UD2B1_RAT
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 03-AUG-2022, entry version 159.
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 + 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: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) + 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 -!- 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 3-O-
CC (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_173295.1.
DR AlphaFoldDB; P09875; -.
DR SMR; P09875; -.
DR IntAct; P09875; 5.
DR STRING; 10116.ENSRNOP00000002724; -.
DR SwissLipids; SLP:000001699; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; P09875; 2 sites.
DR iPTMnet; P09875; -.
DR PhosphoSitePlus; P09875; -.
DR PaxDb; P09875; -.
DR PRIDE; P09875; -.
DR Ensembl; ENSRNOT00000002724; ENSRNOP00000002724; ENSRNOG00000001990.
DR GeneID; 286954; -.
DR KEGG; rno:286954; -.
DR UCSC; RGD:708541; rat.
DR CTD; 7367; -.
DR RGD; 708541; Ugt2b1.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000153212; -.
DR InParanoid; P09875; -.
DR OMA; CCHKTAN; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; P09875; -.
DR TreeFam; TF315472; -.
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 SABIO-RK; P09875; -.
DR PRO; PR:P09875; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000001990; Expressed in duodenum and 11 other tissues.
DR ExpressionAtlas; P09875; baseline and differential.
DR Genevisible; P09875; RN.
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:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070980; P:biphenyl catabolic process; IDA:RGD.
DR GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB.
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: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 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 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
