Difference between revisions of "YPR075C"

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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://db.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006279 YPR075C]  
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Systematic name''' || [http://www.yeastgenome.org/cgi-bin/locus.pl?dbid=S000006279 YPR075C]  
 
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|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''OPY2 ''
 
|valign="top" nowrap bgcolor="{{SGDblue}}"| '''Gene name'''        ||''OPY2 ''
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== Transmembrane Domain GxxxG  ==
  
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The transmembrane domain of Opy2p shows homology with the SKG6/AXL2 alpha-helix transmembrane domain (IPR014805). In particular, this domain contains GftvGivgG. 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 Opy2p dimerises.
  
  

Latest revision as of 09:28, 21 March 2013

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Systematic name YPR075C
Gene name OPY2
Aliases
Feature type ORF, Verified
Coordinates Chr XVI:696819..695737
Primary SGDID S000006279


Description of YPR075C: Integral membrane protein that functions in the signaling branch of the high-osmolarity glycerol (HOG) pathway; interacts with Ste50p; overproduction blocks cell cycle arrest in the presence of mating pheromone[1][2]




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Community Commentary

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Transmembrane Domain GxxxG

The transmembrane domain of Opy2p shows homology with the SKG6/AXL2 alpha-helix transmembrane domain (IPR014805). In particular, this domain contains GftvGivgG. The presence of multiple, overlapping GxxxG motifs [3] strongly indicates that Opy2p dimerises.



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References

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  1. Edwards MC, et al. (1997) Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells. Genetics 147(3):1063-76 SGD PMID 9383053
  2. Wu C, et al. (2006) Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association. Genes Dev 20(6):734-46 SGD PMID 16543225
  3. 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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