ID   UD2A3_CAVPO             Reviewed;         530 AA.
AC   Q9R110;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=UDP-glucuronosyltransferase 2A3;
DE            Short=UDPGT 2A3;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=UGT2A3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Hartley; TISSUE=Liver;
RX   PubMed=10479484; DOI=10.1006/mgme.1999.2892;
RA   Smith S.A., Nagalla S.R., Andrews D.P., Olsen G.D.;
RT   "Morphine regulation of a novel uridine diphosphate glucuronosyl-
RT   transferase in guinea pig pups following in utero exposure.";
RL   Mol. Genet. Metab. 68:68-77(1999).
CC   -!- FUNCTION: UDP-glucuronosyltransferases catalyze phase II
CC       biotransformation reactions in which lipophilic substrates are
CC       conjugated with glucuronic acid to increase water solubility and
CC       enhance excretion. They are of major importance in the conjugation and
CC       subsequent elimination of potentially toxic xenobiotics and endogenous
CC       compounds (By similarity). {ECO:0000250}.
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: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in liver and small
CC       intestine. {ECO:0000269|PubMed:10479484}.
CC   -!- INDUCTION: Up-regulated in kidney and liver following in utero morphine
CC       treatment. {ECO:0000269|PubMed:10479484}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AF175221; AAD51732.1; -; mRNA.
DR   RefSeq; NP_001166497.1; NM_001173026.1.
DR   AlphaFoldDB; Q9R110; -.
DR   SMR; Q9R110; -.
DR   STRING; 10141.ENSCPOP00000019647; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   Ensembl; ENSCPOT00000023420; ENSCPOP00000019647; ENSCPOG00000010848.
DR   GeneID; 100135631; -.
DR   KEGG; cpoc:100135631; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000162432; -.
DR   HOGENOM; CLU_012949_0_2_1; -.
DR   InParanoid; Q9R110; -.
DR   OMA; MVGVPIF; -.
DR   OrthoDB; 508327at2759; -.
DR   TreeFam; TF315472; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000010848; Expressed in liver.
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   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..530
FT                   /note="UDP-glucuronosyltransferase 2A3"
FT                   /id="PRO_0000299145"
FT   TOPO_DOM        24..494
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        516..530
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   530 AA;  59895 MW;  EE2F394D3FD484E1 CRC64;
     MAPGKLASAV LLLLLCCAGS GFCGKVLVWP CEMSHWLNLK TLLEELVKRG HEVTVLTLSN
     NLFIDYNRHP AFNFEVIPVP TDKNMSENIL NEFIELAVNV MPTMPLWQSG KLLQQFFVQI
     TEDLGLNCRN TVYNQSLMKK LRDSKYDVLV TDPVIPCGEL VAEMLGVPFV NMLKFSMGHT
     IEKYCGQLPA PPSYVPVPLG GLTTRMTFME RVKNMVFSVL FDFWIQQYDY KFWDQFYSEA
     LGRPTTLCEI MGKAEIWLIR TYWDFEFPRP YLPNFEFVGG LHCKPAKPLP KEMEEFVQSS
     GEDGVVVFSL GSMVKNLTEE KANLIASALA QIPQKVLWRY KGKKPATLGP NTRLFDWIPQ
     NDLLGHPKTK AFITHGGSNG IYEAIYHGVP MVGMPIFSDQ PDNLAGMKAK GAAVEVNMNT
     MTSADLLGAL RTVINDPTYK ENAMKLSRIH HDQPVKPLDR AAFWVEFVMH HKGAKHLRVA
     AHDLSWFQYH SLDVIGFLLA CVASAILLVT KCCLFSFQNF IKIGKRIKKE