ID   UDB33_MACMU             Reviewed;         529 AA.
AC   Q9GLD9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=UDP-glucuronosyltransferase 2B33;
DE            Short=UDPGT 2B33;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B33;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Liver;
RX   PubMed=15130782; DOI=10.1016/j.abb.2004.03.035;
RA   Dean B., Arison B., Chang S., Thomas P.E., King C.;
RT   "Identification of UGT2B9*2 and UGT2B33 isolated from female rhesus monkey
RT   liver.";
RL   Arch. Biochem. Biophys. 426:55-62(2004).
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 estriol and
CC       does not catalyze the glucuronidation of beta-estradiol. Capable of
CC       conjugating 4-hydroxyestrone, androsterone, diclofenac, and
CC       hyodeoxycholic acid.
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; AF294902; AAG21378.1; -; mRNA.
DR   RefSeq; NP_001028002.1; NM_001032830.1.
DR   AlphaFoldDB; Q9GLD9; -.
DR   SMR; Q9GLD9; -.
DR   STRING; 9544.ENSMMUP00000035077; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PRIDE; Q9GLD9; -.
DR   GeneID; 574147; -.
DR   KEGG; mcc:574147; -.
DR   CTD; 574147; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; Q9GLD9; -.
DR   OrthoDB; 508327at2759; -.
DR   Proteomes; UP000006718; 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:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR   GO; GO:0008210; P:estrogen metabolic process; IBA:GO_Central.
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 2B33"
FT                   /id="PRO_0000036049"
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;  60858 MW;  B1956F947F1F78D6 CRC64;
     MSVKWTSIIL LIQLSFYFSS GSCGKVLVWA AEYSHWMNMK TILEELVQRG HEVTVLASSA
     SILFDPNNSS ALKIEVFPTS LTKTEFENII RQQIKRWSEL PKDTFWLYFS QIQEIMWRFG
     DISIKFCKDV VSNKKLMKKL QESRFDVVLA DPIFPCSELL AELFNIPLVY SLRFTPGYVF
     EKHCGGFLFP PSYVPVVMSE LSDQMTFMER VKNMIYVLYF DFCFQLYDMK KWDQFYSEVL
     GRHTTLSEIM GKADIWLIRN SWNFQFPHPL LPNVDFIGGL LCKPAKPLPK EMEEFVQSSG
     ENGVVVFTLG SMITNMKEER ANVIASALAQ IPQKVLWRFD GNKPDTLGVN TRLYKWIPQN
     DLLGHPKTKA FITHGGANGI YEAIYHGVPM VGIPLFADQP DNIAHMKTRG AAVQLDFDTM
     SSTDLANALK TVINDPLYKE NVMKLSRIQR DQPVKPLDRA VFWIEFVMRH KGAKHLRPAA
     HDLTWFQYHS LDVIGFLLAC VATVIFIIMK CCLFCFWKFT RKGKKGKSD