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   25-MAY-2022, entry version 99.
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   GeneID; 100037718; -.
DR   KEGG; ocu:100037718; -.
DR   CTD; 100037718; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   OrthoDB; 508327at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
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_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