SGID Silkworm Genome Informatics Database
Gene
KWMTBOMO13814
Pre Gene Modal
BGIBMGA011551
Annotation
PREDICTED:_beta-secretase_1-like_[Bombyx_mori]
Full name
Beta-secretase 1      
Alternative Name
Beta-site amyloid precursor protein cleaving enzyme 1
Memapsin-2
Membrane-associated aspartic protease 2
Location in the cell
Extracellular   Reliability : 1.726 PlasmaMembrane   Reliability : 1.508
 

Sequence

CDS
ATGGCGAAGCTGTTAATAATTTTTCTCTATTGTATTTGTGCGAATGGAGAACAGTTTAATTTGCAAGGAGATGCCGGCCTTGCCTATTCTGTTGAGGTAATCATGGGACATCCACATCAAAAGATAAACCTTTTAATTGATACTGGTAGCACAACATTAGCTGTTGCTTCATATTCAAGACAAGATAGTGATAAATACTTTGATGCAAACAATTCTAGCAGCATTTATGACAGTGGGAAAAAGGTGCAGGCAACATACTTTGAAGGCAAATGGATTGGCCGTTTAGTCTCAGATTATATACAGCTCCCATCTATGCCATTGGTGCCAGAAGTCAGGACTGATATGGCACTTATTATGGAAAGCCACAATTTTTTTATGAATGGCTCACAATGGCAGGGTCTTCTAGGACTCGCATATCTACCAGTTGGAGCAAGGGGAGCAGATGTAATTGTGGAATCATGGTTAGATTCCCTTGACCGTACTTTGACTAGACCTGTATCATTTCAACTCAAACTTTGTGCTACATTAAGTACACAAAATGCGACGCACTATGGAAACTTTCAGATACTAGATGGTAAACAAAAAAATGAAAATTTAAACAAATCATACCGAACAACTATAATACAAAAAAGGTGGTATGAAGTTGGTGTTTTATCTGTGAGGGTTATGAGACATGTAAATAAATCAAGCAATCCTCCAGACATAGATGAACATATGTGTCAAACGCTTAATAAAATAAAGGCTATAGTTGATAGCGGAACAACAAATATAAGGTTACCTAATTGTTATTTTAGGCAGATTGTTGATGATTTGAGAAGCGCAGCACAGACTTCTAATATGTTAATTACGGATGACTTTTGGTATGCGGGAGAGACTGGATGTTGGCCAGAGCCTCAAGACTGGTCACTACCCTGGGTAGCGGTAGACCTACTTAGCTACGAAGCAGATAACCAGTACTTTACGTTAATGCTGTCGCCGCAGAATTATATGAGAGTCGTGGCAGCACAGAACAGCAGCGGTGAAAGTGGGACCGTATCAGAATACTGTTACAAATTGGGTTTTGAAAAAGGCGGAGATGAAACTGTACTCGGCTATACAGCCATGGAAGGATTTCAGATCAGCCGGTTGGATCGGCTGGCAGACCTCGGACTGTGGTCCAAACACTAA
Protein
MAKLLIIFLYCICANGEQFNLQGDAGLAYSVEVIMGHPHQKINLLIDTGSTTLAVASYSRQDSDKYFDANNSSSIYDSGKKVQATYFEGKWIGRLVSDYIQLPSMPLVPEVRTDMALIMESHNFFMNGSQWQGLLGLAYLPVGARGADVIVESWLDSLDRTLTRPVSFQLKLCATLSTQNATHYGNFQILDGKQKNENLNKSYRTTIIQKRWYEVGVLSVRVMRHVNKSSNPPDIDEHMCQTLNKIKAIVDSGTTNIRLPNCYFRQIVDDLRSAAQTSNMLITDDFWYAGETGCWPEPQDWSLPWVAVDLLSYEADNQYFTLMLSPQNYMRVVAAQNSSGESGTVSEYCYKLGFEKGGDETVLGYTAMEGFQISRLDRLADLGLWSKH

Summary

Description
Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase. Cleaves APP with much more catalytic efficiency than for the wild-type.
Catalytic Activity
Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.
Subunit
Monomer. Interacts (via DXXLL motif) with GGA1, GGA2 and GGA3 (via their VHS domain); the interaction highly increases when BACE1 is phosphorylated at Ser-498. Interacts with RTN3 and RTN4. Interacts with SNX6. Interacts with PCSK9. Interacts with NAT8 and NAT8B. Interacts with BIN1 (By similarity).
Similarity
Belongs to the peptidase A1 family.
Keywords
Acetylation   Aspartyl protease   Cell membrane   Complete proteome   Cytoplasmic vesicle   Disulfide bond   Endoplasmic reticulum   Endosome   Glycoprotein   Golgi apparatus   Hydrolase   Isopeptide bond   Lipoprotein   Lysosome   Membrane   Palmitate   Phosphoprotein   Protease   Reference proteome   Signal   Transmembrane   Transmembrane helix   Ubl conjugation   Zymogen  
Feature
chain  Beta-secretase 1
EC Number
3.4.23.46
EMBL
KQ459037    KPJ04306.1    KQ461195    KPJ06745.1    KZ149950    PZC76678.1    + More
ODYU01001979    SOQ38921.1    RSAL01000004    RVE54625.1    NWSH01003295    PCG66596.1    GDQN01007004    JAT84050.1    PYGN01003650    PSN29455.1    NEVH01011917    PNF31121.1    KK853314    KDR08609.1    PNF31119.1    QUSF01000089    RLV93740.1    AGTO01001800    AHAT01018414    AHAT01018415    AHAT01018416    AHAT01018417    QRBI01000231    RMB91953.1    MUZQ01000188    OWK55692.1    LMAW01003036    KQK74518.1    AADN05000201    AWGT02000038    OXB81343.1    LSYS01008642    OPJ68289.1    RJVU01011952    ROL53209.1    HAEH01006380    SBR79077.1    HAED01006822    HAEE01010908    SBQ92948.1    HADZ01014130    HAEA01002783    SBP78071.1    HAEJ01002370    SBS42827.1    HAEI01003223    SBR83712.1    HAEB01019932    HAEC01000039    SBQ66459.1    HAEF01017408    HAEG01015172    SBR58567.1    AYCK01017144    KQ042328    KKF15961.1    AKHW03004818    KYO28703.1    AFYH01011934    AFYH01011935    AFYH01011936    GBHZ01000012    JAC94887.1    AERX01021523    KB105943    ELK31936.1    FR904426    CDQ63041.1    JH818774    EKC26973.1    AAPE02046303    AAPE02046304    AAPE02046305    AAPE02046306    AAPE02046307    AAPE02046308    BC065973    AAH65973.1    GBUG01000020    JAC96612.1    CM004479    OCT70472.1    CP026245    AWO99323.1    GCES01063437    JAR22886.1    GBIB01000010    JAC95042.1    AK046175    BAC32620.1    KN122326    KFO31095.1    AGTP01052904    LZPO01075906    OBS68517.1    AAQR03130901    AAQR03130902    GJ062397    DAA22394.1    BC113325    FR904313    CDQ58854.1   
Pfam
PF00026   Asp        + More
PF14541   TAXi_C
PF01359   Transposase_1
Interpro
IPR021109   Peptidase_aspartic_dom_sf        + More
IPR009120   BACE1       
IPR033121   PEPTIDASE_A1       
IPR001461   Aspartic_peptidase_A1       
IPR001969   Aspartic_peptidase_AS       
IPR032799   TAXi_C       
IPR009121   BACE2       
IPR001888   Transposase_1       
IPR009119   BACE       
IPR033874   Memapsin-like       
SUPFAM
SSF50630   SSF50630       
Gene 3D
PDB
6BFX     E-value=5.60752e-46,     Score=464

Ontologies

Topology

Subcellular location
Cell membrane   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Golgi apparatus   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
trans-Golgi network   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Endoplasmic reticulum   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Endosome   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Cell surface   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Cytoplasmic vesicle membrane   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Membrane raft   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Lysosome   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Late endosome   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Early endosome   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
Recycling endosome   Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface (By similarity). Colocalization with APP in early endosomes is due to addition of bisecting N-acetylglucosamine wich blocks targeting to late endosomes and lysosomes (By similarity). Retrogradly transported from endosomal compartments to the trans-Golgi network in a phosphorylation- and GGA1- dependent manner (By similarity).   With evidence from 2 publications.
SignalP
Position:   1 - 16,         Likelihood:  0.977551
 
 
Length:
388
Number of predicted TMHs:
0
Exp number of AAs in TMHs:
0.01044
Exp number, first 60 AAs:
0.0063
Total prob of N-in:
0.00217
outside
1  -  388
 
 

Population Genetic Test Statistics

Pi
254.515329
Theta
190.445741
Tajima's D
1.106975
CLR
0.246682
CSRT
0.683965801709915
Interpretation
Uncertain
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