Recombinant Human UDP-glucuronosyltransferase 1-10 (UGT1A10), Truncated

Uniprot Id

Q9HAW8

Target Species

Human

Target Name

UGT1A10

Target Full Name

UDP-glucuronosyltransferase 1A10

Target Function

UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol. Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, caderastan and zolarsatan, drugs which can inhibit the effect of angiotensin II.; Lacks UGT glucuronidation activity but acts as a negative regulator of isoform 1.

Target Subcellular Location

Endoplasmic reticulum membrane; Single-pass membrane protein.

Target Protein Families

UDP-glycosyltransferase family

Target Tissue Specificity

Liver and colon. Isoform 1 and isoform 2 are expressed in colon, esophagus and small intestine; isoform 2 but not isoform 1 is expressed in liver or kidney.

Target Synonyms

UGT1A10; GNT1; UGT1; UDP-glucuronosyltransferase 1A10; UGT1A10; UDP-glucuronosyltransferase 1-10; UDPGT 1-10; UGT1*10; UGT1-10; UGT1.10; UDP-glucuronosyltransferase 1-J; UGT-1J; UGT1J

Target Background

This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene has glucuronidase activity on mycophenolic acid, coumarins, and quinolines.