ID   UD12_RAT                Reviewed;         533 AA.
AC   P20720; Q64636;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   02-SEP-2026, entry version 138.
DE   RecName: Full=UDP-glucuronosyltransferase 1-2;
DE            Short=UDPGT 1-2;
DE            Short=UGT1*2;
DE            Short=UGT1-02;
DE            Short=UGT1.2;
DE            EC=2.4.1.17;
DE   AltName: Full=B2;
DE   AltName: Full=Bilirubin-specific UDPGT;
DE   AltName: Full=UDP-glucuronosyltransferase 1A2;
DE            Short=UGT1A2;
DE   Flags: Precursor;
GN   Name=Ugt1a2; Synonyms=Ugt1;
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].
RC   TISSUE=Liver;
RX   PubMed=2112380; DOI=10.1016/0006-291x(90)91462-2;
RA   Sato H., Koiwai O., Tanabe K., Kashiwamata S.;
RT   "Isolation and sequencing of rat liver bilirubin UDP-
RT   glucuronosyltransferase cDNA: possible alternate splicing of a common
RT   primary transcript.";
RL   Biochem. Biophys. Res. Commun. 169:260-264(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-288.
RC   STRAIN=Wistar;
RX   PubMed=7608130; DOI=10.1093/jb/117.2.392;
RA   Emi Y., Ikushiro S., Iyanagi T.;
RT   "Drug-responsive and tissue-specific alternative expression of multiple
RT   first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene
RT   complex.";
RL   J. Biochem. 117:392-399(1995).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC         beta-D-glucuronoside + UDP + H(+); 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. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. The different isozymes
CC         have a different N-terminal domain and a common C-terminal domain of
CC         245 residues.;
CC       Name=1;
CC         IsoId=P20720-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; M34007; AAA42312.1; -; mRNA.
DR   EMBL; D38066; BAA07261.1; -; Genomic_DNA.
DR   PIR; A35343; A35343.
DR   AlphaFoldDB; P20720; -.
DR   SMR; P20720; -.
DR   FunCoup; P20720; 15.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; P20720; 4 sites, No reported glycans.
DR   GlyGen; P20720; 4 sites.
DR   PhosphoSitePlus; P20720; -.
DR   AGR; RGD:1549741; -.
DR   RGD; 1549741; Ugt1a2.
DR   InParanoid; P20720; -.
DR   BRENDA; 2.4.1.17; 5301.
DR   Reactome; R-RNO-156588; Glucuronidation.
DR   Reactome; R-RNO-189483; Heme degradation.
DR   Reactome; R-RNO-9749641; Aspirin ADME.
DR   Reactome; R-RNO-9754706; Atorvastatin ADME.
DR   Reactome; R-RNO-9757110; Prednisone ADME.
DR   PRO; PR:P20720; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IBA:GO_Central.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; ISO:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0001972; F:retinoic acid binding; ISO:RGD.
DR   GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR   GO; GO:0032782; P:bile acid secretion; ISO:RGD.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IBA:GO_Central.
DR   GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR   GO; GO:0051552; P:flavone metabolic process; IBA:GO_Central.
DR   GO; GO:0009812; P:flavonoid metabolic process; ISO:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0070640; P:vitamin D3 metabolic process; ISO:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   FunFam; 3.40.50.2000:FF:000001; UDP-glucuronosyltransferase; 1.
DR   FunFam; 3.40.50.2000:FF:000066; UDP-glucuronosyltransferase 1-1; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR050271; UDP-glycosyltransferase.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   PANTHER; PTHR48043:SF161; UDP GLUCURONOSYLTRANSFERASE FAMILY 1 MEMBER A1; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW   Glycosyltransferase; Membrane; Microsome; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..533
FT                   /note="UDP-glucuronosyltransferase 1-2"
FT                   /id="PRO_0000036013"
FT   TRANSMEM        491..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        2..3
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177..178
FT                   /note="CG -> SP (in Ref. 2; BAA07261)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   533 AA;  60045 MW;  5A9E974EF7EBAF5B CRC64;
     MDTGLCAPLR GLSGLLLLLC ALPWAEGGKV LVFPMEGSHW LSMRDVVREL HARGHQAVVL
     APEVTVHMKG EDFFTLQTYA FPYTKEEYQR EILGNAKKGF EPQHFVKTFF ETMASIKKFF
     DLYANSCAAL LHNKTLIQQL NSSSFDVVLT DPVFPCGALL AKYLQIPAVF FLRSVPCGID
     YEATQCPKPS SYIPNLLTML SDHMTFLQRV KNMLYPLTLK YICHLSITPY ESLASELLQR
     EMSLVEVLSH ASVWLFRGDF VFDYPRPIMP NMVFIGGINC VIKKPLSQEF EAYVNASGEH
     GIVVFSLGSM VSEIPEKKAM EIAEALGRIP QTLLWRYTGT RPSNLAKNTI LVKWLPQNDL
     LGHPKARAFI THSGSHGIYE GICNGVPMVM MPLFGDQMDN AKRMETRGAG VTLNVLEMTA
     DDLENALKTV INNKSYKENI MRLSSLHKDR PIEPLDLAVF WVEYVMRHKG APHLRPAAHD
     LTWYQYHSLD VIGFLLAIVL TVVFIVYKSC AYGCRKCFGG KGRVKKSHKS KTH
//