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SULFOTRANSFERASE FAMILY 1C, MEMBER 3; SULT1C3

SULFOTRANSFERASE FAMILY 1C, MEMBER 3; SULT1C3

HGNC Approved Gene Symbol: SULT1C3Cytogenetic location: 2q12.3 Genomic coordinates (GRCh38): 2:108,239,967-108,265,607 (from NCBI)▼ DescriptionSulfate conjug...

HGNC Approved Gene Symbol: SULT1C3

Cytogenetic location: 2q12.3 Genomic coordinates (GRCh38): 2:108,239,967-108,265,607 (from NCBI)

▼ Description
Sulfate conjugation is an important pathway in the biotransformation of many endogenous and exogenous compounds, including neurotransmitters, hormones, drugs, and xenobiotics. SULT1C3 belongs to a family of cytosolic sulfotransferases that usually function as homodimers (Freimuth et al., 2004).

▼ Cloning and Expression
Using a genomewide search for novel human sulfotransferase genes, Freimuth et al. (2004) identified SULT1C3. The first coding exon of SULT1C3 contains 3 in-frame ATG codons capable of producing proteins of 304, 294, or 284 amino acids. Exons 7a, 7b, 8a, and 8b may also be alternatively spliced.

By database analysis, Meinl et al. (2008) found evidence that human SULT1C3 was expressed in heart, skeletal muscle, ovary, and some areas of brain.

By RT-PCR of 20 human tissues, followed by sequence analysis, Duniec-Dmuchowski et al. (2014) detected SULT1C3 transcripts containing exons 7a and 8a in colon and small intestine. The same transcript was also expressed in LS180 human colorectal adenocarcinoma cells. An apparently different splice variant was detected in skeletal muscle and placenta. Using 5-prime RACE, the authors showed that LS180 cells expressed SULT1C3 from the first of 3 possible transcription start sites. In vitro transcription-translation revealed that SULT1C3 translation primarily began at the first of 3 in-frame ATG codons.

▼ Gene Function
Meinl et al. (2008) found that recombinant human SULT1C3 functioned as a sulfotransferase for activation of bulky benzylic alcohols into promutagenic forms. It did not recognize standard 4-nitrophenol or 1-naphthol substrates that are usually preferred by SULT enzymes. SULT1C3 also sulfated ethanol and other small alcohols, but it required a much higher substrate concentration than that needed with larger molecules. Meinl et al. (2008) noted that activation of promutagens is a tolerated side activity rather than a physiologic function of enzymes, suggesting that the physiologic substrates for SULT1C3 may be relatively large endogenous or xenobiotic molecules. Duniec-Dmuchowski et al. (2014) noted that the SULT1C3 isoform used in the functional studies of Meinl et al. (2008) was translated from a transcript containing exons 7b and 8b.

▼ Biochemical Features
Using computer-based structural analysis, Duniec-Dmuchowski et al. (2014) found that SULT1C3 transcripts containing exons 7a and 8a and those containing exons 7b and 8b were translated into proteins with essentially identical overall structures. However, the 2 proteins had significant differences in the inner wall of the substrate-binding pocket and were likely to have different substrate specificity.

▼ Gene Structure
Freimuth et al. (2004) determined that the SULT1C3 gene contains 10 exons and spans approximately 18 kb. The first exon is noncoding, and exon 2 contains 3 putative ATG translational start codons. The last 4 exons, exons 7a, 8a, 7b, and 8b, result from duplication.

Duniec-Dmuchowski et al. (2014) identified a TATA box in the 5-prime upstream region of the SULT1C3 gene.

▼ Mapping
By genomic sequence analysis, Freimuth et al. (2004) mapped the SULT1C3 gene to chromosome 2q12.2, where it lies in a cluster with the SULT1C1 (SULT1C2; 602385) and SULT1C2 (SULT1C4; 608357) genes and the SULT1C1P pseudogene. The order of the genes in the cluster is cen--SULT1C3--SULT1C1--SULT1C1P--SULT1C2--ter, and they are separated by approximately 23, 5, and 45 kb, respectively.

Tags: 2q12.3