HICF2: GRM4 R44H
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HIFC2 entry with custom annotation ported to Michelanglo.
This mutation is close to the surface of the N-terminal domain (extracellular), which forms the receiving part of the receptor. But the mutation is not at the dimerisation intereface.
R44H cannot salt bridge with E133 in the model, but it is a large fold and this is probably too far from the binding site to have an effect. In GRM8 R41 is still flanked by R101, but there is no salt bridging Glutamate. They are simply in the air on the side opposite the membrane. I don't think this is a di-Arginine ER retention motif as it is a plasma membrane protein...
It is not a glycosylated arginine. But it is a very conserved residue.
This variant exists in 16 ExAC patients (none homozygous). Likewise R104C in 4.
If something binds it is not known...
paper about crystal structure of homologue link