A cDNA clone encoding a heat-stable sweet protein, mabinlin II (MAB), was isolated and sequenced. The encoded precursor to MAB was composed of 155 amino acid (aa) residues, including a signal sequence of 20 aa, an N-terminal extension peptide of 15 aa, a linker peptide of 14 aa and one residue of C-terminal extension. Comparison of the proteolytic cleavage sites during post-translational processing of MAB precursor with those of like 2S seed-storage proteins of Arabidopsis thaliana, Brassica napus and Bertholletia excelsa shows that the three individual cleavage sites between respective species are conserved.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
A cDNA clone encoding a heat-stable sweet protein, mabinlin II (MAB), was isolated and sequenced. The encoded precursor to MAB was composed of 155 amino acid (aa) residues, including a signal sequence of 20 aa, an N-terminal extension peptide of 15 aa, a linker peptide of 14 aa and one residue of C-terminal extension. Comparison of the proteolytic cleavage sites during post-translational processing of MAB precursor with those of like 2S seed-storage proteins of Arabidopsis thaliana, Brassica napus and Bertholletia excelsa shows that the three individual cleavage sites between respective species are conserved.
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| skos:exactMatch | |
| uniprot:name |
Gene
|
| uniprot:author |
Kurihara Y.,
Masuda Y.,
Nakaya K.,
Nirasawa S.
|
| uniprot:date |
1996
|
| uniprot:pages |
225-227
|
| uniprot:title |
Cloning and sequencing of a cDNA encoding a heat-stable sweet protein, mabinlin II.
|
| uniprot:volume |
181
|
| dc-term:identifier |
doi:10.1016/S0378-1119(96)00465-9
|