Cloning of a full-length complementary DNA for an Artemia salina glycine-rich protein. Structural relationship with RNA binding proteins.
Overlapping cDNAs have been isolated containing all the coding sequences for Artemia salina protein GRP33, a glycine-rich protein (16.6 mol % glycine), with a molecular weight of 32,992. GRP33 is closely related to HD40, the major protein component of Artemia heterogeneous nuclear ribonucleoprotein particles, and shares certain characteristics with other RNA binding proteins. The C-terminal region (123 amino acids) contains 39 glycine residues. This region has multiple arginine residues flanked by glycines, resembling the glycine-dimethylarginine clusters present in other RNA binding proteins. Secondary structure predictions for the protein reveal two distinct domains: a hydrophilic C-terminal domain with an extended conformation and a larger N-terminal domain with a number of alpha-helices and beta-sheets.
D000595:Amino Acid Sequence; D000818:Animals; D001156:Artemia / Q000235:genetics*; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism*; D019476:Insect Proteins; D007447:Invertebrate Hormones / Q000235:genetics*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins
D002352:Carrier Proteins; C053819:GRP33 protein, Artemia salina; D019476:Insect Proteins; D007447:Invertebrate Hormones; D016601:RNA-Binding Proteins; D012313:RNA; D004247:DNA