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   28-JUN-2023, entry version 131.
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 = 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: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   GlyCosmos; Q62789; 1 site, No reported glycans.
DR   GlyGen; Q62789; 1 site.
DR   PhosphoSitePlus; Q62789; -.
DR   GeneID; 286989; -.
DR   KEGG; rno:286989; -.
DR   UCSC; RGD:708417; rat.
DR   AGR; RGD:708417; -.
DR   CTD; 7364; -.
DR   RGD; 708417; Ugt2b7.
DR   InParanoid; Q62789; -.
DR   OrthoDB; 382054at2759; -.
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   Reactome; R-RNO-9757110; Prednisone ADME.
DR   PRO; PR:Q62789; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   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:SF64; UDP-GLUCURONOSYLTRANSFERASE; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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
//