ID   UDB18_MACFA             Reviewed;         529 AA.
AC   O97951;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=UDP-glucuronosyltransferase 2B18;
DE            Short=UDPGT 2B18;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B18;
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], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Prostate;
RX   PubMed=9480769; DOI=10.1006/jmbi.1997.1486;
RA   Beaulieu M., Levesque E., Barbier O., Turgeon D., Belanger G., Hum D.W.,
RA   Belanger A.;
RT   "Isolation and characterization of a simian UDP-glucuronosyltransferase
RT   UGT2B18 active on 3-hydroxyandrogens.";
RL   J. Mol. Biol. 275:785-794(1998).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds. This isozyme displays activity toward 3-hydroxyandrogens. It
CC       is principally active on C19 steroids having a hydroxyl group at
CC       position 3-alpha of the steroid molecule and also active on planar
CC       phenols and bile acids.
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:0000250}; Single-pass
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, prostate, kidney, testis,
CC       adrenal, bile duct, bladder, colon, small intestine, cerebellum and
CC       pancreas. {ECO:0000269|PubMed:9480769}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF016310; AAC98726.1; -; mRNA.
DR   RefSeq; NP_001306408.1; NM_001319479.1.
DR   AlphaFoldDB; O97951; -.
DR   SMR; O97951; -.
DR   STRING; 9541.XP_005555229.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 102127013; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   SABIO-RK; O97951; -.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..529
FT                   /note="UDP-glucuronosyltransferase 2B18"
FT                   /id="PRO_0000036042"
FT   TRANSMEM        493..513
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"
SQ   SEQUENCE   529 AA;  60801 MW;  3ECEB497B8C3601F CRC64;
     MSVKWTSVIL LIQLSFYFSS GSCGKVLVWA AEYSHWMNMK TILEELVQRG HEVTVLASSA
     SILFDPNNSS ALKIEVFPTS LTKTEFENII RQQIKRWSEL PKDTFWLYFS QMQEIMWKFG
     DITRNFCKDV VSNKKLMKKL QKSRFDVVFA DAIFPCSELL AELLNTPLVY SLRFTPGYNF
     EKHCGGFLFP PSYVPVVMSE LSDHMTFMER VKNMIYMLYF DFCFQIYAMK KWDQFYSEVL
     GRPTTLSETM GKADIWLIRN SWNFQFPHPL LPNVDFVGGL HCKPAKPLPK EMEEFVQSSG
     ENGVVVFSLG SMVTNMKEER ANVIASALAQ IPQKVLWRFD GKKPDTLGLN TRLYKWIPQN
     DLLGHPKTRA FITHGGSNGI YEAIYHGVPM VGIPLFADQP DNIAHMKAKG AAVRLDFDTM
     SSTDLVNALK TVINDPLYKE NVMKLSRIQH DQPVKPLDRA VFWIEFVMRH KGAKHLRPAA
     HDLTWFQYHS LDVIGFLLAC VATVIFIIMK CCLFCFWKFA RKGKKGKSD