The reference OMIM entry for this protein is 604182

Ribosomal protein l38; rpl38

For background information on ribosomal proteins, see 180466.

CLONING

By subtractive cloning using undifferentiated HT-29 colon cancer cells and the M6 subpopulation of mucus-secreting cells, Espinosa et al. (1997) isolated a 372-bp full-length M6 cDNA encoding RPL38. Northern blot analysis showed that RPL38 was expressed at high levels in all intestinal and pancreatic carcinoma cell lines examined. The small size of the RPL38 mRNA was compatible with the length of the isolated cDNA. The 5-prime UTR of the RPL38 cDNA contains a stretch of thymidines similar to the polypyrimidine tract known to be involved in translational regulation of ribosomal protein mRNAs. The deduced 70-amino acid RPL38 protein is basic, with a calculated pI of 10.56. The human RPL38 protein is identical to rat Rpl38. Noben-Trauth and Latoche (2011) found that the mouse Rpl38 protein had an apparent molecular mass of about 8 kD and was predominantly expressed in erythrocytes.

MAPPING

By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi et al. (1998) mapped the human RPL38 gene to chromosome 17q. Espinosa et al. (1997) identified a processed RPL38 pseudogene in the promoter region of the type 1 angiotensin II receptor gene (AGTR1; 106165) on chromosome 3. Noben-Trauth and Latoche (2011) stated that the mouse Rpl38 gene maps to distal chromosome 11.

GENE FUNCTION

Xue et al. (2015) uncovered unique RNA regulons embedded in homeobox (HOX) 5-prime UTRs that confer ribosome-mediated control of gene expression. These structured RNA elements, resembling viral internal ribosome entry sites (IRESs), are found in subsets of HOX mRNAs. They facilitate ribosome recruitment and require the ribosomal protein RPL38 for their activity. Despite numerous layers of HOX gene regulation, these IRES elements are essential for converting HOX transcripts into proteins to pattern the mammalian body plan. This specialized mode of IRES-dependent translation is enabled by an additional regulatory element that the authors called the translation inhibitory element (TIE), which blocks cap-dependent translation of transcripts. Xue et al. (2015) concluded that these data uncovered a new paradigm for ribosome-mediated control of gene expression and organismal development. Xue et al. (2015) found that the Hoxa9 (142956) IRES is required for axial skeleton patterning but not for Hoxa9 mRNA expression in mouse, and that the Hoxa9 IRES is critical for Hoxa9 translation in vivo.

ANIMAL MODEL

Noben-Trauth and Latoche (2011) reviewed the phenotype of tail-short (Ts) mice, which are characterized by a shortened, kinked tail and reduced body weight. The severity of the Ts allele varies on different genetic backgrounds, but even on the most permissive strains, 30% of heterozygotes (Ts/+) suffer perinatal lethality. Ts/+ mice undergo a transient embryonic anemia accompanied by protracted growth and skeletal abnormalities. Ts homozygosity is embryonic lethal, with death in early gestation. Noben-Trauth and Latoche (2011) identified the Ts mutation as a deletion of about 18 kb of genomic DNA, including the complete Rpl38 gene, with the missing segment replaced by a 657-bp insertion showing high sequence similarity to the gag/pro-pol-dUTPase genes of the endogenous retrovirus MuERV-L. Noben-Trauth and Latoche (2011) also found that Ts/+ mice suffered a conductive hearing impairment due to overossification at the round window ridge of the middle ear, ec ... More on the omim web site

Subscribe to this protein entry history

Dec. 9, 2018: Protein entry updated
Automatic update: model status changed

Nov. 16, 2018: Protein entry updated
Automatic update: OMIM entry 604182 was added.

Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).