UD12_RAT
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 03-AUG-2022, entry version 126.
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 + 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. 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 CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; P20720; 4 sites.
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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0015020; F:glucuronosyltransferase 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:0052695; P:cellular glucuronidation; ISO:RGD.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:RGD.
DR GO; GO:0052696; P:flavonoid glucuronidation; ISO:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0070640; P:vitamin D3 metabolic process; ISO:RGD.
DR GO; GO:0052697; P:xenobiotic glucuronidation; ISO:RGD.
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 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
