UD3A1_XENLA
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 03-AUG-2022, entry version 61.
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 DNASU; 494747; -.
DR GeneID; 494747; -.
DR KEGG; xla:494747; -.
DR CTD; 494747; -.
DR Xenbase; XB-GENE-5824808; ugt3a2.L.
DR OrthoDB; 508327at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 494747; Expressed in ovary and 8 other tissues.
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..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