
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=22709795; DOI=10.1101/gr.139170.112;
RA Tu Q., Cameron R.A., Worley K.C., Gibbs R.A., Davidson E.H.;
RT "Gene structure in the sea urchin Strongylocentrotus purpuratus based on
RT transcriptome analysis.";
RL Genome Res. 22:2079-2087(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Deng J., Liu Y., Angeri F., Arias F., Bandaranaike D., Bess C.,
RA Blankenburg K., Chen D., Deiros R.D.R., Denson S., Dinh H., Francisco L.,
RA Fu Q., Gubbala S., Han Y., Hiang H., Javaid M., Jayaseelan J.C., Jing C.,
RA Jones J., Korchina V., Lara F., Lee S., Li H., Mims S., Munidasa M.,
RA Ngo R., Nguyen L., Ongeri F., Osuji N., Palculict T., Patil S., Paul S.,
RA Pellon M., Perales L., Pu L., Puazo M., Qin X., Qu C., Raj R., Saada N.,
RA Shafer J., Shah N., Song H., Tang L., Vee V., Wang Y., Weissenberger G.,
RA Xin Y., Nazareth L., Newsham I., Wang M., Wu Y., Worley K.C., Reid J.G.,
RA Han Y., Muzny D.M., Gibbs R.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:CCQ18550.1}
RP IDENTIFICATION.
RX PubMed=24381583; DOI=10.3389/fgene.2013.00293;
RA Southan C., Hancock J.M.;
RT "A tale of two drug targets: the evolutionary history of BACE1 and BACE2.";
RL Front. Genet. 4:293-293(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000255|RuleBase:RU000454}.
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DR EMBL; JT121371; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; HE967761; CCQ18550.1; -; mRNA.
DR RefSeq; NP_001278230.1; NM_001291301.1.
DR AlphaFoldDB; W8W138; -.
DR SMR; W8W138; -.
DR STRING; 7668.SPU_027888-tr; -.
DR EnsemblMetazoa; NM_001291301; NP_001278230; GeneID_585631.
DR GeneID; 585631; -.
DR KEGG; spu:585631; -.
DR CTD; 34182; -.
DR eggNOG; KOG1339; Eukaryota.
DR OMA; ELEDCGY; -.
DR OrthoDB; 753343at2759; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0050435; P:amyloid-beta metabolic process; IBA:GO_Central.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05473; beta_secretase_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR009119; BACE.
DR InterPro; IPR009120; BACE1.
DR InterPro; IPR033874; Memapsin-like.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47965; PTHR47965; 1.
DR PANTHER; PTHR47965:SF69; PTHR47965:SF69; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR01815; BACEFAMILY.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Disulfide bond; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT PROPEP 32..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000432827"
FT CHAIN ?..540
FT /note="Beta-secretase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432828"
FT TOPO_DOM ?..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 81..435
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 302
FT /evidence="ECO:0000305"
FT DISULFID 222..439
FT /evidence="ECO:0000250|UniProtKB:P56817"
FT DISULFID 291..469
FT /evidence="ECO:0000250|UniProtKB:P56817"
FT DISULFID 345..397
FT /evidence="ECO:0000250|UniProtKB:P56817"
SQ SEQUENCE 540 AA; 59336 MW; 1AD432042D105EE6 CRC64;
MHFSLPTSRI VVVVPAAAIC IVCVLIETCT AARSHVYTIP LRKGKETSFA ETVGEPVRTN
QVNVSVEEQK NNIRGRPGLG YYIEVDIGTP PQKLNVLIDT GSSNFAVAAS SHNAISTYYR
RNESSTYEDQ GTYVKVPYTQ GEWSGDLGQD LVQIASLGNQ SFQANIAAIT ESKMFFLNDS
RWQGILGLGY AEIARPDSSV EPFFDSLTSQ TSIQDIFALQ MCGALASTND TNLGSSADGP
VEEVIGSMNI GGLDASLYHG TMQYAPLRDE WFYEVIMTDI RVGNDSLGLD CKEYNFDKTI
VDSGTTNLRL PVRVFEAITN AIKAHTTKHM PDVPSEFWTG MNLMCPTDST SPYEPYHWFP
TLTLDLQSTN QGQAFSLVVS PQQYLRRDYD HEDKKNCFKF AIAPSTNHAG AVIGAVIMEG
FYVVFDRENK RVGFARSTCP GACEKTGTCV GNSPLITEAF NIDFDASDCG YDRSTSYDPA
LTITAYVLAA ICLVCLIPVI VFALTHQINK RCKGRRGRGV VNHHRLDQEG LAENEPNSDP
