Sulfotransferase family 1C member 4 (SULT1C4)

Sulfotransferase family 1C member 4 (SULT1C4) is a cytosolic enzyme of the sulfotransferase superfamily responsible for catalyzing the sulfation of endogenous compounds (such as hormones and estrogens), xenobiotic chemicals, dietary flavonoids, and drugs, including acetaminophen and environmental pollutants like bisphenol A[1][2]. SULT1C4 shows high sulfonation capacity among the SULT1C subfamily[1], and is particularly expressed at the mRNA level in prenatal liver but shows discordant low protein expression due to transcript variant differences[1]. It plays important roles in drug metabolism, detoxification, and possibly procarcinogen activation, with implications in developmental biology, toxicity, and certain diseases such as inherited dystrophies and cancer risk[1][5]. Drugs like rifampicin can induce its expression, and ligand-activated nuclear receptors may regulate its transcription[3]. Safety concerns include the variability of protein expression, potential for metabolic activation of carcinogens, and involvement in adverse drug reactions (e.g., skin rash)[1][4].

Other names

Sulfotransferase 1C4SULT1C4SULT1C2ST1C4SULT1C#2SULT1CSulfotransferase 1C2sulfotransferase 1C4sulfotransferase 1C2sulfotransferase family, cytosolic, 1C, member 2sulfotransferase family, cytosolic, 1C, member 4sulfotransferase family, cytosolic, 1C, member C2

Sulfation (sulfonate group transfer) of drugs and xenobiotics, increasing solubility and promoting excretion, leading to drug detoxification/metabolic inactivation. It can also cause metabolic activation of procarcinogens.