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
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
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
Population Genetic Test Statistics