| First Author | Lo PK | Year | 2002 |
| Journal | Biochim Biophys Acta | Volume | 1576 |
| Issue | 1-2 | Pages | 209-13 |
| PubMed ID | 12031504 | Mgi Jnum | J:77252 |
| Mgi Id | MGI:2181250 | Doi | 10.1016/s0167-4781(02)00305-6 |
| Citation | Lo PK, et al. (2002) Identification of transcriptional start sites and splicing of mouse thiamine transporter gene THTR-1 (Slc19a2). Biochim Biophys Acta 1576(1-2):209-13 |
| abstractText | We have previously reported the cDNA cloning of the mouse thiamine transporter THTR-1 as a p53 transcriptional target gene (renamed THTR-1a hereinafter). The mouse THTR-1a is predicted to encode a protein of 12 hydrophobic stretches and a hydrophilic loop of 87 amino acids between transmembrane helices VI and VII. The mouse THTR-1 gene has been cloned, two major transcriptional start sites located at -175 and -183 relative to the translation start codon were identified. In addition, we have cloned a spliced variant, designated THTR-1b, from mouse liver cDNA library. This isoform is characterized by an inframe deletion of 114 nucleotides from the 3'-terminal region of exon 2, predicting the expression of a truncated protein lacking the central 38 amino acids of the loop region. THTR-1b coexpressed with THTR-1a in many of the mouse tissues and in day-7 to day-17 embryos, but in lower levels than the THTR-1a. When expressed in mammalian cells, both isoforms were able to mediate the transport of thiamine. Therefore, the transport function of the mouse THTR-1 is not determined by the central 38 amino acids of its loop region. |
