LADomain in the RNA-binding Lupus La protein; unknown function
|SMART accession number:||SM00715|
|Interpro abstract (IPR006630):|
Human Ro ribonucleoproteins (RNPs) are composed of one of the four small Y RNAs and at least two proteins, Ro60 and La. The La protein is a 47 kDa polypeptide that frequently acts as an autoantigen in systemic lupus erythematosus and Sjogren's syndrome [(PUBMED:15016896)]. In the nucleus, La acts as a RNA polymerase III (RNAP III) transcription factor, while in the cytoplasm, La acts as a translation factor [(PUBMED:14636586)]. In the nucleus, La binds to the 3'UTR of nascent RNAP III transcripts to assist in folding and maturation [(PUBMED:15004549)]. In the cytoplasm, La recognises specific classes of mRNAs that contain a 5'-terminal oligopyrimidine (5'TOP) motif known to control protein synthesis [(PUBMED:14690589)]. The specific recognition is mediated by the N-terminal domain of La, which comprises a La motif and a RNA recognition motif (RRM). The La motif adopts an alpha/beta fold that comprises a winged-helix motif [(PUBMED:15048103)].
Homologous La domain-containing proteins have been identified in a wide range of organisms except Archaea, bacteria and viruses [(PUBMED:7799435)].
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Cellular role (predicted cellular role)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)