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 11-JUL-2012, entry version 94. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX MEDLINE=87033594; PubMed=2429951; RA McKenzie P.I.; RT "Rat liver UDP-glucuronosyltransferase. cDNA sequence and expression RT of a form glucuronidating 3-hydroxyandrogens."; RL J. Biol. Chem. 261:14112-14117(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91369480; 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 RT gene encoding a constitutive UDP glucuronosyltransferase that RT metabolizes etiocholanolone and androsterone."; RL DNA Cell Biol. 10:515-524(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-530. RC TISSUE=Liver; RX MEDLINE=86120371; 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 RT gene family."; RL Nucleic Acids Res. 14:779-795(1986). RN [4] RP PROTEIN SEQUENCE OF 24-44, AND LIPID-BINDING. RX MEDLINE=96077159; PubMed=7492328; RA Yamashita A., Watanabe M., Tonegawa T., Sugiura T., Waku K.; RT "Acyl-CoA binding and acylation of UDP-glucuronosyltransferase RT isoforms of 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 CC endogenous compounds. 2B2 acts on various endogenous steroids, CC especially etiocholanolone and androsterone. CC -!- CATALYTIC ACTIVITY: UDP-glucuronate + acceptor = UDP + acceptor CC beta-D-glucuronoside. CC -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane CC protein (Potential). Endoplasmic reticulum membrane; Single-pass CC membrane protein (Potential). CC -!- INDUCTION: Constitutively expressed. CC -!- PTM: Autoacylation in vitro. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. 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 IPI; IPI00212110; -. DR PIR; A40467; A40467. DR UniGene; Rn.2521; -. DR ProteinModelPortal; P08541; -. DR SMR; P08541; 286-447. DR IntAct; P08541; 1. DR STRING; P08541; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR PRIDE; P08541; -. DR UCSC; RGD:3936; rat. DR RGD; 3936; Ugt2b. DR eggNOG; COG1819; -. DR HOGENOM; HOG000220831; -. DR HOVERGEN; HBG004033; -. DR BRENDA; 2.4.1.17; 5301. DR Genevestigator; P08541; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell. DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:RGD. DR InterPro; IPR002213; UDP_glucos_trans. DR PANTHER; PTHR11926; UDP_glucos_trans; 1. DR Pfam; PF00201; UDPGT; 1. DR PROSITE; PS00375; UDPGT; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Glycoprotein; Glycosyltransferase; Membrane; Microsome; KW Reference proteome; Signal; Transferase; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 23 FT CHAIN 24 530 UDP-glucuronosyltransferase 2B2. FT /FTId=PRO_0000036026. FT TRANSMEM 494 510 Helical; (Potential). FT CARBOHYD 316 316 N-linked (GlcNAc...) (Potential). FT CONFLICT 159 159 D -> E (in Ref. 3; CAA27198). FT CONFLICT 286 286 A -> S (in Ref. 3; CAA27198). FT CONFLICT 351 351 N -> I (in Ref. 3; CAA27198). FT CONFLICT 363 363 L -> I (in Ref. 3; CAA27198). 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 //