UD16_MOUSE
ID UD16_MOUSE Reviewed; 531 AA.
AC Q64435; P70692; Q62580; Q6XL47;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=UDP-glucuronosyltransferase 1-6;
DE Short=UDPGT 1-6;
DE Short=UGT1*6;
DE Short=UGT1-06;
DE Short=UGT1.6;
DE EC=2.4.1.17 {ECO:0000269|PubMed:8068691};
DE AltName: Full=Phenol UDP-glucuronosyltransferase;
DE AltName: Full=UDP-glucuronosyltransferase 1A6;
DE Short=UGT1A6;
DE AltName: Full=UGP1A1;
DE AltName: Full=UGT1A7;
DE Flags: Precursor;
GN Name=Ugt1a6; Synonyms=Ugt1, Ugt1a6a, Ugt1a7;
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], AND CATALYTIC ACTIVITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=8068691; DOI=10.1021/bi00200a037;
RA Lamb J.G., Straub P., Tukey R.H.;
RT "Cloning and characterization of cDNAs encoding mouse Ugt1.6 and rabbit
RT UGT1.6: differential induction by 2,3,7,8-tetrachlorodibenzo-p-dioxin.";
RL Biochemistry 33:10513-10520(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA Reuter S.F., Vasiliou V., Puga A., Nebert D.W.;
RT "Characterization of the murine dioxin-inducible UDP
RT glucuronosyltransferase (Ugt1-06) gene.";
RL Toxicologist 14:410-410(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7677729; DOI=10.1007/bf00557949;
RA Koiwai O., Hasada K., Yasui Y., Sakai Y., Sato H., Watanabe T.;
RT "Isolation of cDNAs for mouse phenol and bilirubin UDP-
RT glucuronosyltransferases and mapping of the mouse gene for phenol UDP-
RT glucuronosyltransferase (Ugtla1) to chromosome 1 by restriction fragment
RT length variations.";
RL Biochem. Genet. 33:111-122(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Testis;
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: UDPGT is of major importance in the conjugation and
CC subsequent elimination of potentially toxic xenobiotics and endogenous
CC compounds. Conjugates small planar phenolic molecules such as 4-
CC nitrophenol, 1-naphthol, and 4-methylumbelliferone. The bulky phenol 4-
CC hydroxybiphenyl, androgens and estrogens are not substrates. 2-
CC hydroxybiphenyl is an excellent substrate.
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:8068691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000269|PubMed:8068691};
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 may be produced. Isoforms have a
CC different N-terminal domain and a common C-terminal domain of 245
CC residues.;
CC Name=1;
CC IsoId=Q64435-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney and at very low levels
CC in colon. {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; U09930; AAA51871.1; -; mRNA.
DR EMBL; U16818; AAA65979.1; -; mRNA.
DR EMBL; D87867; BAA13483.1; -; mRNA.
DR EMBL; AY227197; AAP48596.1; -; mRNA.
DR CCDS; CCDS48314.1; -. [Q64435-1]
DR PIR; A55788; A55788.
DR RefSeq; NP_659545.2; NM_145079.3. [Q64435-1]
DR AlphaFoldDB; Q64435; -.
DR SMR; Q64435; -.
DR STRING; 10090.ENSMUSP00000108759; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q64435; 2 sites.
DR iPTMnet; Q64435; -.
DR PhosphoSitePlus; Q64435; -.
DR SwissPalm; Q64435; -.
DR jPOST; Q64435; -.
DR MaxQB; Q64435; -.
DR PaxDb; Q64435; -.
DR PeptideAtlas; Q64435; -.
DR PRIDE; Q64435; -.
DR ProteomicsDB; 275376; -. [Q64435-1]
DR DNASU; 94284; -.
DR Ensembl; ENSMUST00000014263; ENSMUSP00000014263; ENSMUSG00000054545. [Q64435-1]
DR Ensembl; ENSMUST00000113134; ENSMUSP00000108759; ENSMUSG00000054545. [Q64435-1]
DR Ensembl; ENSMUST00000113135; ENSMUSP00000108760; ENSMUSG00000090124. [Q64435-1]
DR GeneID; 94284; -.
DR KEGG; mmu:94284; -.
DR UCSC; uc007bye.1; mouse. [Q64435-1]
DR CTD; 94284; -.
DR MGI; MGI:2137698; Ugt1a6a.
DR VEuPathDB; HostDB:ENSMUSG00000054545; -.
DR VEuPathDB; HostDB:ENSMUSG00000090124; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000163820; -.
DR HOGENOM; CLU_012949_3_0_1; -.
DR InParanoid; Q64435; -.
DR OMA; CHYFEEG; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q64435; -.
DR TreeFam; TF315472; -.
DR BRENDA; 2.4.1.17; 3474.
DR Reactome; R-MMU-156588; Glucuronidation.
DR Reactome; R-MMU-9749641; Aspirin ADME.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR BioGRID-ORCS; 94284; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Ugt1a6a; mouse.
DR PRO; PR:Q64435; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q64435; protein.
DR Bgee; ENSMUSG00000054545; Expressed in urinary bladder and 85 other tissues.
DR ExpressionAtlas; Q64435; baseline and differential.
DR Genevisible; Q64435; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0019899; F:enzyme binding; IBA:GO_Central.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:MGI.
DR GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR GO; GO:0019585; P:glucuronate metabolic process; IDA:MGI.
DR GO; GO:0001889; P:liver development; 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 Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Microsome; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..531
FT /note="UDP-glucuronosyltransferase 1-6"
FT /id="PRO_0000036017"
FT TRANSMEM 489..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 43
FT /note="K -> G (in Ref. 3; BAA13483)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="E -> R (in Ref. 3; BAA13483)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="T -> N (in Ref. 4; AAP48596)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="P -> L (in Ref. 4; AAP48596)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="S -> L (in Ref. 3; BAA13483)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="D -> G (in Ref. 4; AAP48596)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> P (in Ref. 3; BAA13483)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="I -> V (in Ref. 4; AAP48596)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="H -> K (in Ref. 2; AAA51871)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="G -> V (in Ref. 4; AAP48596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 60439 MW; AE7CA5FC5818DC12 CRC64;
MACLLPAAQT LPAGFLFLVL WASVLGDKLL VVPQDGSHWL SMKEIVEHLS ERGHDIMVLV
PEVNLLLGES KYYRRKIFSV TYSLEELQTR FRTFGNNHFL PGASLMGPLR EYRNNMIVVD
MFFSNCQSLL KDSATLSFLR ENKFDALFTD PAMPCGVILA EYLNLPSVYL FRGFPCSLEH
MLGQSPSPVS YVPRFYTKFS DHMTFPQRLA NFIVNILENY LYYCLYSKYE IIASDLLKRD
VSLPSLHQNS LWLLRYDFVF EYPRPVMPNM IFLGGINCKK KGKLTQEFEA YVNASGEHGI
VVFSLGSMVS EIPEKKAMEI AEALGRIPQT VLWRYTGTRP SNLAKNTILV KWLPQNDLLG
HPKTRAFITH SGSHGIYEGI CNGVPMVMMP LFGDQMDNAK RMETRGAGVT LNVLEMTADD
LENALKTVIN NKSYKENIMR LSSLHKDRPI EPLDLAVFWV EYVMRHKGAP HLRPAAHDLT
WYQYHSLDVI GFLLAIVLTV VFIVFKCCAY GCRKCFGGKG RVKKSHKSKT H
