Difference between revisions of "YDL211C"
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| − | == | + | == Transmembrane Domain GxxxG == |
| − | Transmembrane Domain GxxxG == | ||
| − | The transmembrane domain of | + | The transmembrane domain of Ydl211c shows homology with the SKG6/AXL2 alpha-helix transmembrane domain (IPR014805). In particular, this domain begins with tGvivGstvGvviG. The presence of multiple, overlapping GxxxG motifs <ref name='PMID 15313242'> Senes A, Engel DE and DeGrado WF (2004) Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr Opin Struct Biol. 2004 14(4):465-79. PMID 15313242</ref> strongly indicates that ydl211c multimerises. |
Latest revision as of 08:14, 21 March 2013
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| Systematic name | YDL211C |
| Gene name | |
| Aliases | |
| Feature type | ORF, Uncharacterized |
| Coordinates | Chr IV:80412..79294 |
| Primary SGDID | S000002370 |
Description of YDL211C: Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the vacuole[1]
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Community Commentary
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Transmembrane Domain GxxxG
The transmembrane domain of Ydl211c shows homology with the SKG6/AXL2 alpha-helix transmembrane domain (IPR014805). In particular, this domain begins with tGvivGstvGvviG. The presence of multiple, overlapping GxxxG motifs [2] strongly indicates that ydl211c multimerises.
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References
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- ↑ Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91 SGD PMID 14562095
- ↑ Senes A, Engel DE and DeGrado WF (2004) Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr Opin Struct Biol. 2004 14(4):465-79. PMID 15313242
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