UD16_RAT
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 03-AUG-2022, entry version 146.
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 GlyGen; P08430; 3 sites.
DR iPTMnet; P08430; -.
DR PhosphoSitePlus; P08430; -.
DR PeptideAtlas; P08430; -.
DR PRIDE; P08430; -.
DR GeneID; 113992; -.
DR KEGG; rno:113992; -.
DR CTD; 54578; -.
DR RGD; 620949; Ugt1a6.
DR InParanoid; P08430; -.
DR OrthoDB; 508327at2759; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
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 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; 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
