Proline Rich G Carboxyglutamic Acid 2 (PRRG2)

PRGP2 carboxylation and propeptide processing were concerted and sequentially ordered processes in Chinese hamster ovary cells, and that carboxylation was rate limiting. Sequence analysis suggested that the N-terminal Gla domain of PRGP2 is exposed to the ER lumen and that the C terminus is cytoplasmic.Yeast 2-hybrid analysis revealed that the cytoplasmic tail of PRGP2 interacted with a YAP (YAP1) isoform containing 2 type I WW domains. Both PY motifs of PRGP2 and both WW domains of YAP were required to form a tight complex.The presence of an N-terminal signal peptide and a putative transmembrane region defines PRRG2 as a type I single-pass transmembrane protein with the C terminus oriented to the cytoplasm.