ID   UDB31_CANLF             Reviewed;         530 AA.
AC   Q6K1J1;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=UDP-glucuronosyltransferase 2B31;
DE            Short=UDPGT 2B31;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2B31;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=12694866; DOI=10.1016/s0006-2952(03)00064-9;
RA   Soars M.G., Fettes M., O'Sullivan A.C., Riley R.J., Ethell B.T.,
RA   Burchell B.;
RT   "Cloning and characterisation of the first drug-metabolising canine UDP-
RT   glucuronosyltransferase of the 2B subfamily.";
RL   Biochem. Pharmacol. 65:1251-1259(2003).
CC   -!- FUNCTION: UDPGTs are of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds. This isozyme has glucuronidating capacity on phenols,
CC       opioids, and carboxylic acid-containing drugs.
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   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY135176; AAN10154.1; -; mRNA.
DR   RefSeq; NP_001003381.1; NM_001003381.1.
DR   AlphaFoldDB; Q6K1J1; -.
DR   SMR; Q6K1J1; -.
DR   STRING; 9612.ENSCAFP00000021107; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; Q6K1J1; -.
DR   GeneID; 442984; -.
DR   CTD; 442984; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; Q6K1J1; -.
DR   OMA; WKFARTA; -.
DR   OrthoDB; 508327at2759; -.
DR   BRENDA; 2.4.1.17; 1153.
DR   SABIO-RK; Q6K1J1; -.
DR   Proteomes; UP000002254; 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   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Microsome; Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..530
FT                   /note="UDP-glucuronosyltransferase 2B31"
FT                   /id="PRO_0000036048"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         136
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   530 AA;  60706 MW;  50D8B26D1A962C2A CRC64;
     MSMKWISVLL GLQLSCYFSS GSCGKVLVWP TEYSHWINVK TILDELVQRG HEVTVLTSSA
     SILVDPNKLS AIKFEIYSAH LSRGDFEAFF IKLLNILIYD MPKDSFWTYF SLMQEFFWEF
     YECAQKLCKD VVLNKKLMTK LQESKFDLVL ADTIIPCGEL LAELLKIPLV YSLRFSPGYA
     FEKHSGGLPL PPSYVPVILS ELTDQMTFME RVKNMLYVLY FDFWFQTINE KSWDQFYSEV
     LGRPTTLYEL MRKADIWLIR TYWDFEYPHP LLPHFDFVGG LHCKPAKSLP TEMEEFVQSS
     GENGIVVFSL GSMVNNMTEE RANVIASALA QIPQKVLWRF DGKKPDTLGP NTRLYKWLPQ
     NDLLGHPKTK AFITHGGTNG IYEAIYHGIP MVGIPLFADQ ADNIVHMKAK GAAIRLDFST
     MSSADLLNAL RMVINDPSYK ENAMKLSGIH HDQPIKPLDR AVFWIEYVMR HQGAKHLRPA
     SHDLTWFQYH SLDVIGFLLA CVATAIFVTT QCCLFCCRKV AKTGKKIKKE