UD2B7_RAT
ID UD2B7_RAT Reviewed; 530 AA.
AC Q62789;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=UDP-glucuronosyltransferase 2B7 {ECO:0000305};
DE Short=UDPGT 2B7;
DE Short=UGT2B7;
DE EC=2.4.1.17 {ECO:0000250|UniProtKB:P16662};
DE AltName: Full=UGT2B-RH4;
DE Flags: Precursor;
GN Name=Ugt2b7 {ECO:0000312|RGD:708417}; Synonyms=Ugt2b8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hepatoma;
RA Cohen H., Trus M., Benvenisty N., Reshef L.;
RT "A novel member of the UDPGT family is abundantly expressed in H4IIEC3
RT hepatoma cells.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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. Essential for the elimination and detoxification of drugs,
CC xenobiotics and endogenous compounds. Catalyzes the glucuronidation of
CC endogenous steroid hormones such as androgens (epitestosterone,
CC androsterone) and estrogens (estradiol, epiestradiol, estriol,catechol
CC estrogens). Also regulates the levels of retinoic acid, a major
CC metabolite of vitamin A involved in apoptosis, cellular growth and
CC differentiation, and embryonic development. Contributes to bile acid
CC (BA) detoxification by catalyzing the glucuronidation of BA substrates,
CC which are natural detergents for dietary lipids absorption. 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. Also metabolizes mycophenolate, an immunosuppressive
CC agent. {ECO:0000250|UniProtKB:P16662}.
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52465;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53005;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53041;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53061;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52453;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52473;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52881;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52921;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52917;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52569;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52965;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52969;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55769;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55777;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63701;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63721;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63725;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63729;
CC Evidence={ECO:0000250|UniProtKB:P16662};
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:0000250|UniProtKB:P16662};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63733;
CC Evidence={ECO:0000250|UniProtKB:P16662};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P16662}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U27518; AAA86833.1; -; mRNA.
DR RefSeq; NP_775445.1; NM_173323.1.
DR AlphaFoldDB; Q62789; -.
DR SMR; Q62789; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q62789; 1 site.
DR PhosphoSitePlus; Q62789; -.
DR PRIDE; Q62789; -.
DR GeneID; 286989; -.
DR KEGG; rno:286989; -.
DR UCSC; RGD:708417; rat.
DR CTD; 7364; -.
DR RGD; 708417; Ugt2b7.
DR InParanoid; Q62789; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q62789; -.
DR BRENDA; 2.4.1.17; 5301.
DR Reactome; R-RNO-156588; Glucuronidation.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:Q62789; -.
DR Proteomes; UP000002494; Unplaced.
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:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008209; P:androgen metabolic process; ISS:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; ISS:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Lipid metabolism;
KW Membrane; Reference proteome; Signal; Steroid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..530
FT /note="UDP-glucuronosyltransferase 2B7"
FT /id="PRO_0000036032"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 374..380
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="UDP-alpha-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:58052"
FT /evidence="ECO:0000250"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 60089 MW; 532519950C6CAEDE CRC64;
MPQKWISALL LLQISFCFRS GNCGKVLVWP LEYSHWMNLK IILDELVQRG HEVTVLRPSS
SVSLDPKKAS GLVYETSPTT SNNDEVEKSF YPVGDMWTYD VPKYTCLRYY PSLNKMFGQF
SDLWLQLCRE VVSNKELIAK LKESQFDVVL SDAVGPCGEL IAEILQLPFV YSLRFATAPG
IEKYSAGQPF PPSYVPIILS GFSGQMTFME RVENMLCLLY FDSWFESFPA KDWDPFFSEI
LGRPTTMVDT MKKAEIWLIR SYWDLEFPRP SLPNIEFVGG LHCQPAKPLP KEMEDFAQSS
GEHGVWVFSL GSMIRNITQE RANTIASALA QIPQKVFWRF EGKKPDTLGP NTRVFKWIPQ
NDLLGHPKTK AFVTHGGANG IYESIHYGIP PMVGIPLFAE QRDNVAHMVA KGAAVSIDFH
TMSSSDLLNA LKAVINNPSY KKKVMWLSAI HHDQPLKPLD RAVFWIEFVM RHKGAKHLRP
LAHNLALVSV HSLDVIGFLL ACVLAIVLLA VKCCLFLYRF FVKVAKNKRD
