ID   UD2B9_MACFA             Reviewed;         529 AA.
AC   O02663;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=UDP-glucuronosyltransferase 2B9;
DE            Short=UDPGT 2B9;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B9;
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].
RC   TISSUE=Prostate;
RX   PubMed=9364930; DOI=10.1089/dna.1997.16.1195;
RA   Belanger G., Beaulieu M., Levesque E., Hum D.W., Belanger A.;
RT   "Expression and characterization of a novel UDP-glucuronosyltransferase,
RT   UGT2B9, from cynomolgus monkey.";
RL   DNA Cell Biol. 16:1195-1205(1997).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds. This isozyme is active on C18, C19, and C21 steroids, bile
CC       acids, and several xenobiotics including eugenol, 1-naphthol, and p-
CC       nitrophenol.
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; U91582; AAB50249.1; -; mRNA.
DR   RefSeq; NP_001270204.1; NM_001283275.1.
DR   AlphaFoldDB; O02663; -.
DR   SMR; O02663; -.
DR   STRING; 9541.XP_005555232.1; -.
DR   ChEMBL; CHEMBL3763003; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 102127901; -.
DR   CTD; 57721; -.
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   GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Bile acid catabolism; Endoplasmic reticulum; Glycoprotein;
KW   Glycosyltransferase; Lipid degradation; Lipid metabolism; Membrane;
KW   Microsome; Reference proteome; Signal; Steroid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..529
FT                   /note="UDP-glucuronosyltransferase 2B9"
FT                   /id="PRO_0000036033"
FT   TRANSMEM        494..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        68
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   529 AA;  60970 MW;  F110F85FE3A9DB8D CRC64;
     MSVKWTSVIL LIQLSFYFSS GSCGKVLVWA AEYSHWMNMK TILEELVQRG HEVTVLASSA
     SILFDPNNSS ALKIEVFPTS LTKTEFENIS MQEVKRWIEL PKDTFWLYFS QMQEIMWRFG
     DIIRNFCKDV VSNKKLMKKL QESRFDVVFA DPIFPCSELL AELFNIPLVY SLRFTPGYIF
     EKHCGGFLFP PSYVPVVMSE LSDQMTFMER VKNMIYMLSF DFYFQMYDMK KWDQFYSEVL
     GRPTTLSETM GKADIWLIRN SWNFQFPHPL LPNVDFVGGL HCKPAKPLPK EMEEFVQSSG
     ENGVVVFSLG SMVTNMEEER ANVIASALAQ IPQKVLWRFD GKKPDTLGLN TRLYKWIPQN
     DLLGHPKTRA FITHGGANGI YEAIYHGVPM VGIPLFADQP DNIAHMKTKG AAVRLDFDTM
     SSTDLANRLK TVINDPLYKE NVMKLSRIQH DQPVKPLDRA VFWIEFVMRH KGAKHLRPAA
     HDLTWFQYHS LDVIGFLLAC VATVIFVIMK CCLFCFWKFA RKGKKGKSD