ID   UDB23_MACFA             Reviewed;         529 AA.
AC   Q9TSL6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=UDP-glucuronosyltransferase 2B23;
DE            Short=UDPGT 2B23;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B23;
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.
RX   PubMed=10579317; DOI=10.1210/endo.140.12.7192;
RA   Barbier O., Levesque E., Belanger A., Hum D.W.;
RT   "UGT2B23, a novel uridine diphosphate-glucuronosyltransferase enzyme
RT   expressed in steroid target tissues that conjugates androgen and estrogen
RT   metabolites.";
RL   Endocrinology 140:5538-5548(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 on 6 steroids and
CC       the bile acid, hyodeoxycholic acid. May potentially play an important
CC       role in estrogen and androgen catabolism in peripheral steroid target
CC       tissues.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.9 uM for androsterone;
CC         KM=13.5 uM for 3-alpha-diol;
CC         KM=1.6 uM for estriol;
CC         KM=5.7 uM for 4-hydroxyestrone;
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   -!- TISSUE SPECIFICITY: Expressed in several tissues, including the
CC       prostate, mammary gland, epididymis, testis and ovary.
CC       {ECO:0000269|PubMed:10579317}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF112113; AAF14353.1; -; mRNA.
DR   RefSeq; NP_001271768.1; NM_001284839.1.
DR   AlphaFoldDB; Q9TSL6; -.
DR   SMR; Q9TSL6; -.
DR   STRING; 9541.XP_005555223.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 102125239; -.
DR   CTD; 102125239; -.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..529
FT                   /note="UDP-glucuronosyltransferase 2B23"
FT                   /id="PRO_0000036045"
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"
SQ   SEQUENCE   529 AA;  60957 MW;  646315E6D970541A CRC64;
     MSVKWTSVIL LIQLSFYFSS GSCGKVLVWA AEYSHWMNMK TILEELVQRG HEVTALASSA
     SILFDPNNSS ALKIEVFPTS LPKPEFENIV TQEIKRWIEL PKDTFWLYFS QMQEIMWKFG
     DIFRNFCKDV VSNKKLMKKL QESRFDVVFA DPIFPCSELL AELFNIPLVY SLRFTPGYVF
     EKHCGGFLFP PSYVPVVMSE LSDQMTFMER VKNMIYMLYF DFCFQIYDMK KWDQFYTEVL
     GRHTTLSEIM GKADIWLIRN SWNFQFPHPL LPNVDFIGGL LCKPAKPLPK EMEEFVQSSG
     ENGVVVFTLG SMITNMKEER ANVIASALAQ IPQKVLWRFD GNKPDTLGVN TRLYKWIPQN
     DLLGHPKTKA FITHGGANGI YEAIYHGVPM VGIPLFADQP DNIAHMKTRG AAVQLDFDTM
     SSTDLVNALK TVINDPLYKE NVMKLSRIQR DQPVKPLDRA VFWIEFVMRH KGAKHLRPAA
     HDLTWFQYHS FDVIGFLLAC VATVIFIIMK CCLFCFWKFA RKGKKGKSD