ID   UD16_RAT                Reviewed;         529 AA.
AC   P08430;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   27-MAR-2024, entry version 152.
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;
DE   AltName: Full=A1;
DE   AltName: Full=P-nitrophenol-specific UDPGT;
DE   AltName: Full=UDP-glucuronosyltransferase 1A6;
DE            Short=UGT1A6;
DE   Flags: Precursor;
GN   Name=Ugt1a6; 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   STRAIN=Wistar;
RX   PubMed=3096993; DOI=10.1016/s0021-9258(18)66758-4;
RA   Iyanagi T., Haniu M., Sogawa K., Fujii-Kuriyama Y., Watanabe S.,
RA   Shively J.E., Anan K.F.;
RT   "Cloning and characterization of cDNA encoding 3-methylcholanthrene
RT   inducible rat mRNA for UDP-glucuronosyltransferase.";
RL   J. Biol. Chem. 261:15607-15614(1986).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 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=P08430-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; J02612; AAA42311.1; -; mRNA.
DR   PIR; A24600; A24600.
DR   RefSeq; NP_001034780.1; NM_001039691.2.
DR   AlphaFoldDB; P08430; -.
DR   SMR; P08430; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; P08430; 3 sites, No reported glycans.
DR   GlyGen; P08430; 3 sites.
DR   iPTMnet; P08430; -.
DR   PhosphoSitePlus; P08430; -.
DR   PeptideAtlas; P08430; -.
DR   GeneID; 113992; -.
DR   KEGG; rno:113992; -.
DR   AGR; RGD:620949; -.
DR   CTD; 54578; -.
DR   RGD; 620949; Ugt1a6.
DR   InParanoid; P08430; -.
DR   OrthoDB; 382054at2759; -.
DR   BRENDA; 2.4.1.17; 5301.
DR   Reactome; R-RNO-156588; Glucuronidation.
DR   Reactome; R-RNO-9749641; Aspirin ADME.
DR   Reactome; R-RNO-9753281; Paracetamol ADME.
DR   PRO; PR:P08430; -.
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:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IDA:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0018880; P:4-chlorobiphenyl metabolic process; IDA:RGD.
DR   GO; GO:0052695; P:cellular glucuronidation; ISO:RGD.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:RGD.
DR   GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR   GO; GO:0001889; P:liver development; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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:SF157; UDP GLUCURONOSYLTRANSFERASE 1 FAMILY POLYPEPTIDE A3 PRECURSOR-RELATED; 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; Membrane; Microsome; Phosphoprotein;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..529
FT                   /note="UDP-glucuronosyltransferase 1-6"
FT                   /id="PRO_0000036019"
FT   TRANSMEM        487..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   529 AA;  60132 MW;  144AACD47EDDE04B CRC64;
     MACLLPAARL PAGFLFLVLW GSVLGDKLLV VPQDGSHWLS MKEIVEHLSE RGHDIVVLVP
     EVNLLLGESK YYRRKSFPVP YNLEELRTRY RSFGNNHFAA SSPLMAPLRE YRNNMIVIDM
     CFFSCQSLLK DSATLSFLRE NQFDALFTDP AMPCGVILAE YLKLPSIYLF RGFPCSLEHI
     GQSPSPVSYV PRFYTKFSDH MTFPQRLANF IANILENYLY HCLYSKYEIL ASDLLKRDVS
     LPALHQNSLW LLRYDFVFEY PRPVMPNMIF IGGTNCKKKG NLSQEFEAYV NASGEHGIVV
     FSLGSMVSEI PEKKAMEIAE ALGRIPQTLL WRYTGTRPSN LAKNTILVKW LPQNDLLGHP
     KARAFITHSG SHGIYEGICN GVPMVMMPLF GDQMDNAKRM ETRGAGVTLN VLEMTADDLE
     NALKTVINNK SYKENIMRLS SLHKDRPIEP LDLAVFWVEY VMRHKGAPHL RPAAHDLTWY
     QYHSLDVIGF LLAIVLTVVF IVYKSCAYGC RKCFGGKGRV KKSHKSKTH
//