The human RD protein is closely related to nuclear RNA-binding proteins and has been highly conserved.
We have isolated cDNA clones encoding the human RD protein, which is closely related to several known nuclear RNA-binding proteins. The RD protein contains a 60-amino acid (aa) tract consisting almost entirely of alternating basic and acidic aa, (RD)n, primarily arginine (Arg; R) and aspartic acid (Asp; D). The protein also contains an 'RNP sequence domain'. Arg-rich tracts and the RNP sequence domain are both features of nuclear RNA-binding proteins. However, we have been unable to detect RNA-binding by the human RD protein. The very strong evolutionary conservation of the mammalian RD protein aa sequence suggests that it plays an important role in the cell.
Surowy
C S
CS
Department of Medical Genetics, University of Wisconsin, Madison 53706.
Hoganson
G
G
Gosink
J
J
Strunk
K
K
Spritz
R A
RA
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D002352:Carrier Proteins / Q000235:genetics*; D004247:DNA / Q000235:genetics; D015698:Genomic Library; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000235:genetics*; D012333:RNA, Messenger / Q000096:biosynthesis; D016601:RNA-Binding Proteins; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors; D035602:Transcriptional Elongation Factors
D002352:Carrier Proteins; D009687:Nuclear Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; C498268:Rdbp protein, mouse; D014157:Transcription Factors; D035602:Transcriptional Elongation Factors; C118437:negative elongation factor; D004247:DNA