ID L8YFG8_TUPCH Unreviewed; 683 AA.
AC L8YFG8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Beta-secretase 1 {ECO:0000256|ARBA:ARBA00017314};
DE EC=3.4.23.46 {ECO:0000256|ARBA:ARBA00013261};
DE AltName: Full=Beta-site amyloid precursor protein cleaving enzyme 1 {ECO:0000256|ARBA:ARBA00031276};
DE AltName: Full=Memapsin-2 {ECO:0000256|ARBA:ARBA00032591};
DE AltName: Full=Membrane-associated aspartic protease 2 {ECO:0000256|ARBA:ARBA00032613};
GN ORFNames=TREES_T100007974 {ECO:0000313|EMBL:ELV13879.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV13879.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-
CC Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid
CC precursor protein.; EC=3.4.23.46;
CC Evidence={ECO:0000256|ARBA:ARBA00000187};
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Early endosome
CC {ECO:0000256|ARBA:ARBA00004412}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|ARBA:ARBA00004601}. Late endosome
CC {ECO:0000256|ARBA:ARBA00004603}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Recycling endosome
CC {ECO:0000256|ARBA:ARBA00004172}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; KB360263; ELV13879.1; -; Genomic_DNA.
DR STRING; 246437.L8YFG8; -.
DR eggNOG; KOG1339; Eukaryota.
DR InParanoid; L8YFG8; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR009120; BACE1.
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:SF69; BETA-SECRETASE 1; 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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023139};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 257..598
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 17..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 471
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 683 AA; 75704 MW; 0B47E5BA874B15D1 CRC64;
MLQGGLRLGR GHRRPLSTGA CLPCHGKTTL PSDPREKRKP FGFDSRHHKS FRLPSPPGSW
ELGAGLWWPE SQRSRGSPAE AGRSPPDVAG FRIPCSASPV PRGFLLPGPG EWPRACRLWS
PDASTLPFLR GHQQHPDLGA CDRNERGLEP AQRAQRPGPA MAPALPWLLL WVGCGLLPAQ
GTQHGIRLPL RSGLGGNPLG LRLAPGTEEE AEEXXXXXXX XGWRLPRETD EEPEEPGRRG
SFVEMVDNLR GKSGQGYYVE MTVGSPPQTL NILVDTGSSN FAVGAAPHPF LHRYYQRQLS
STYRDLRKGV YVPYTQGKWE GELGTDLVSI PHGPNVTVRA NIAAITESDK FFINGSNWEG
ILGLAYAEIA RPDDSLEPFF DSLVKQTHVP NLFSLQLCGT GFPLNQSEVL ASVGGSMIIG
GIDHSLYTGS LWYTPIRREW YYEVIIVRVE INGQDLNMDC KEYNYDKSIV DSGTTNLRLP
KKVFEAAVKS IKAASSTEKF PDGFWLGEQL VCWQAGTTPW NIFPVISLYL MGEVTNQSFR
ITILPQQYLR PVEDVATSQD DCYKFAISQS STGTVMGAVI MEGFYVVFDR ARKRIGFAVS
ACHVHDEFRT AAVEGPFVTP DMEDCGYNIP QTDESTLMTI AYVMAAICAL FMLPLCLMVC
QWRCLRCLRH QHDDFADDIS LLK
//
