HICF2: PLPPR5 R117C
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HIFC2 entry with custom annotation ported to Michelanglo.
PLPPR5, also known as PRG5, is a transmembrane protein that is phospholipid phosphatase.
These compound heterozygous have different effects. L13F is destabilising and alters binding site of the phospholipid.
While R117C is a surface mutation and harder to tell.
The structure of distant homologue know. Mutation R117C is on an outside loop of this transmembrane protein. This loop is conserved within PRG5. The arginine is a part a cytosol facing di-arginine motif which is a signal for ER locationsation, which is a first step towards plasma membrane localisation.
Cysteine is a cross-linking residue so there is a possibility it could be affecting other cysteines. It is a cytosolic loop so it is unlikely to start with. But if the loop has a potential disulphide bond and the extra cysteine may be altering its shape. In terms of disulphide crosslinks, not all options were tested due to my struggling with disulfides, but R117C disulfides scored worse than unbound, so are unlikely.