| First Author | Deussing J | Year | 2000 |
| Journal | Biochim Biophys Acta | Volume | 1491 |
| Issue | 1-3 | Pages | 93-106 |
| PubMed ID | 10760573 | Mgi Jnum | J:65737 |
| Mgi Id | MGI:1927236 | Doi | 10.1016/s0167-4781(00)00021-x |
| Citation | Deussing J, et al. (2000) Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization. Biochim Biophys Acta 1491(1-3):93-106 |
| abstractText | A novel murine cysteine protease from the family of papain-like cysteine proteinases was identified by dbEST-database search. A 1. 4-kb full-length cDNA encoding a predicted polypeptide of 306 amino acids was characterized. The new protease, tentatively named cathepsin Z, exhibits all features characteristics of a papain-like cysteine protease, including the highly conserved residues of the 'catalytic triad'. Cathepsin Z shares only 26-35% overall homology with previously described mammalian papain-like cysteine peptidases and has an unusually short propeptide, which may indicate that it is a member of a putative new subfamily within the family of papain-like cysteine peptidases. Genomic clones covering the murine and human cathepsin Z genes were isolated. They comprise six exons and five introns spanning a 12-kb region of genomic DNA, respectively. Murine cathepsin Z was mapped to chromosome 2, a region with synteny homology to a region of human chromosome 20 to which human cathepsin Z has been mapped previously. Northern blot analysis revealed ubiquitous expression of murine cathepsin Z. Multiple transcriptional start sites were identified for the murine cathepsin Z gene and together with the absence of a TATA box, a high G+C content, a CpG island and the presence of several Sp1-binding sites in the promoter region, murine cathepsin Z may be classified as a 'housekeeping' gene. |
