ID UD2B7_HUMAN Reviewed; 529 AA. AC P16662; B2R810; Q6GTW0; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 25-APR-2018, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=UDP-glucuronosyltransferase 2B7 {ECO:0000303|PubMed:18719240}; DE Short=UDPGT 2B7; DE Short=UGT2B7; DE EC=2.4.1.17 {ECO:0000269|PubMed:17442341, ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:19022937, ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:23756265, ECO:0000269|PubMed:26220143}; DE AltName: Full=3,4-catechol estrogen-specific UDPGT; DE AltName: Full=UDP-glucuronosyltransferase 2B9; DE Short=UDPGT 2B9; DE AltName: Full=UDPGTh-2; DE Flags: Precursor; GN Name=UGT2B7 {ECO:0000312|HGNC:HGNC:12554}; Synonyms=UGTB2B9; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HIS-268. RC TISSUE=Liver; RX PubMed=2159463; DOI=10.1016/s0021-9258(19)39016-7; RA Ritter J.K., Sheen Y.Y., Owens I.S.; RT "Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 RT cells. 3,4-catechol estrogens and estriol as primary substrates."; RL J. Biol. Chem. 265:7900-7906(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBCELLULAR LOCATION. RX PubMed=10702251; DOI=10.1074/jbc.275.10.6908; RA Samokyszyn V.M., Gall W.E., Zawada G., Freyaldenhoven M.A., Chen G., RA Mackenzie P.I., Tephly T.R., Radominska-Pandya A.; RT "4-hydroxyretinoic acid, a novel substrate for human liver microsomal UDP- RT glucuronosyltransferase(s) and recombinant UGT2B7."; RL J. Biol. Chem. 275:6908-6914(2000). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15472229; DOI=10.1210/jc.2004-0331; RA Lepine J., Bernard O., Plante M., Tetu B., Pelletier G., Labrie F., RA Belanger A., Guillemette C.; RT "Specificity and regioselectivity of the conjugation of estradiol, estrone, RT and their catecholestrogen and methoxyestrogen metabolites by human uridine RT diphospho-glucuronosyltransferases expressed in endometrium."; RL J. Clin. Endocrinol. Metab. 89:5222-5232(2004). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15470161; DOI=10.1124/dmd.104.001651; RA Picard N., Ratanasavanh D., Premaud A., Le Meur Y., Marquet P.; RT "Identification of the UDP-glucuronosyltransferase isoforms involved in RT mycophenolic acid phase II metabolism."; RL Drug Metab. Dispos. 33:139-146(2005). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18674515; DOI=10.1016/j.bcp.2008.07.006; RA Alonen A., Finel M., Kostiainen R.; RT "The human UDP-glucuronosyltransferase UGT1A3 is highly selective towards RT N2 in the tetrazole ring of losartan, candesartan, and zolarsartan."; RL Biochem. Pharmacol. 76:763-772(2008). RN [12] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18177842; DOI=10.1016/j.bcp.2007.11.008; RA Hashizume T., Xu Y., Mohutsky M.A., Alberts J., Hadden C., Kalhorn T.F., RA Isoherranen N., Shuhart M.C., Thummel K.E.; RT "Identification of human UDP-glucuronosyltransferases catalyzing hepatic RT 1alpha,25-dihydroxyvitamin D3 conjugation."; RL Biochem. Pharmacol. 75:1240-1250(2008). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18719240; DOI=10.1124/dmd.108.022731; RA Itaeaho K., Mackenzie P.I., Ikushiro S., Miners J.O., Finel M.; RT "The configuration of the 17-hydroxy group variably influences the RT glucuronidation of beta-estradiol and epiestradiol by human UDP- RT glucuronosyltransferases."; RL Drug Metab. Dispos. 36:2307-2315(2008). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19022937; DOI=10.1124/dmd.108.024844; RA Sten T., Bichlmaier I., Kuuranne T., Leinonen A., Yli-Kauhaluoma J., RA Finel M.; RT "UDP-glucuronosyltransferases (UGTs) 2B7 and UGT2B17 display converse RT specificity in testosterone and epitestosterone glucuronidation, whereas RT UGT2A1 conjugates both androgens similarly."; RL Drug Metab. Dispos. 37:417-423(2009). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE RP SPECIFICITY. RX PubMed=23288867; DOI=10.1124/dmd.112.049072; RA Sneitz N., Vahermo M., Mosorin J., Laakkonen L., Poirier D., Finel M.; RT "Regiospecificity and stereospecificity of human UDP- RT glucuronosyltransferases in the glucuronidation of estriol, 16-epiestriol, RT 17-epiestriol, and 13-epiestradiol."; RL Drug Metab. Dispos. 41:582-591(2013). RN [16] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23756265; DOI=10.1124/dmd.113.052613; RA Perreault M., Gauthier-Landry L., Trottier J., Verreault M., Caron P., RA Finel M., Barbier O.; RT "The Human UDP-glucuronosyltransferase UGT2A1 and UGT2A2 enzymes are highly RT active in bile acid glucuronidation."; RL Drug Metab. Dispos. 41:1616-1620(2013). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=26220143; DOI=10.1016/j.jsbmb.2015.07.013; RA Kallionpaeae R.A., Jaervinen E., Finel M.; RT "Glucuronidation of estrone and 16alpha-hydroxyestrone by human UGT RT enzymes: The key roles of UGT1A10 and UGT2B7."; RL J. Steroid Biochem. Mol. Biol. 154:104-111(2015). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 285-451, CATALYTIC ACTIVITY, RP FUNCTION TOWARDS STEROIDS, AND MUTAGENESIS OF SER-15; HIS-35; ASP-151; RP THR-373; HIS-374; ASN-378; GLY-379; ASP-398 AND GLN-399. RX PubMed=17442341; DOI=10.1016/j.jmb.2007.03.066; RA Miley M.J., Zielinska A.K., Keenan J.E., Bratton S.M., RA Radominska-Pandya A., Redinbo M.R.; RT "Crystal structure of the cofactor-binding domain of the human phase II RT drug-metabolism enzyme UDP-glucuronosyltransferase 2B7."; RL J. Mol. Biol. 369:498-511(2007). RN [19] RP VARIANT HIS-268. RX PubMed=11186130; DOI=10.1097/00008571-200011000-00002; RA Bhasker C.R., McKinnon W., Stone A., Lo A.C., Kubota T., Ishizaki T., RA Miners J.O.; RT "Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino RT acid 268: ethnic diversity of alleles and potential clinical RT significance."; RL Pharmacogenetics 10:679-685(2000). CC -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II CC biotransformation reactions in which lipophilic substrates are CC conjugated with glucuronic acid to increase the metabolite's water CC solubility, thereby facilitating excretion into either the urine or CC bile (PubMed:10702251, PubMed:15472229, PubMed:15470161, CC PubMed:18674515, PubMed:18719240, PubMed:19022937, PubMed:23288867, CC PubMed:23756265, PubMed:26220143, PubMed:17442341). Essential for the CC elimination and detoxification of drugs, xenobiotics and endogenous CC compounds (PubMed:15470161, PubMed:18674515, PubMed:23756265). CC Catalyzes the glucuronidation of endogenous steroid hormones such as CC androgens (epitestosterone, androsterone) and estrogens (estradiol, CC epiestradiol, estriol, catechol estrogens) (PubMed:2159463, CC PubMed:15472229, PubMed:18719240, PubMed:19022937, PubMed:23288867, CC PubMed:26220143, PubMed:17442341). Also regulates the levels of CC retinoic acid, a major metabolite of vitamin A involved in apoptosis, CC cellular growth and differentiation, and embryonic development CC (PubMed:10702251). Contributes to bile acid (BA) detoxification by CC catalyzing the glucuronidation of BA substrates, which are natural CC detergents for dietary lipids absorption (PubMed:23756265). Involved in CC the glucuronidation of the AGTR1 angiotensin receptor antagonist CC losartan, caderastan and zolarsatan, drugs which can inhibit the effect CC of angiotensin II (PubMed:18674515). Also metabolizes mycophenolate, an CC immunosuppressive agent (PubMed:15470161). CC {ECO:0000269|PubMed:10702251, ECO:0000269|PubMed:15470161, CC ECO:0000269|PubMed:15472229, ECO:0000269|PubMed:17442341, CC ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240, CC ECO:0000269|PubMed:19022937, ECO:0000269|PubMed:2159463, CC ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:23756265, CC ECO:0000269|PubMed:26220143}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17; CC Evidence={ECO:0000269|PubMed:10702251, ECO:0000269|PubMed:15470161, CC ECO:0000269|PubMed:15472229, ECO:0000269|PubMed:17442341, CC ECO:0000269|PubMed:18674515, ECO:0000269|PubMed:18719240, CC ECO:0000269|PubMed:19022937, ECO:0000269|PubMed:23288867, CC ECO:0000269|PubMed:23756265, ECO:0000269|PubMed:26220143}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033; CC Evidence={ECO:0000305|PubMed:10702251, ECO:0000305|PubMed:15470161, CC ECO:0000305|PubMed:15472229, ECO:0000305|PubMed:17442341, CC ECO:0000305|PubMed:18674515, ECO:0000305|PubMed:18719240, CC ECO:0000305|PubMed:19022937, ECO:0000305|PubMed:23288867, CC ECO:0000305|PubMed:23756265, ECO:0000305|PubMed:26220143}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha- CC estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136642; CC Evidence={ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873; CC Evidence={ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol CC 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52464, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:82961; CC Evidence={ECO:0000269|PubMed:18719240}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52465; CC Evidence={ECO:0000305|PubMed:18719240}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2- CC hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:53004, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136931; CC Evidence={ECO:0000269|PubMed:15472229}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53005; CC Evidence={ECO:0000305|PubMed:15472229}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 17beta- CC estradiol 4-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:53040, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:62845, ChEBI:CHEBI:136937; CC Evidence={ECO:0000269|PubMed:15472229}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53041; CC Evidence={ECO:0000305|PubMed:15472229}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxyestrone + UDP-alpha-D-glucuronate = estrone 4-O- CC (beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53060, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:87602, ChEBI:CHEBI:136970; CC Evidence={ECO:0000269|PubMed:15472229}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53061; CC Evidence={ECO:0000305|PubMed:15472229}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha-hydroxyestrone + UDP-alpha-D-glucuronate = 16alpha- CC hydroxyestrone 16-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52452, ChEBI:CHEBI:776, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136636; CC Evidence={ECO:0000269|PubMed:26220143}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52453; CC Evidence={ECO:0000305|PubMed:26220143}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17beta-estriol + UDP-alpha-D-glucuronate = CC 16alpha,17beta-estriol 16-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52472, ChEBI:CHEBI:15378, ChEBI:CHEBI:27974, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136650; CC Evidence={ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52473; CC Evidence={ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16beta,17beta-estriol + UDP-alpha-D-glucuronate = CC 16beta,17beta-estriol 16-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52880, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:87620, ChEBI:CHEBI:136886; CC Evidence={ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52881; CC Evidence={ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate = CC 16alpha,17alpha-estriol 16-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52920, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136884; CC Evidence={ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52921; CC Evidence={ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate = CC 16alpha,17alpha-estriol 17-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52916, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136883; CC Evidence={ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52917; CC Evidence={ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=epitestosterone + UDP-alpha-D-glucuronate = epitestosterone CC 17-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52568, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:42534, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:136673; CC Evidence={ECO:0000269|PubMed:19022937}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52569; CC Evidence={ECO:0000305|PubMed:19022937}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hyodeoxycholate + UDP-alpha-D-glucuronate = H(+) + CC hyodeoxycholate 6-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52964, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:58875, ChEBI:CHEBI:136905; CC Evidence={ECO:0000269|PubMed:23756265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52965; CC Evidence={ECO:0000305|PubMed:23756265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=hyocholate + UDP-alpha-D-glucuronate = H(+) + hyocholate 6-O- CC (beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:52968, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:133661, CC ChEBI:CHEBI:136906; Evidence={ECO:0000269|PubMed:23756265}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52969; CC Evidence={ECO:0000305|PubMed:23756265}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-retinoate + UDP-alpha-D-glucuronate = all-trans- CC retinoyl-1-O-(beta-D-glucuronate) + UDP; Xref=Rhea:RHEA:55768, CC ChEBI:CHEBI:35291, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:139181; Evidence={ECO:0000269|PubMed:10702251}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55769; CC Evidence={ECO:0000305|PubMed:10702251}; CC -!- CATALYTIC ACTIVITY: CC Reaction=all-trans-4-hydroxyretinoate + UDP-alpha-D-glucuronate = all- CC trans-4-hydroxy-4-O-(beta-D-glucuronide)-retinoate + H(+) + UDP; CC Xref=Rhea:RHEA:55776, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:134178, ChEBI:CHEBI:139182; CC Evidence={ECO:0000269|PubMed:10702251}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55777; CC Evidence={ECO:0000305|PubMed:10702251}; CC -!- CATALYTIC ACTIVITY: CC Reaction=mycophenolate + UDP-alpha-D-glucuronate = mycophenolic acid O- CC acyl-beta-D-glucuronide + UDP; Xref=Rhea:RHEA:63700, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:62932, CC ChEBI:CHEBI:66982; Evidence={ECO:0000269|PubMed:15470161}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63701; CC Evidence={ECO:0000305|PubMed:15470161}; CC -!- CATALYTIC ACTIVITY: CC Reaction=losartan + UDP-alpha-D-glucuronate = losartan-2-N-beta-D- CC glucuronide + UDP; Xref=Rhea:RHEA:63720, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149504, ChEBI:CHEBI:149507; CC Evidence={ECO:0000269|PubMed:18674515}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63721; CC Evidence={ECO:0000305|PubMed:18674515}; CC -!- CATALYTIC ACTIVITY: CC Reaction=candesartan + UDP-alpha-D-glucuronate = candesartan O-beta-D- CC glucuronoside + UDP; Xref=Rhea:RHEA:63724, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149509, ChEBI:CHEBI:149522; CC Evidence={ECO:0000269|PubMed:18674515}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725; CC Evidence={ECO:0000305|PubMed:18674515}; CC -!- CATALYTIC ACTIVITY: CC Reaction=candesartan + UDP-alpha-D-glucuronate = candesartan-2-N-beta- CC D-glucuronide + UDP; Xref=Rhea:RHEA:63728, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149509, ChEBI:CHEBI:149523; CC Evidence={ECO:0000269|PubMed:18674515}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63729; CC Evidence={ECO:0000305|PubMed:18674515}; CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-alpha-D-glucuronate + zolasartan = UDP + zolarsartan O- CC beta-D-glucuronoside; Xref=Rhea:RHEA:63732, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:149524, ChEBI:CHEBI:149526; CC Evidence={ECO:0000269|PubMed:18674515}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63733; CC Evidence={ECO:0000305|PubMed:18674515}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=10 uM for 17beta-estradiol/estradiol (when assaying CC glucuronidation at position 17) {ECO:0000269|PubMed:15472229}; CC KM=33 uM for the formation of 2-hydroxy-17beta-estradiol (when CC assaying glucuronidation at position 2) CC {ECO:0000269|PubMed:15472229}; CC KM=33 uM for 2-hydroxy-17beta-estradiol (when assaying CC glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; CC KM=22 uM for 4-hydroxy-17beta-estradiol (when assaying CC glucuronidation at position 3) {ECO:0000269|PubMed:15472229}; CC KM=10 uM for 4-hydroxy-17beta-estradiol (when assaying CC glucuronidation at position 4) {ECO:0000269|PubMed:15472229}; CC KM=62 uM for 4-hydroxy-estrone (when assaying glucuronidation at CC position 4) {ECO:0000269|PubMed:15472229}; CC KM=3.4 uM for 16alpha-hydroxyestrone (when assaying glucuronidation CC at position 16) {ECO:0000269|PubMed:26220143}; CC KM=5.96 uM for 17beta-estradiol/estradiol (when assaying CC glucuronidation at position 17) {ECO:0000269|PubMed:18719240}; CC KM=1.7 uM for epitestosterone (when assaying glucuronidation at CC position 17) {ECO:0000269|PubMed:19022937}; CC KM=1.3 uM for all-trans-retinoate {ECO:0000269|PubMed:10702251}; CC KM=221 uM for all-trans-4-hydroxyretinoate CC {ECO:0000269|PubMed:10702251}; CC KM=200 uM for mycophenolate (when assaying glucuronidation at CC position 6') {ECO:0000269|PubMed:15470161}; CC KM=162.3 uM for losartan {ECO:0000269|PubMed:18674515}; CC KM=4.2 uM for calcitriol (when assaying glucuronidation at position CC 25) {ECO:0000269|PubMed:18177842}; CC Vmax=42 pmol/min/mg enzyme for the formation of 17beta-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; CC Vmax=14 pmol/min/mg enzyme for the formation of CC 2-hydroxy-17beta-estradiol 2-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:15472229}; CC Vmax=372 pmol/min/mg enzyme for the formation of CC 2-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:15472229}; CC Vmax=48 pmol/min/mg enzyme for the formation of CC 4-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:15472229}; CC Vmax=523 pmol/min/mg enzyme for the formation of CC 4-hydroxy-17beta-estradiol 4-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:15472229}; CC Vmax=872 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone CC 4-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229}; CC Vmax=190 pmol/min/mg enzyme for the formation of CC 16alpha-hydroxyestrone 16-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:26220143}; CC Vmax=590 pmol/min/mg enzyme for the formation of 17alpha-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; CC Vmax=631 pmol/min/mg enzyme for the formation of 17beta-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; CC Vmax=32.6 pmol/min/mg enzyme for the formation of 17alpha-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; CC Vmax=4.5 pmol/min/mg enzyme for the formation of 17beta-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; CC Vmax=1198 pmol/min/mg enzyme for the formation of CC 16alpha,17beta-estriol 16-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=2717 pmol/min/mg enzyme for the formation of CC 16beta,17beta-estriol 16-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=35.2 pmol/min/mg enzyme for the formation of CC 16alpha,17alpha-estriol 16-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=1537 pmol/min/mg enzyme for the formation of CC 16alpha,17alpha-estriol 17-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=337 pmol/min/mg enzyme for the formation of epitestosterone CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:19022937}; CC Vmax=523 pmol/min/mg enzyme for the formation of all-trans-retinoate CC 1-O-(beta-D-glucuronate) {ECO:0000269|PubMed:10702251}; CC Vmax=1709 pmol/min/mg enzyme for the formation of CC 4-hydroxy-4-O-(beta-D-glucuronide)-all-trans-retinoate CC {ECO:0000269|PubMed:10702251}; CC Vmax=220 pmol/min/mg enzyme for the formation of mycophenolic acid CC O-acyl-glucuronide {ECO:0000269|PubMed:15472229}; CC Vmax=16.1 pmol/min/mg enzyme for the formation of CC losartan-N2-beta-D-glucuronide {ECO:0000269|PubMed:18674515}; CC Vmax=1.4 pmol/min/mg enzyme for the formation of calcitriol CC 25-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18177842}; CC Note=Some kinetic parameters were assessed using commercial enzymes, CC which may represent a mix of both active and inactive protein forms, CC and therefore modify the kinetic values. CC {ECO:0000305|PubMed:15470161, ECO:0000305|PubMed:18177842}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:10702251}; Single-pass membrane protein CC {ECO:0000255}. CC -!- POLYMORPHISM: 2 alleles have been identified: UGT2B7*1 (His-268) and CC UGT2B7*2 (Tyr-268). The sequence shown is that of allele UGT2B7*2. CC {ECO:0000269|PubMed:11186130, ECO:0000269|PubMed:2159463}. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05428; AAA36793.1; -; mRNA. DR EMBL; AK313190; BAG36007.1; -; mRNA. DR EMBL; AK223142; BAD96862.1; -; mRNA. DR EMBL; AC111000; AAY41045.1; -; Genomic_DNA. DR EMBL; BC030974; AAH30974.1; -; mRNA. DR CCDS; CCDS3526.1; -. DR PIR; A35366; A35366. DR RefSeq; NP_001065.2; NM_001074.3. DR RefSeq; NP_001317648.1; NM_001330719.1. DR PDB; 2O6L; X-ray; 1.80 A; A/B=285-451. DR PDBsum; 2O6L; -. DR AlphaFoldDB; P16662; -. DR SMR; P16662; -. DR BioGRID; 113211; 3. DR IntAct; P16662; 42. DR STRING; 9606.ENSP00000304811; -. DR BindingDB; P16662; -. DR ChEMBL; CHEMBL4370; -. DR DrugBank; DB13783; Acemetacin. DR DrugBank; DB06403; Ambrisentan. DR DrugBank; DB01217; Anastrozole. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB09274; Artesunate. DR DrugBank; DB12597; Asciminib. DR DrugBank; DB11936; Bempedoic acid. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB14737; Cannabinol. DR DrugBank; DB00564; Carbamazepine. DR DrugBank; DB01136; Carvedilol. DR DrugBank; DB06119; Cenobamate. DR DrugBank; DB06777; Chenodeoxycholic acid. DR DrugBank; DB05239; Cobimetinib. DR DrugBank; DB00318; Codeine. DR DrugBank; DB14635; Curcumin sulfate. DR DrugBank; DB06695; Dabigatran etexilate. DR DrugBank; DB06292; Dapagliflozin. DR DrugBank; DB09213; Dexibuprofen. DR DrugBank; DB00514; Dextromethorphan. DR DrugBank; DB00586; Diclofenac. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB12243; Edaravone. DR DrugBank; DB09038; Empagliflozin. DR DrugBank; DB13874; Enasidenib. DR DrugBank; DB00445; Epirubicin. DR DrugBank; DB11827; Ertugliflozin. DR DrugBank; DB12235; Estetrol. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB00977; Ethinylestradiol. DR DrugBank; DB00749; Etodolac. DR DrugBank; DB00973; Ezetimibe. DR DrugBank; DB04854; Febuxostat. DR DrugBank; DB01544; Flunitrazepam. DR DrugBank; DB00712; Flurbiprofen. DR DrugBank; DB01095; Fluvastatin. DR DrugBank; DB00983; Formoterol. DR DrugBank; DB11796; Fostemsavir. DR DrugBank; DB01241; Gemfibrozil. DR DrugBank; DB00327; Hydromorphone. DR DrugBank; DB12471; Ibrexafungerp. DR DrugBank; DB01050; Ibuprofen. DR DrugBank; DB00328; Indomethacin. DR DrugBank; DB01026; Ketoconazole. DR DrugBank; DB00465; Ketorolac. DR DrugBank; DB00598; Labetalol. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB01006; Letrozole. DR DrugBank; DB00678; Losartan. DR DrugBank; DB00227; Lovastatin. DR DrugBank; DB09212; Loxoprofen. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00784; Mefenamic acid. DR DrugBank; DB08893; Mirabegron. DR DrugBank; DB01252; Mitiglinide. DR DrugBank; DB00295; Morphine. DR DrugBank; DB00688; Mycophenolate mofetil. DR DrugBank; DB01024; Mycophenolic acid. DR DrugBank; DB06230; Nalmefene. DR DrugBank; DB08804; Nandrolone decanoate. DR DrugBank; DB00788; Naproxen. DR DrugBank; DB11837; Osilodrostat. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB01174; Phenobarbital. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB08860; Pitavastatin. DR DrugBank; DB12016; Ponesimod. DR DrugBank; DB00794; Primidone. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB06207; Silodosin. DR DrugBank; DB00641; Simvastatin. DR DrugBank; DB12713; Sotagliflozin. DR DrugBank; DB00870; Suprofen. DR DrugBank; DB00675; Tamoxifen. DR DrugBank; DB06204; Tapentadol. DR DrugBank; DB12095; Telotristat ethyl. DR DrugBank; DB00871; Terbutaline. DR DrugBank; DB00197; Troglitazone. DR DrugBank; DB13609; Umifenovir. DR DrugBank; DB06235; Vadimezan. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB06737; Zaltoprofen. DR DrugBank; DB00495; Zidovudine. DR SwissLipids; SLP:000001695; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR GlyCosmos; P16662; 3 sites, No reported glycans. DR GlyGen; P16662; 3 sites. DR iPTMnet; P16662; -. DR PhosphoSitePlus; P16662; -. DR BioMuta; UGT2B7; -. DR DMDM; 136727; -. DR jPOST; P16662; -. DR MassIVE; P16662; -. DR PaxDb; 9606-ENSP00000304811; -. DR PeptideAtlas; P16662; -. DR ProteomicsDB; 53391; -. DR Antibodypedia; 44203; 191 antibodies from 27 providers. DR DNASU; 7364; -. DR Ensembl; ENST00000305231.12; ENSP00000304811.7; ENSG00000171234.14. DR GeneID; 7364; -. DR KEGG; hsa:7364; -. DR MANE-Select; ENST00000305231.12; ENSP00000304811.7; NM_001074.4; NP_001065.2. DR UCSC; uc003heg.4; human. DR AGR; HGNC:12554; -. DR CTD; 7364; -. DR DisGeNET; 7364; -. DR GeneCards; UGT2B7; -. DR HGNC; HGNC:12554; UGT2B7. DR HPA; ENSG00000171234; Group enriched (kidney, liver). DR MIM; 600068; gene. DR neXtProt; NX_P16662; -. DR OpenTargets; ENSG00000171234; -. DR PharmGKB; PA361; -. DR VEuPathDB; HostDB:ENSG00000171234; -. DR eggNOG; KOG1192; Eukaryota. DR GeneTree; ENSGT00940000158332; -. DR HOGENOM; CLU_012949_3_2_1; -. DR InParanoid; P16662; -. DR OMA; STRFHDQ; -. DR OrthoDB; 382054at2759; -. DR PhylomeDB; P16662; -. DR TreeFam; TF315472; -. DR BioCyc; MetaCyc:HS10272-MONOMER; -. DR BRENDA; 2.4.1.17; 2681. DR PathwayCommons; P16662; -. DR Reactome; R-HSA-156588; Glucuronidation. DR Reactome; R-HSA-9749641; Aspirin ADME. DR Reactome; R-HSA-9757110; Prednisone ADME. DR SABIO-RK; P16662; -. DR SignaLink; P16662; -. DR SIGNOR; P16662; -. DR BioGRID-ORCS; 7364; 9 hits in 1056 CRISPR screens. DR ChiTaRS; UGT2B7; human. DR EvolutionaryTrace; P16662; -. DR GeneWiki; UGT2B7; -. DR GenomeRNAi; 7364; -. DR Pharos; P16662; Tchem. DR PRO; PR:P16662; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P16662; Protein. DR Bgee; ENSG00000171234; Expressed in liver and 65 other cell types or tissues. DR ExpressionAtlas; P16662; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB. DR GO; GO:0008209; P:androgen metabolic process; IDA:UniProtKB. DR GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB. DR GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB. DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR CDD; cd03784; GT1_Gtf-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR002213; UDP_glucos_trans. DR InterPro; IPR035595; UDP_glycos_trans_CS. DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1. DR PANTHER; PTHR48043:SF87; UDP-GLUCURONOSYLTRANSFERASE 2B7; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00375; UDPGT; 1. PE 1: Evidence at protein level; KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; KW Lipid metabolism; Membrane; Reference proteome; Signal; Steroid metabolism; KW Transferase; Transmembrane; Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000250" FT CHAIN 24..529 FT /note="UDP-glucuronosyltransferase 2B7" FT /id="PRO_0000036031" FT TRANSMEM 493..509 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 373..379 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000305" FT BINDING 398 FT /ligand="UDP-alpha-D-glucuronate" FT /ligand_id="ChEBI:CHEBI:58052" FT /evidence="ECO:0000305" FT CARBOHYD 67 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 68 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 315 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 71 FT /note="A -> S (in dbSNP:rs12233719)" FT /id="VAR_057327" FT VARIANT 268 FT /note="Y -> H (in allele UGT2B7*1; dbSNP:rs7439366)" FT /evidence="ECO:0000269|PubMed:11186130, FT ECO:0000269|PubMed:2159463" FT /id="VAR_012342" FT VARIANT 378 FT /note="N -> S (in dbSNP:rs35590824)" FT /id="VAR_057328" FT MUTAGEN 15 FT /note="S->A: Reduced androsterone, hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 35 FT /note="H->A: Reduced androsterone, hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 151 FT /note="D->A: Reduced androsterone and tetrachlorocatechol FT glucuronosyltransferase activities; abolished FT hyodeoxycholic acid glucuronosyltransferase activity." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 151 FT /note="D->N: Abolished androsterone glucuronosyltransferase FT activity; reduced hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 373 FT /note="T->V: Reduced androsterone, hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 374 FT /note="H->A,E: Abolished androsterone FT glucuronosyltransferase activity; reduced hyodeoxycholic FT acid and tetrachlorocatechol glucuronosyltransferase FT activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 378 FT /note="N->A: Abolished androsterone glucuronosyltransferase FT activity; reduced hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 379 FT /note="G->D: Abolished androsterone glucuronosyltransferase FT activity; reduced hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 379 FT /note="G->S: Abolished androsterone glucuronosyltransferase FT activity; no change in hyodeoxycholic acid and FT tetrachlorocatechol glucuronosyltransferase activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 398 FT /note="D->A,N: Reduced androsterone, hyodeoxycholic acid FT and tetrachlorocatechol glucuronosyltransferase FT activities." FT /evidence="ECO:0000269|PubMed:17442341" FT MUTAGEN 399 FT /note="Q->A: Abolished androsterone, hyodeoxycholic acid FT and tetrachlorocatechol glucuronosyltransferase FT activities." FT /evidence="ECO:0000269|PubMed:17442341" FT HELIX 290..297 FT /evidence="ECO:0007829|PDB:2O6L" FT TURN 298..302 FT /evidence="ECO:0007829|PDB:2O6L" FT STRAND 304..308 FT /evidence="ECO:0007829|PDB:2O6L" FT HELIX 318..328 FT /evidence="ECO:0007829|PDB:2O6L" FT STRAND 331..338 FT /evidence="ECO:0007829|PDB:2O6L" FT STRAND 351..356 FT /evidence="ECO:0007829|PDB:2O6L" FT HELIX 359..363 FT /evidence="ECO:0007829|PDB:2O6L" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:2O6L" FT HELIX 377..386 FT /evidence="ECO:0007829|PDB:2O6L" FT STRAND 390..392 FT /evidence="ECO:0007829|PDB:2O6L" FT HELIX 399..407 FT /evidence="ECO:0007829|PDB:2O6L" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:2O6L" FT STRAND 411..414 FT /evidence="ECO:0007829|PDB:2O6L" FT TURN 417..419 FT /evidence="ECO:0007829|PDB:2O6L" FT HELIX 422..434 FT /evidence="ECO:0007829|PDB:2O6L" FT HELIX 436..445 FT /evidence="ECO:0007829|PDB:2O6L" FT TURN 448..450 FT /evidence="ECO:0007829|PDB:2O6L" SQ SEQUENCE 529 AA; 60721 MW; 94B8B31CE929C836 CRC64; MSVKWTSVIL LIQLSFCFSS GNCGKVLVWA AEYSHWMNIK TILDELIQRG HEVTVLASSA SILFDPNNSS ALKIEIYPTS LTKTELENFI MQQIKRWSDL PKDTFWLYFS QVQEIMSIFG DITRKFCKDV VSNKKFMKKV QESRFDVIFA DAIFPCSELL AELFNIPFVY SLSFSPGYTF EKHSGGFIFP PSYVPVVMSE LTDQMTFMER VKNMIYVLYF DFWFEIFDMK KWDQFYSEVL GRPTTLSETM GKADVWLIRN SWNFQFPYPL LPNVDFVGGL HCKPAKPLPK EMEDFVQSSG ENGVVVFSLG SMVSNMTEER ANVIASALAQ IPQKVLWRFD GNKPDTLGLN TRLYKWIPQN DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGIPLFADQP DNIAHMKARG AAVRVDFNTM SSTDLLNALK RVINDPSYKE NVMKLSRIQH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA HDLTWFQYHS LDVIGFLLVC VATVIFIVTK CCLFCFWKFA RKAKKGKND //