ID A0A821YU06_9NEOB Unreviewed; 221 AA. AC A0A821YU06; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 24-JAN-2024, entry version 9. DE RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059}; DE EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059}; GN ORFNames=RIMITATOR_LOCUS6008127 {ECO:0000313|EMBL:CAF4965124.1}; OS Ranitomeya imitator (mimic poison frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Neobatrachia; Hyloidea; Dendrobatidae; Dendrobatinae; OC Ranitomeya. OX NCBI_TaxID=111125 {ECO:0000313|EMBL:CAF4965124.1}; RN [1] {ECO:0000313|EMBL:CAF4965124.1} RP NUCLEOTIDE SEQUENCE. RA Stuckert A.; RL Submitted (FEB-2021) 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. {ECO:0000256|ARBA:ARBA00037451}. 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 Evidence={ECO:0000256|RuleBase:RU362059}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362059}; Single- CC pass membrane protein {ECO:0000256|RuleBase:RU362059}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CAF4965124.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CAJOBX010015765; CAF4965124.1; -; Genomic_DNA. DR AlphaFoldDB; A0A821YU06; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro. DR CDD; cd03784; GT1_Gtf-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. 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 3: Inferred from homology; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|RuleBase:RU003718}; Membrane {ECO:0000256|RuleBase:RU362059}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003718}; KW Transmembrane {ECO:0000256|RuleBase:RU362059}; KW Transmembrane helix {ECO:0000256|RuleBase:RU362059}. FT TRANSMEM 186..212 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU362059" SQ SEQUENCE 221 AA; 25397 MW; 2E79CF00EB6B24C3 CRC64; MISSLPILEF VKEMNDGFAK IRQKVIWRYK RSHWPKEVDV APNVRLVDWL SQNDLLGQPK VRLLVTHGGM NSLMEAVYHG VPVVGIPLFG DQYENLIRIK AKNMGTFIPP EEMEAESFAN SMREVIENSR YKTSAMKLSV ILRSRPFPPE RQLLGWVEHI LQSGGGGHLR PYSYQQPWYQ RHLLDVILFI STIVAAVVYL TVKVCTVLLS FLPPNRKQKL N //