ID UD16_RABIT Reviewed; 531 AA.
AC Q28611;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=UGT1A6;
DE Flags: Precursor;
GN Name=UGT1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=New Zealand white; 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).
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 -!- 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 may have a
CC different N-terminal domain and a common C-terminal domain of 245
CC residues.;
CC Name=1;
CC IsoId=Q28611-1; Sequence=Displayed;
CC -!- INDUCTION: By dioxin.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U09030; AAA51867.1; -; mRNA.
DR PIR; B55788; B55788.
DR RefSeq; NP_001082788.1; NM_001089319.1. [Q28611-1]
DR AlphaFoldDB; Q28611; -.
DR SMR; Q28611; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyCosmos; Q28611; 1 site, No reported glycans.
DR GeneID; 100037718; -.
DR KEGG; ocu:100037718; -.
DR CTD; 100037718; -.
DR eggNOG; KOG1192; Eukaryota.
DR InParanoid; Q28611; -.
DR OrthoDB; 382054at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
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; 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_0000036018"
FT TRANSMEM 489..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 531 AA; 60099 MW; 872D317852F0928F CRC64;
MACLLSAAQR ASAGVLFVAL WGTVLGDRLL VVPQDGSHWL SMQDIVEALG ARGHEIVVLV
PEVNLLLRES RFYTRRIYPV PFDQEEQSYR YRTFGEKHFT DRSWLSGPQT EYRNNMVVID
MYFINCQSLL RHGDTLDFLR AGKFDALFTD PALPCGVILA EYLGLPSVYL FRGFPCSLEH
GFGGSPNPVS YIPRCYTKFS DQMSFPQRVV NFLVNLLEVP LFYCLYSKYE DLAVELLKRE
VDLPTLFQKD PVWLLRYDFV FEYPRPVMPN MVLIGGINCK KPDVLSQEFE AYVNASGEHG
IVVFSLGSMV SEIPEKKAME IADALGKIPQ TVLWRYTGSR PSNLAKNTYL VKWLPQNVLL
GHPKTRAFIT HSGSHGIYEG ICNGVPMVML PLFGDQMDNA KRIETRGAGV TLNVLEMTSD
DLANALKTVI NDKSYKENIM RLSSLHKDRP VEPLDLAVFW VEFVMRHKGA APRPAAHDLT
WYQYHSLDVI GFLLAIVLTV AFVTFKCCAF AWGKCFGKKG RVKKAHKSKV H
//
