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 02-JUN-2021, entry version 135. DE RecName: Full=UDP-glucuronosyltransferase 2B2; DE Short=UDPGT 2B2; DE EC=2.4.1.17; DE AltName: Full=3-hydroxyandrogen-specific UDPGT; DE AltName: Full=RLUG23; DE AltName: Full=UDPGTr-4; 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]. RC TISSUE=Liver; RX PubMed=2429951; 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 -!- 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 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 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:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA: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 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 //