ID   UDB13_RABIT             Reviewed;         531 AA.
AC   P36512;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=UDP-glucuronosyltransferase 2B13;
DE            Short=UDPGT 2B13;
DE            EC=2.4.1.17;
DE   AltName: Full=EGT10;
DE   Flags: Precursor;
GN   Name=UGT2B13;
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].
RC   STRAIN=New Zealand white; TISSUE=Liver;
RX   PubMed=8325897; DOI=10.1016/s0021-9258(18)82464-4;
RA   Tukey R.H., Pendurthi U.R., Nguyen N.T., Green M.D., Tephly T.R.;
RT   "Cloning and characterization of rabbit liver UDP-glucuronosyltransferase
RT   cDNAs. Developmental and inducible expression of 4-hydroxybiphenyl
RT   UGT2B13.";
RL   J. Biol. Chem. 268:15260-15266(1993).
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 2B16 it is active toward
CC       octylgallate.
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}.
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DR   EMBL; L01081; AAA18020.1; -; mRNA.
DR   PIR; B47113; B47113.
DR   RefSeq; NP_001164485.1; NM_001171014.1.
DR   AlphaFoldDB; P36512; -.
DR   SMR; P36512; -.
DR   STRING; 9986.ENSOCUP00000021284; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GeneID; 100328586; -.
DR   KEGG; ocu:100328586; -.
DR   CTD; 100328586; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   InParanoid; P36512; -.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Microsome; Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT   CHAIN           25..531
FT                   /note="UDP-glucuronosyltransferase 2B13"
FT                   /id="PRO_0000036037"
FT   TRANSMEM        495..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   531 AA;  60552 MW;  961DA58AC4CB9932 CRC64;
     MPVKCISVLL LLLQLSCCFS SGSCGKVLVW PMEFSHWMNM KTILDALVQQ GHEVTVLRSS
     ASIVIGSNNE SGIKFETFHT SYRKDEIENF FMDWFYKMIY NVSIESYWET FSLTKMVILK
     YSDICEDICK EVILNKKLMT KLQESRFDVV LADPVSPGGE LLAELLKIPL VYSLRGFVGY
     MLQKHGGGLL LPPSYVPVMM SGLGSQMTFM ERVQNLLCVL YFDFWFPKFN EKRWDQFYSE
     VLGRPVTFLE LMGKADMWLI RSYWDLEFPR PLLPNFDFIG GLHCKPAKPL PQEMEDFVQS
     SGEEGVVVFS LGSMISNLTE ERANVIASAL AQLPQKVLWR FEGKKPDMLG SNTRLYKWIP
     QNDLLGHPKT KAFITHGGAN GVFEAIYHGI PMVGLPLFGD QLDNIVYMKA KGAAVKLNLK
     TMSSADLLNA LKTVINDPSY KENAMTLSRI HHDQPMKPLD RAVFWIEYVM RHKGAKHLRV
     AAHDLTWYQY HSLDVIGFLL ACVAITTYLI VKCCLLVYRY VLGAGKKKKR D