ID   UD2B1_RAT               Reviewed;         529 AA.
AC   P09875;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   02-SEP-2026, entry version 175.
DE   RecName: Full=UDP-glucuronosyltransferase 2B1 {ECO:0000303|PubMed:18719240};
DE            Short=UDPGT 2B1;
DE            Short=UGT2B1;
DE            EC=2.4.1.17 {ECO:0000269|PubMed:18719240};
DE   AltName: Full=UDPGTr-2;
DE   Flags: Precursor;
GN   Name=Ugt2b1 {ECO:0000312|RGD:708541}; Synonyms=Udpgtr2;
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], AND SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=3084479; DOI=10.1016/s0021-9258(17)38500-9;
RA   McKenzie P.I.;
RT   "Rat liver UDP-glucuronosyltransferase. Sequence and expression of a cDNA
RT   encoding a phenobarbital-inducible form.";
RL   J. Biol. Chem. 261:6119-6125(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2113533; DOI=10.1016/s0021-9258(19)38595-3;
RA   McKenzie P.I., Rodbourn L.;
RT   "Organization of the rat UDP-glucuronosyltransferase, UDPGTr-2, gene and
RT   characterization of its promoter.";
RL   J. Biol. Chem. 265:11328-11332(1990).
RN   [3]
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).
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:18719240). Essential for the elimination and
CC       detoxification of drugs, xenobiotics and endogenous compounds
CC       (PubMed:18719240). Catalyzes the glucuronidation of the endogenous
CC       estrogen hormone estradiol (PubMed:18719240).
CC       {ECO:0000269|PubMed:18719240}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC         beta-D-glucuronoside + UDP + H(+); 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:18719240};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC         Evidence={ECO:0000305|PubMed:18719240};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol
CC         17-O-(beta-D-glucuronate) + UDP + H(+); 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13.4 uM for 17beta-estradiol/estradiol (when assaying
CC         glucuronidation at position 17) {ECO:0000269|PubMed:18719240};
CC         Vmax=1630 pmol/min/mg enzyme for the formation of 17beta-estradiol
CC         17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC         Vmax=55 pmol/min/mg enzyme for the formation of 17beta-estradiol
CC         3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:3084479}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: By phenobarbital. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M13506; AAA42313.1; -; mRNA.
DR   EMBL; M35086; AAA42310.1; -; Genomic_DNA.
DR   EMBL; M35202; AAA42310.1; JOINED; Genomic_DNA.
DR   EMBL; M35080; AAA42310.1; JOINED; Genomic_DNA.
DR   EMBL; M35082; AAA42310.1; JOINED; Genomic_DNA.
DR   EMBL; M35083; AAA42310.1; JOINED; Genomic_DNA.
DR   PIR; A42233; A42233.
DR   RefSeq; NP_775417.1; NM_173295.2.
DR   AlphaFoldDB; P09875; -.
DR   SMR; P09875; -.
DR   FunCoup; P09875; 346.
DR   IntAct; P09875; 5.
DR   STRING; 10116.ENSRNOP00000002724; -.
DR   SwissLipids; SLP:000001699; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; P09875; 2 sites, No reported glycans.
DR   GlyGen; P09875; 2 sites.
DR   iPTMnet; P09875; -.
DR   PhosphoSitePlus; P09875; -.
DR   PaxDb; 10116-ENSRNOP00000002724; -.
DR   Ensembl; ENSRNOT00000139046.1; ENSRNOP00000104488.1; ENSRNOG00000001990.6.
DR   GeneID; 286954; -.
DR   KEGG; rno:286954; -.
DR   UCSC; RGD:708541; rat.
DR   AGR; RGD:708541; -.
DR   CTD; 71773; -.
DR   RGD; 708541; Ugt2b1.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000153212; -.
DR   InParanoid; P09875; -.
DR   OMA; EFSDQMT; -.
DR   OrthoDB; 5835829at2759; -.
DR   PhylomeDB; P09875; -.
DR   BRENDA; 2.4.1.17; 5301.
DR   Reactome; R-RNO-156588; Glucuronidation.
DR   Reactome; R-RNO-9749641; Aspirin ADME.
DR   Reactome; R-RNO-9757110; Prednisone ADME.
DR   SABIO-RK; P09875; -.
DR   PRO; PR:P09875; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000001990; Expressed in duodenum and 11 other cell types or tissues.
DR   ExpressionAtlas; P09875; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0070980; P:biphenyl catabolic process; IDA:RGD.
DR   GO; GO:0071361; P:cellular response to ethanol; IEP:RGD.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR   GO; GO:0071378; P:cellular response to growth hormone stimulus; IEP:RGD.
DR   GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:RGD.
DR   GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR   GO; GO:0051291; P:protein heterooligomerization; ISO:RGD.
DR   GO; GO:0051260; P:protein homooligomerization; ISO:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:RGD.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   FunFam; 3.40.50.2000:FF:000001; UDP-glucuronosyltransferase; 1.
DR   FunFam; 3.40.50.2000:FF:000081; UDP-glucuronosyltransferase 2A2; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR050271; UDP-glycosyltransferase.
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:SF12; UDP-GLUCURONOSYLTRANSFERASE 2B4; 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   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..529
FT                   /note="UDP-glucuronosyltransferase 2B1"
FT                   /id="PRO_0000036025"
FT   TRANSMEM        494..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   529 AA;  60485 MW;  14DF0224BF1C3044 CRC64;
     MSMKQTSVFL LIQLICYFRP GACGKVLVWP TEYSHWINIK IILNELAQRG HEVTVLVSSA
     SILIEPTKES SINFEIYSVP LSKSDLEYSF AKWIDEWTRD FETLSIWTYY SKMQKVFNEY
     SDVVENLCKA LIWNKSLMKK LQGSQFDVIL ADAVGPCGEL LAELLKTPLV YSLRFCPGYR
     CEKFSGGLPL PPSYVPVVLS ELSDRMTFVE RVKNMLQMLY FDFWFQPFKE KSWSQFYSDV
     LGRPTTLTEM MGKADIWLIR TFWDLEFPHP FLPNFDFVGG LHCKPAKPLP REMEEFVQSS
     GEHGVVVFSL GSMVKNLTEE KANVVASALA QIPQKVVWRF DGKKPDTLGS NTRLYKWIPQ
     NDLLGHPKTK AFVAHGGTNG IYEAIYHGIP IVGIPLFADQ PDNINHMVAK GAAVRVDFSI
     LSTTGLLTAL KIVMNDPSYK ENAMRLSRIH HDQPVKPLDR AVFWIEYVMR HKGAKHLRST
     LHDLSWFQYH SLDVIGFLLL CVVGVVFIIT KFCLFCCRKT ANMGKKKKE
//