ID   UD3A1_XENLA             Reviewed;         523 AA.
AC   Q63ZR6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=UDP-glucuronosyltransferase 3A1;
DE            Short=UDPGT 3A1;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=ugt3a1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BC082844; AAH82844.1; -; mRNA.
DR   RefSeq; NP_001088053.1; NM_001094584.1.
DR   AlphaFoldDB; Q63ZR6; -.
DR   SMR; Q63ZR6; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; Q63ZR6; 1 site, No reported glycans.
DR   DNASU; 494747; -.
DR   GeneID; 494747; -.
DR   KEGG; xla:494747; -.
DR   AGR; Xenbase:XB-GENE-5824808; -.
DR   CTD; 494747; -.
DR   Xenbase; XB-GENE-5824808; ugt3a2.L.
DR   OrthoDB; 382054at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 494747; Expressed in ovary and 8 other cell types or tissues.
DR   GO; GO:0016020; C: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:SF24; UDP-GLUCURONOSYLTRANSFERASE 3A2; 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   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..523
FT                   /note="UDP-glucuronosyltransferase 3A1"
FT                   /id="PRO_0000299152"
FT   TOPO_DOM        24..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..523
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   523 AA;  60436 MW;  73B728B7D1CE5CA0 CRC64;
     MAVGRKSLIL SLLIQHFVLL HGAKILTVCF LGGSHYLWMD EISRILHNNG QEVTMFLQIA
     DGLLPDYQMQ ESPYRLITWS LDKNYLKEFS EFFRDSKYNF KDCDELSSYL GLMTHFSRQC
     KMIFNQTSIM NLLKEEKYDL AVIDSFNPCT FLVSEKLGIP FIATHPFPVK SPWHSGIPNQ
     LSYMPVYQSQ LTDHMDFFER VKNVFMYIAS AVLERKIYSL FDDVIEEHFP ACSRPSFEEL
     YKKTALWMYL TDFTIEFPHP FFPNVLYIGG VLAKPAKPVS EELEDFIAQS GEHGFIIVTF
     GSMVPSNPLT EFVKEMNDGF SKIPQKVIWR YRISEWPKVL QLAPNVKIMN WISQNDLLGH
     PKARLLVTHG GVNSIQEAIY HGVPMVAIPL FFDQFDNAVR IKAKHLGTFI PKDQLKAEKL
     ANAIRDVIGG ESYKNSAMHL SLIQRSQPFP KDQQIVRWVE HIVKVGGTDH LIPYSYQQPL
     YQQYLLDVFL FVCVCVIGAC YLTVKLLKMF IQKLCSFRKL KQN
//