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Database: UniProt
Entry: UD11_MOUSE
LinkDB: UD11_MOUSE
Original site: UD11_MOUSE 
ID   UD11_MOUSE              Reviewed;         535 AA.
AC   Q63886; Q561M6; Q6XL50;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=UDP-glucuronosyltransferase 1A1 {ECO:0000305};
DE            Short=UGT1A1;
DE            EC=2.4.1.17 {ECO:0000250|UniProtKB:P22309};
DE   AltName: Full=UDP-glucuronosyltransferase 1-1;
DE            Short=UDPGT 1-1;
DE            Short=UGT1*1;
DE            Short=UGT1-01;
DE            Short=UGT1.1;
DE   AltName: Full=UGTBR1;
DE   Flags: Precursor;
GN   Name=Ugt1a1 {ECO:0000312|MGI:MGI:98898}; Synonyms=Ugt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8464825; DOI=10.1023/a:1018965011846;
RA   Kong A.N., Ma M., Tao D., Yang L.;
RT   "Molecular cloning of two cDNAs encoding the mouse bilirubin/phenol family
RT   of UDP-glucuronosyltransferases (mUGTBr/p).";
RL   Pharm. Res. 10:461-465(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Colon;
RX   PubMed=14672974; DOI=10.1101/gr.1225204;
RA   Zhang T., Haws P., Wu Q.;
RT   "Multiple variable first exons: a mechanism for cell- and tissue-specific
RT   gene regulation.";
RL   Genome Res. 14:79-89(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II
CC       biotransformation reactions in which lipophilic substrates are
CC       conjugated with glucuronic acid to increase the metabolite's water
CC       solubility, thereby facilitating excretion into either the urine or
CC       bile (By similarity). Essential for the elimination and detoxification
CC       of drugs, xenobiotics and endogenous compounds (By similarity).
CC       Catalyzes the glucuronidation of endogenous estrogen hormones such as
CC       estradiol, estrone and estriol (By similarity). Involved in the
CC       glucuronidation of bilirubin, a degradation product occurring in the
CC       normal catabolic pathway that breaks down heme in vertebrates (By
CC       similarity). Also catalyzes the glucuronidation the isoflavones
CC       genistein, daidzein, glycitein, formononetin, biochanin A and prunetin,
CC       which are phytoestrogens with anticancer and cardiovascular properties
CC       (By similarity). Involved in the glucuronidation of the AGTR1
CC       angiotensin receptor antagonist losartan, a drug which can inhibit the
CC       effect of angiotensin II (By similarity). Involved in the
CC       biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the
CC       pharmacologically active metabolite of the anticancer drug irinotecan
CC       (By similarity). {ECO:0000250|UniProtKB:Q64550}.
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:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + UDP-alpha-D-glucuronate = 17beta-estradiol
CC         3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:52460,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136641;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52461;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyestrone + UDP-alpha-D-glucuronate = 2-hydroxyestrone
CC         3-O-(beta-D-glucuronate) + H(+) + UDP; Xref=Rhea:RHEA:53048,
CC         ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:136967;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53049;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2-
CC         hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:53004, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136931;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53005;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methoxy-17beta-estradiol + UDP-alpha-D-glucuronate = 2-
CC         methoxy-17beta-estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:53072, ChEBI:CHEBI:15378, ChEBI:CHEBI:28955,
CC         ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136974;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53073;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC         estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:52868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC         ChEBI:CHEBI:57529, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16beta,17beta-estriol + UDP-alpha-D-glucuronate =
CC         16beta,17beta-estriol 16-O-(beta-D-glucuronate) + H(+) + UDP;
CC         Xref=Rhea:RHEA:52880, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:87620, ChEBI:CHEBI:136886;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52881;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=losartan + UDP-alpha-D-glucuronate = losartan-2-N-beta-D-
CC         glucuronide + UDP; Xref=Rhea:RHEA:63720, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:149504, ChEBI:CHEBI:149507;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63721;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prunetin + UDP-alpha-D-glucuronate = prunetin-4'-O-beta-D-
CC         glucuronide + UDP; Xref=Rhea:RHEA:63588, ChEBI:CHEBI:58052,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:147403, ChEBI:CHEBI:147404;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63589;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=SN-38 + UDP-alpha-D-glucuronate = H(+) + SN-38 O-beta-D-
CC         glucuronide + UDP; Xref=Rhea:RHEA:63696, ChEBI:CHEBI:8988,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:149482; Evidence={ECO:0000250|UniProtKB:P22309};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63697;
CC         Evidence={ECO:0000250|UniProtKB:P22309};
CC   -!- SUBUNIT: Homodimers. Homooligomer. Interacts with UGT1A3, UGT1A4,
CC       UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10 to form heterodimers.
CC       {ECO:0000250|UniProtKB:P22309}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P22309}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=UGT1A1 is one of the isoforms produced at the UGT1A complex
CC         locus. The UGT1A complex locus produces different isoforms based on
CC         alternative use of promoters, first exons and terminal exons.
CC         {ECO:0000250|UniProtKB:P22309};
CC       Name=1;
CC         IsoId=Q63886-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and at lower levels in
CC       colon, kidney, stomach and intestine. {ECO:0000269|PubMed:14672974}.
CC   -!- INDUCTION: By dioxin.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; S64760; AAB26033.2; -; mRNA.
DR   EMBL; AY227194; AAP48593.1; -; mRNA.
DR   EMBL; BC093516; AAH93516.1; -; mRNA.
DR   CCDS; CCDS15143.1; -. [Q63886-1]
DR   RefSeq; NP_964007.2; NM_201645.2. [Q63886-1]
DR   AlphaFoldDB; Q63886; -.
DR   SMR; Q63886; -.
DR   STRING; 10090.ENSMUSP00000072803; -.
DR   ChEMBL; CHEMBL4523337; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; Q63886; 3 sites, No reported glycans.
DR   GlyGen; Q63886; 3 sites.
DR   iPTMnet; Q63886; -.
DR   PhosphoSitePlus; Q63886; -.
DR   SwissPalm; Q63886; -.
DR   jPOST; Q63886; -.
DR   MaxQB; Q63886; -.
DR   PaxDb; 10090-ENSMUSP00000072803; -.
DR   PeptideAtlas; Q63886; -.
DR   ProteomicsDB; 298192; -. [Q63886-1]
DR   Pumba; Q63886; -.
DR   Antibodypedia; 35061; 266 antibodies from 27 providers.
DR   DNASU; 394436; -.
DR   Ensembl; ENSMUST00000073049.7; ENSMUSP00000072803.7; ENSMUSG00000089960.2. [Q63886-1]
DR   GeneID; 394436; -.
DR   KEGG; mmu:394436; -.
DR   UCSC; uc007byk.1; mouse. [Q63886-1]
DR   AGR; MGI:98898; -.
DR   CTD; 54658; -.
DR   MGI; MGI:98898; Ugt1a1.
DR   VEuPathDB; HostDB:ENSMUSG00000089960; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000159677; -.
DR   HOGENOM; CLU_012949_3_0_1; -.
DR   InParanoid; Q63886; -.
DR   OMA; SFRTEIY; -.
DR   OrthoDB; 382054at2759; -.
DR   PhylomeDB; Q63886; -.
DR   TreeFam; TF315472; -.
DR   BRENDA; 2.4.1.17; 3474.
DR   Reactome; R-MMU-156588; Glucuronidation.
DR   Reactome; R-MMU-189483; Heme degradation.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   Reactome; R-MMU-9753281; Paracetamol ADME.
DR   BioGRID-ORCS; 394436; 15 hits in 81 CRISPR screens.
DR   PRO; PR:Q63886; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q63886; Protein.
DR   Bgee; ENSMUSG00000089960; Expressed in duodenum and 47 other cell types or tissues.
DR   Genevisible; Q63886; MM.
DR   GO; GO:0070069; C:cytochrome complex; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0004857; F:enzyme inhibitor activity; ISO:MGI.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0001972; F:retinoic acid binding; ISO:MGI.
DR   GO; GO:0005496; F:steroid binding; ISO:MGI.
DR   GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
DR   GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR   GO; GO:0070980; P:biphenyl catabolic process; ISO:MGI.
DR   GO; GO:0052695; P:cellular glucuronidation; ISS:UniProtKB.
DR   GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR   GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR   GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0051552; P:flavone metabolic process; ISO:MGI.
DR   GO; GO:0052696; P:flavonoid glucuronidation; ISO:MGI.
DR   GO; GO:0001889; P:liver development; IEA:Ensembl.
DR   GO; GO:2001030; P:negative regulation of cellular glucuronidation; ISO:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR   GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR   GO; GO:0042594; P:response to starvation; IEA:Ensembl.
DR   GO; GO:0052697; P:xenobiotic glucuronidation; ISS:UniProtKB.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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:SF147; UDP GLUCURONOSYLTRANSFERASE 1 FAMILY, POLYPEPTIDE A7; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW   Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW   Signal; Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..535
FT                   /note="UDP-glucuronosyltransferase 1A1"
FT                   /id="PRO_0000036010"
FT   TRANSMEM        493..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        25
FT                   /note="S -> Y (in Ref. 1; AAB26033)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="L -> I (in Ref. 1; AAB26033)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="H -> R (in Ref. 2; AAP48593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   535 AA;  60047 MW;  8C938AFD2D6DEB1D CRC64;
     MTVVCWSSRL LLLLPYLLLC VFGPSASHAG RLLVFPMDGS HWLSMLGVIQ QLQQKGHEVV
     VIAPEASIHI KEGSFYTLRK FPVPFQKENV TATLVELGRT AFNQDSFLLR VVKIYMKVKR
     DSSMLLAGCS HLLHNAEFMA SLEESHFDAL LTDPFLPCGS IVAQYLTVPT VYFLNKLPCS
     LDSEATQCPV PLSYVPKSLS FNSDRMNFLQ RVKNVLLAVS ENFMCRVVYS PYGSLATEIL
     QKEVTVQDLL SPASIWLMRS DFVKDYPRPI MPNMVFIGGI NCLQKKPLSQ EFEAYVNASG
     EHGIVVFSLG SMVSEIPEKK AMEIAEALGR IPQTVLWRYT GTRPSNLAKN TILVKWLPQN
     DLLGHPKTRA FITHSGSHGI YEGICNGVPM VMMPLFGDQM DNAKRMETRG AGVTLNVLEM
     TADDLENALK TVINNKSYKE NIMRLSSLHK DRPIEPLDLA VFWVEYVMRH KGAPHLRPAA
     HDLTWYQYHS LDVIGFLLAI VLTVVFIVFK CCAYGCRKCF GGKGRVKKSH KSKTH
//
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