ID   UDB30_MACFA             Reviewed;         528 AA.
AC   Q8WN97;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=UDP-glucuronosyltransferase 2B30;
DE            Short=UDPGT 2B30;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B30;
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=12071853; DOI=10.1042/bj20011594;
RA   Girard C., Barbier O., Turgeon D., Belanger A.;
RT   "Isolation and characterization of the monkey UGT2B30 gene that encodes a
RT   uridine diphosphate-glucuronosyltransferase enzyme active on
RT   mineralocorticoid, glucocorticoid, androgen and oestrogen hormones.";
RL   Biochem. J. 365:213-222(2002).
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 testosterone,
CC       dihydrotestosterone, 5-alpha-androstane-3-alpha,17-beta-diol,
CC       androsterone, oestradiol, tetrahydroaldosterone and
CC       tetrahydrocortisone. This enzyme is essential to inactivation of
CC       several steroids.
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   -!- TISSUE SPECIFICITY: Expressed in several tissues, including prostate,
CC       testis, mammary gland, kidney, adrenals and intestine.
CC       {ECO:0000269|PubMed:12071853}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF401657; AAL60145.1; -; mRNA.
DR   RefSeq; NP_001306409.1; NM_001319480.1.
DR   AlphaFoldDB; Q8WN97; -.
DR   SMR; Q8WN97; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 102127692; -.
DR   SABIO-RK; Q8WN97; -.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..528
FT                   /note="UDP-glucuronosyltransferase 2B30"
FT                   /id="PRO_0000036047"
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;  60366 MW;  361349D4717C68D5 CRC64;
     MSMKWTSALL LIQLSCYLSS GNCGKVLVWP TEFSHWMNIK TILDELVQRG HEVTVLAYSP
     SILPGPNNPS ALKFEICPTS LTETEFEDSV TQLVKRWSDI PKDTFWPHFL QVQEMMWTYG
     DMIRKFCKDV VSNKKLMKKL QESRFDVVLA DAISPCGELL AELLKIPFVY SLRFSPGYAI
     EKHGGGFLFP PSYVPVVMSE FSDQMTFMER VKNMIYMVYF DFWFQAWDTK KWDQFYSEVL
     GRPTTLFETM AKAEIWLIRN YWDFQFPHPL LPHVELVGGL HCKPAKPLPK EMEGFVQSSG
     DNGVVVFSLG SMVSNMSEER ANVIASALAK IPQKVLWRFD GNKPDTLGLN TQLYKWLPQN
     DLLGHPKTRA FITHGGANAI YEAIYHGIPM VGVPLFADQL DNIAHMKAKG ARVSLDFNTM
     SSTDLLHALK TVINDPFYKE NAMKLSSIHH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA
     YDLTWFQYHS LDVIGFLLAC VATVIFIITK CLFCVLKFVR TGKKGKRD