UD2B2_RAT
ID UD2B2_RAT Reviewed; 530 AA.
AC P08541;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=UDP-glucuronosyltransferase 2B2;
DE Short=UDPGT 2B2;
DE EC=2.4.1.17 {ECO:0000269|PubMed:2429951};
DE AltName: Full=3-hydroxyandrogen-specific UDPGT;
DE AltName: Full=RLUG23;
DE AltName: Full=UDPGTr-4 {ECO:0000303|PubMed:2429951};
DE Flags: Precursor;
GN Name=Ugt2b; Synonyms=Ugt2b2;
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 [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=2429951; DOI=10.1016/s0021-9258(18)66989-3;
RA McKenzie P.I.;
RT "Rat liver UDP-glucuronosyltransferase. cDNA sequence and expression of a
RT form glucuronidating 3-hydroxyandrogens.";
RL J. Biol. Chem. 261:14112-14117(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1909872; DOI=10.1089/dna.1991.10.515;
RA Haque S.J., Peterson D.D., Nebert D.W., McKenzie P.I.;
RT "Isolation, sequence, and developmental expression of rat UGT2B2: the gene
RT encoding a constitutive UDP glucuronosyltransferase that metabolizes
RT etiocholanolone and androsterone.";
RL DNA Cell Biol. 10:515-524(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-530.
RC TISSUE=Liver;
RX PubMed=3003696; DOI=10.1093/nar/14.2.779;
RA Jackson M.R., Burchell B.;
RT "The full length coding sequence of rat liver androsterone UDP-
RT glucuronyltransferase cDNA and comparison with other members of this gene
RT family.";
RL Nucleic Acids Res. 14:779-795(1986).
RN [4]
RP PROTEIN SEQUENCE OF 24-44, AND LIPID-BINDING.
RX PubMed=7492328; DOI=10.1042/bj3120301;
RA Yamashita A., Watanabe M., Tonegawa T., Sugiura T., Waku K.;
RT "Acyl-CoA binding and acylation of UDP-glucuronosyltransferase isoforms of
RT rat liver: their effect on enzyme activity.";
RL Biochem. J. 312:301-308(1995).
CC -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC subsequent elimination of potentially toxic xenobiotics and endogenous
CC compounds. 2B2 acts on various endogenous steroids, especially
CC etiocholanolone and androsterone.
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:2429951};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000305|PubMed:2429951};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: Constitutively expressed.
CC -!- PTM: Autoacylation in vitro.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02589; AAA42314.1; -; Genomic_DNA.
DR EMBL; M74439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X03478; CAA27198.1; -; mRNA.
DR PIR; A40467; A40467.
DR AlphaFoldDB; P08541; -.
DR SMR; P08541; -.
DR IntAct; P08541; 2.
DR STRING; 10116.ENSRNOP00000043239; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; P08541; 1 site.
DR iPTMnet; P08541; -.
DR PhosphoSitePlus; P08541; -.
DR PaxDb; P08541; -.
DR UCSC; RGD:3936; rat.
DR RGD; 3936; Ugt2b.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; P08541; -.
DR PhylomeDB; P08541; -.
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:P08541; -.
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; IDA:RGD.
DR GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR GO; GO:0008210; P:estrogen metabolic process; IBA:GO_Central.
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 Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Microsome; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:7492328"
FT CHAIN 24..530
FT /note="UDP-glucuronosyltransferase 2B2"
FT /id="PRO_0000036026"
FT TRANSMEM 494..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 159
FT /note="D -> E (in Ref. 3; CAA27198)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> S (in Ref. 3; CAA27198)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="N -> I (in Ref. 3; CAA27198)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> I (in Ref. 3; CAA27198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 60986 MW; F2FFF3E23E2D75B2 CRC64;
MPRKWISALF LLQISYCFKS GHCGKVLVWP MDFSHWMNIK IILDELVQRG HEVTVLKPSA
YFFLDPKKSS DLKFEIFSTS ISKDELQNHF IKLLDVWTYE LPRDTCLSYS PILQNLVYEF
SYFYLSICKD AVSNKQLMTK LQESKFDVLF ADPVASCGDL IAELLHIPFL YSLSFSPGHK
LEKSIGKFIL PPSYVPVILS GLAGKMTFID RVKNMICMLY FDFWFERLRH KEWDTFYSEI
LGRPTTVDET MSKVEIWLIR SYWDLKFPHP TLPNVDYIGG LHCKPAKPLP KDMEEFVQSS
GEHGVVVFSL GSMVSNMTEE KANAIAWALA QIPQKVLWKF DGKTPATLGP NTRVYKWLPQ
NDLLGHPKTK AFVTHGGANG LYEAIYHGIP MIGIPLFGDQ PDNIAHMVAK GAAVSLNIRT
MSKLDFLSAL EEVIDNPFYK KNVMLLSTIH HDQPMKPLDR AVFWIEFIMR HKGAKHLRPL
GHNLPWYQYH SLDVIGFLLT CFAVIAALTV KCLLFMYRFF VKKEKKMKNE
