ID   UDB20_MACFA             Reviewed;         530 AA.
AC   O77649;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=UDP-glucuronosyltransferase 2B20;
DE            Short=UDPGT 2B20;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B20;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Liver, and Prostate;
RX   PubMed=9895303; DOI=10.1042/bj3370567;
RA   Barbier O., Belanger A., Hum D.W.;
RT   "Cloning and characterization of a simian UDP-glucuronosyltransferase
RT   enzyme UGT2B20, a novel C19 steroid-conjugating protein.";
RL   Biochem. J. 337:567-574(1999).
CC   -!- FUNCTION: UDPGTs are of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds. This isozyme has glucuronidating capacity with androgens,
CC       such as testosterone, dihydrotestosterone (DHT) and 3-alpha-diol. It is
CC       also active on catecholoestrogens including 1,3,5,10-oestratriene-3,4-
CC       diol-17-one.
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   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF072223; AAD08808.1; -; mRNA.
DR   RefSeq; NP_001271878.1; NM_001284949.1.
DR   AlphaFoldDB; O77649; -.
DR   SMR; O77649; -.
DR   STRING; 9541.XP_005555234.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 102128580; -.
DR   CTD; 102128580; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   OrthoDB; 508327at2759; -.
DR   Proteomes; UP000233100; 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; IEA:UniProtKB-EC.
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   Microsome; Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..530
FT                   /note="UDP-glucuronosyltransferase 2B20"
FT                   /id="PRO_0000036044"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         136
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   530 AA;  61225 MW;  A5EB47F8D517D8DA CRC64;
     MSLKWTSVFL LLQLSCYFSS GSCGKVLVWP TEYSHWINMK TILEELVRRR HEVTVLTSSA
     STFVNDSKSS AIKFEVYPTS LTKNDMEDSL MKLLDIWTYS ISNSTFLSYF SKLQELCWEY
     YYYSEKLCKD AVLNKKLMTK LKETKFDVIL ADALNPCGEL LAELFNIPFV YSLRFTVGYT
     FEKNGGGFLF PPSYVPVVMS ELSDQMTFTE RIKNMIHKLY FDFWFQIHDI KKWDQFYSEV
     LGRPTTLFET MRKAEMWLIR TYWDFEFPRP FLPNVDFVGG LHCKPAKPLP KEMEEFVQSS
     GENGVVVFSL GSMISNMSEE RANMIASALA QIPQKVLWKF DGKKPNTLGS NTRLYKWLPQ
     NDLLGHPKTK AFITHGGTNG IYEAIYHGIP MVGIPLFADQ HDNIVHMKVK GAALSVDIRT
     MSSRDLLNAL KSVINEPIYK ENAMKLSRIH HDQPMKPLDR AVFWIEFVMR HKGAKHLRVA
     AHNLTWIQYH SLDVIAFLLA CVAAVIFIIT KCCLFCFRKL AKTGKKKKWD