ID   UDB19_MACFA             Reviewed;         528 AA.
AC   Q9XT55;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=UDP-glucuronosyltransferase 2B19;
DE            Short=UDPGT 2B19;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B19;
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=10102998; DOI=10.1046/j.1432-1327.1999.00197.x;
RA   Belanger G., Barbier O., Hum D.W., Belanger A.;
RT   "Molecular cloning, expression and characterization of a monkey steroid
RT   UDP-glucuronosyltransferase, UGT2B19, that conjugates testosterone.";
RL   Eur. J. Biochem. 260:701-708(1999).
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 several classes of
CC       xenobiotic substrates: eugenol, 4-methyllumbelliferone, p-nitrophenol,
CC       1-naphthol, p,p'-biphenol, naringenin and o,o'-biphenol. Active also on
CC       3a-hydroxy and 17b-hydroxy positions of steroids.
CC   -!- FUNCTION: Contributes to the formation of androgen glucuronide in
CC       extrahepatic steroid target tissues such as the prostate.
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, ovary, prostate, colon, kidney,
CC       pancreas, brain, cerebellum, mammary gland and epididymis. Not
CC       expressed in small intestine, spleen, bladder, adrenal gland and
CC       testis.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF112112; AAD24435.1; -; mRNA.
DR   RefSeq; NP_001306405.1; NM_001319476.1.
DR   AlphaFoldDB; Q9XT55; -.
DR   SMR; Q9XT55; -.
DR   STRING; 9541.XP_005555219.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 102123935; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   SABIO-RK; Q9XT55; -.
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..528
FT                   /note="UDP-glucuronosyltransferase 2B19"
FT                   /id="PRO_0000036043"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   528 AA;  60742 MW;  3BFD2AE714A27AEE CRC64;
     MSMKWTSALL LIQLSCYLSF GSCGKVLVWP TEFSHWMNIK TILDELVQRG HEVTVLAYST
     SILPDPNNPS PLKFEICPTS LTETEFQDSV TQLVKRWSDI RKDTFWPHFL HVQEMMWTYG
     DMIRKFCKDV VSNKKLMKKL QESRFDVVLA DAISPCGELL AELLKIPFVY SLRFSPGYAL
     EKHGGGFLFP PSYVPVTMSE LRDQMTFMER VQNMIYMVYF DFWFQVWDVK NWDQFYSKVL
     GRPTTLFEIM AKAEIWLIRN YWDFQFPHPL LPNVEFVGGL HCKPAKPLPK EMEEFVQSSG
     DNGVVVFSLG SMVSNMSEER ANVIASALAK IPQKVLWRFD GNKPDTLGLN TQLYKWLPQN
     DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGVPLFADQP DNIAHMKAKG AAVRLDFDTM
     SSTDLLNALK TVINDPIYKE NAMKLSSIHH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA
     HDLTWFQYHS LDVIGFLLAC VATVIFIITK CLFCVWKFVR TRKKGKRD