UD2B7_HUMAN
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 03-AUG-2022, entry version 199.
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 = 4-
CC hydroxy-4-O-(beta-D-glucuronide)-all-trans-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 17-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229};
CC Vmax=14 pmol/min/mg enzyme for the formation of 2-hydroxy-17beta-
CC estradiol 2-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229};
CC Vmax=372 pmol/min/mg enzyme for the formation of 2-hydroxy-17beta-
CC estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229};
CC Vmax=48 pmol/min/mg enzyme for the formation of 4-hydroxy-17beta-
CC estradiol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229};
CC Vmax=523 pmol/min/mg enzyme for the formation of 4-hydroxy-17beta-
CC estradiol 4-O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229};
CC Vmax=872 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone 4-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:15472229};
CC Vmax=190 pmol/min/mg enzyme for the formation of 16alpha-
CC 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 17-
CC 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 17-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=1198 pmol/min/mg enzyme for the formation of 16alpha,17beta-
CC estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=2717 pmol/min/mg enzyme for the formation of 16beta,17beta-
CC estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=35.2 pmol/min/mg enzyme for the formation of 16alpha,17alpha-
CC estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=1537 pmol/min/mg enzyme for the formation of 16alpha,17alpha-
CC estriol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=337 pmol/min/mg enzyme for the formation of epitestosterone 17-
CC 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 4-hydroxy-4-O-
CC (beta-D-glucuronide)-all-trans-retinoate
CC {ECO:0000269|PubMed:10702251};
CC Vmax=220 pmol/min/mg enzyme for the formation of mycophenolic acid O-
CC acyl-glucuronide {ECO:0000269|PubMed:15472229};
CC Vmax=16.1 pmol/min/mg enzyme for the formation of losartan-N2-beta-D-
CC glucuronide {ECO:0000269|PubMed:18674515};
CC Vmax=1.4 pmol/min/mg enzyme for the formation of calcitriol 25-O-
CC (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}.
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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; 2.
DR IntAct; P16662; 1.
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; DB00564; Carbamazepine.
DR DrugBank; DB01136; Carvedilol.
DR DrugBank; DB06119; Cenobamate.
DR DrugBank; DB06777; Chenodeoxycholic acid.
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; 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; 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; DB00870; Suprofen.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB06204; Tapentadol.
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 GlyGen; P16662; 3 sites.
DR iPTMnet; P16662; -.
DR PhosphoSitePlus; P16662; -.
DR BioMuta; UGT2B7; -.
DR DMDM; 136727; -.
DR jPOST; P16662; -.
DR MassIVE; P16662; -.
DR PaxDb; P16662; -.
DR PeptideAtlas; P16662; -.
DR PRIDE; P16662; -.
DR ProteomicsDB; 53391; -.
DR Antibodypedia; 44203; 182 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 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; HNIVHMK; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; P16662; -.
DR TreeFam; TF315472; -.
DR BioCyc; MetaCyc:HS10272-MON; -.
DR BRENDA; 2.4.1.17; 2681.
DR PathwayCommons; P16662; -.
DR Reactome; R-HSA-156588; Glucuronidation.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; P16662; -.
DR SignaLink; P16662; -.
DR SIGNOR; P16662; -.
DR BioGRID-ORCS; 7364; 9 hits in 995 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 tissues.
DR ExpressionAtlas; P16662; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 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
