ID   UDB37_RAT               Reviewed;         530 AA.
AC   P19488; P19489;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=UDP-glucuronosyltransferase 2B37;
DE            Short=UDPGT 2B37;
DE            EC=2.4.1.17 {ECO:0000269|PubMed:1692835};
DE   AltName: Full=17-beta-hydroxysteroid-specific UDPGT;
DE   AltName: Full=UDP-glucuronosyltransferase R-21;
DE            Short=UDPGTr-21;
DE   AltName: Full=UDPGTr-5;
DE   Flags: Precursor;
GN   Name=Ugt2b37; Synonyms=Ugt2b5, Ugt2b6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=1692835; DOI=10.1016/s0021-9258(19)38945-8;
RA   McKenzie P.I.;
RT   "The cDNA sequence and expression of a variant 17 beta-hydroxysteroid UDP-
RT   glucuronosyltransferase.";
RL   J. Biol. Chem. 265:8699-8703(1990).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds. About 30-fold less active than Ugt2b17 toward testosterone
CC       and dihydrotestosterone. {ECO:0000269|PubMed:1692835}.
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         Evidence={ECO:0000269|PubMed:1692835};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC         Evidence={ECO:0000305|PubMed:1692835};
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   -!- INDUCTION: Constitutively expressed.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M33746; AAA03216.1; -; mRNA.
DR   EMBL; M33746; AAA03217.1; -; mRNA.
DR   EMBL; M33747; AAA03218.1; -; mRNA.
DR   EMBL; M33747; AAA03219.1; -; mRNA.
DR   PIR; A36276; A36276.
DR   AlphaFoldDB; P19488; -.
DR   SMR; P19488; -.
DR   STRING; 10116.ENSRNOP00000045002; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; P19488; -.
DR   PhosphoSitePlus; P19488; -.
DR   PaxDb; P19488; -.
DR   UCSC; RGD:3937; rat.
DR   RGD; 3937; Ugt2b37.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; P19488; -.
DR   PhylomeDB; P19488; -.
DR   Reactome; R-RNO-156588; Glucuronidation.
DR   Reactome; R-RNO-9749641; Aspirin ADME.
DR   Reactome; R-RNO-9753281; Paracetamol ADME.
DR   PRO; PR:P19488; -.
DR   Proteomes; UP000002494; 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; IDA:RGD.
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; Glycosyltransferase; Membrane; Microsome;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..530
FT                   /note="UDP-glucuronosyltransferase 2B37"
FT                   /id="PRO_0000036030"
FT   TRANSMEM        494..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        397
FT                   /note="F -> L (in Ref. 1; AAA03218/AAA03219)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        444
FT                   /note="M -> T (in Ref. 1; AAA03218/AAA03219)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   530 AA;  60593 MW;  F6B23E436B9BDAEA CRC64;
     MPGKWIFALL LLQISFCLRS AKCGKVLVWP MEFSHWMNIK TILDELVQRG HEVTVLKPSA
     YYVLDPKKSP DLKFETFPTS VSKDELEKYF IKLADAWTYE LQRDTCLSFS PLLQNMMDEF
     SDYYLSVCKD AVSNKQLMAK LQESKFDVLL SDPVAACGEL IAEVLHIPFL YSLRASPGHK
     IEKSSGRFIL PPSYVPVILS GLGGQMTFID RVKNMICMLY FDFWFHMFNA KNWDPFYTEI
     LGRPTTLAET MGKAEMWLIR SYWDLEFPHP TLPNVDYIGG LQCKPAKPLP KDIEDFVQSS
     GEHGVVVFSL GSMVSSMTEE KANAIAWALA QIPQKVLWKF DGKIPATLGP NTRVYKWLPQ
     NDLLGHPKTK AFVTHGGANG VYEAIYHGIP MIGIPMFGEQ HDNIAHMVAK GAAVTLNIRT
     MSKSDLFNAL KEVINNPFYK KNAMWLSTIH HDQPMKPLDK AIFWIEYVMR HKRAKHLRPL
     GHNLPWYQYH SLDVIGFLLA CLAVIAALAV KCFLFIYRFF AKKQKKMKNE