| pubmed-article:19266312 | pubmed:abstractText | The ubiquitin-proteasome cycle is a complex, non-lysosomal biochemical process for intracellular protein degradation. This process involves many enzymes. One enzyme involved in this process is ubiquitin carboxyl-terminal hydrolase L5 (UCHL5), which deubiquitylates the polyubiquitin chain into ubiquitin. In this report, we isolated, sequenced, and characterized the channel catfish UCHL5 cDNA. The complete nucleic acid sequence of the channel catfish UCHL5 cDNA is comprised of 1,357 nucleotides, including an open reading frame, which appears to encode a putative peptide of 329 amino acid residues. The estimated molecular mass and pI of this peptide are 37.6 kDa and 4.84 at pH 7.0, respectively. The degree of conservation of the channel catfish UCHL5 amino acid sequence in comparison to other species ranged from 85% (vs. mouse) to 92% (vs. zebrafish and spotted green pufferfish). The channel catfish UCHL5 transcript was detected by RT-PCR in spleen, head kidney, liver, intestine, skin and gill, suggesting the UCHL5 transcript is constitutively expressed. This research provides important information for further elucidating UCHL5 in the channel catfish ubiquitin-proteasome pathway. | lld:pubmed |
