ID   UDB16_RABIT             Reviewed;         523 AA.
AC   O19103;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   08-NOV-2023, entry version 102.
DE   RecName: Full=UDP-glucuronosyltransferase 2B16;
DE            Short=UDPGT 2B16;
DE            EC=2.4.1.17;
DE   Flags: Precursor; Fragment;
GN   Name=UGT2B16;
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].
RX   PubMed=9013565; DOI=10.1074/jbc.272.6.3272;
RA   Li Q., Lou X., Peyronneau M.-A., Straub P.O., Tukey R.H.;
RT   "Expression and functional domains of rabbit liver UDP-
RT   glucuronosyltransferase 2B16 and 2B13.";
RL   J. Biol. Chem. 272:3272-3279(1997).
CC   -!- FUNCTION: UDPGT is of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds. Acts on small phenolic agents such as 2-beta-naphthol and 4-
CC       methylumbelliferone as well as bulky phenolic compounds like 2-
CC       hydroxy- and 4-hydroxybiphenyl. In contrast to 2B13 it is active toward
CC       4-hydroxyesterone.
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 membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}. Endoplasmic reticulum membrane
CC       {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed primarily in adult rabbits.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U72742; AAB71494.1; -; mRNA.
DR   AlphaFoldDB; O19103; -.
DR   SMR; O19103; -.
DR   STRING; 9986.ENSOCUP00000025975; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; O19103; 1 site, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000025975; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; O19103; -.
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:SF12; UDP-GLUCURONOSYLTRANSFERASE 2B17-RELATED; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Microsome; Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          <1..16
FT   CHAIN           17..523
FT                   /note="UDP-glucuronosyltransferase 2B16"
FT                   /id="PRO_0000036040"
FT   TRANSMEM        487..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         129
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   523 AA;  60078 MW;  224088E7F68ED3DE CRC64;
     LLLLLQLSCC FSSGSCGKVL VWPMEFSHWM NMKTILDALV QRGHAVTVLR SSASILVNSN
     DESGITFETF PTTSTKDEME AFFMYWLNKL TNDVSKDALW EYFQTWQKFF MEYSDNYENI
     CKDLVLNKKI MAKLQESRFD VVLADPIAPC GELLAELLNR PLVYSVRFTP GYTYEKYSGG
     LLFPPSYVPV IMSDLSGQMT FMERVKNMLW MLYFDFWFQM LNVKRWDQFC SEVLGRPVTF
     SELVGKAEIW LIRSYWDLEF PRPLLPNSYF VGGLHCKPAQ PLPKEMEEFV QSSGEEGVVV
     FSLGSMISNL TEERANVIAS TLAQLPQKVL WKFDGKKPDN LGTNTQLYKW IPQNDLLGHT
     VSKAFITHGG ANGVFEAIYH GIPMVGLPLF ADQHDNLAHM RAKGAAIRLD WKTMSSSDFL
     NALKTVINDP SYKEKAMTLS RIHHDQPMKP LDQAIFWIEF VMRHKGAKHL RVAAHDLTWF
     QYHSLDVIGF LLACLTITTY LVIKCWLLVY QNILMTGKKK KRD
//