HGNC Approved Gene Symbol: ARSJ
Cytogenetic location: 4q26 Genomic coordinates (GRCh38) : 4:113,900,284-113,979,647 (from NCBI)
Sulfatases such as arylsulfatase J (ARSJ) hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. They are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules (Sardiello et al., 2005).
By searching databases for novel sulfatase genes, Sardiello et al. (2005) and Obaya (2006) identified ARSJ. They determined that all human sulfatases, including ARSJ, have 9 regions of strong evolutionary conservation, most of which contain residues involved in the sulfatase hydrolysis reaction. ARSJ shares 57% amino acid identity with ARSI (610009).
Obaya (2006) determined that the deduced 596-amino acid ARSJ protein has a predicted molecular mass of 67 kD, and they identified a splice variant that encodes a protein in which the C-terminal 10 amino acids are replaced with 7 different amino acids. Northern blot analysis detected high expression of an approximately 4.4-kb transcript in fetal kidney, with lower expression in fetal lung and 2 human cancer cell lines. No expression was detected in any normal adult tissues examined. Western blot analysis of HeLa cells expressing epitope-tagged ARSJ detected the protein in both the soluble and particulate fractions, suggesting a portion of ARSJ associates with cellular organelles or membrane structures.
Sardiello et al. (2005) and Obaya (2006) determined that the ARSJ gene contains 2 exons. Obaya (2006) found the ARSJ gene spans about 76.7 kb.
Sardiello et al. (2005) and Obaya (2006) stated that the ARSJ gene maps to chromosome 4q26. Obaya (2006) noted that the mouse Arsj gene maps to a region of chromosome 3 that shares homology of synteny with human chromosome 4q26; the rat and chimpanzee Arsj genes also map to syntenic chromosomal regions.
Obaya, A. J. Molecular cloning and initial characterization of three novel human sulfatases. Gene 372: 110-117, 2006. [PubMed: 16500042] [Full Text: https://doi.org/10.1016/j.gene.2005.12.023]
Sardiello, M., Annunziata, I., Roma, G., Ballabio, A. Sulfatases and sulfatase modifying factors: an exclusive and promiscuous relationship. Hum. Molec. Genet. 14: 3203-3217, 2005. [PubMed: 16174644] [Full Text: https://doi.org/10.1093/hmg/ddi351]