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Entry: O18009_CAEEL
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ID   O18009_CAEEL            Unreviewed;       535 AA.
AC   O18009;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=ugt-30 {ECO:0000313|EMBL:CAB03266.1,
GN   ECO:0000313|WormBase:T01G5.2};
GN   ORFNames=CELE_T01G5.2 {ECO:0000313|EMBL:CAB03266.1}, T01G5.2
GN   {ECO:0000313|WormBase:T01G5.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAB03266.1, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAB03266.1, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAB03266.1,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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|ARBA:ARBA00000301,
CC         ECO:0000256|RuleBase:RU362059};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167,
CC       ECO:0000256|RuleBase:RU362059}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167, ECO:0000256|RuleBase:RU362059}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009995, ECO:0000256|RuleBase:RU003718}.
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DR   EMBL; BX284605; CAB03266.1; -; Genomic_DNA.
DR   PIR; T24309; T24309.
DR   RefSeq; NP_506729.1; NM_074328.1.
DR   AlphaFoldDB; O18009; -.
DR   SMR; O18009; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   PaxDb; 6239-T01G5-2; -.
DR   PeptideAtlas; O18009; -.
DR   EnsemblMetazoa; T01G5.2.1; T01G5.2.1; WBGene00011340.
DR   GeneID; 187955; -.
DR   KEGG; cel:CELE_T01G5.2; -.
DR   UCSC; T01G5.2; c. elegans.
DR   AGR; WB:WBGene00011340; -.
DR   WormBase; T01G5.2; CE12976; WBGene00011340; ugt-30.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000170294; -.
DR   HOGENOM; CLU_012949_1_4_1; -.
DR   InParanoid; O18009; -.
DR   OMA; EILDVWW; -.
DR   OrthoDB; 382054at2759; -.
DR   PhylomeDB; O18009; -.
DR   Reactome; R-CEL-9753281; Paracetamol ADME.
DR   Reactome; R-CEL-9757110; Prednisone ADME.
DR   Reactome; R-CEL-9840309; Glycosphingolipid biosynthesis.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00011340; Expressed in adult organism and 1 other cell type or tissue.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
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:SF14; GLUCURONOSYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU003718}; Membrane {ECO:0000256|RuleBase:RU362059};
KW   Proteomics identification {ECO:0007829|EPD:O18009};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, 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   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           19..535
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5005142208"
FT   TRANSMEM        499..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   535 AA;  60811 MW;  F338B62BA63B5548 CRC64;
     MLYLQSIIFF CLLLYSNCLN ILVYAPAFAA SHSKFLGKLA DTLTERGHNV TYLMPVVNIA
     KRDECKGVKI TKDVVIVEAG EKMLSQKQAD TPNDEILDVW WTVQMDSSNS REIFQFFCSD
     MKIACENFLS RRDIFEDMKA RNFDLAILEP VSACGLGFVK ALGIEKTILA SSSVFYDVIL
     PYIGEPLDYS YVPSGYSVTG QELSLGEKFE NWMVSREISI ALEGLFDGEM EIYRRLLGHN
     LTNWRHLFPS ASIFFVNSNP FFDFPRPVLE KTVPIGGISV NMGVRKEDML TEEWEKVLNQ
     RPHTMLVSFG TLVMSTHMPK KWRSGLLEAF KSFPNVTFIW KYESDDHSFA NGIDNIYFSK
     WVPQNELLND NRLTAFLSHG GLGSIMELAF SGKPALIIPV FADQTRNANT LARHRGAICL
     HKSQMKNTEV LKKAFKSVLF DASFKNNSLK LAATLRNQPN KPKDTLIKYT EFVGEFGPFP
     QMDPYGRHLN VFQKSFIDIY TLIIVVSSIF VALIFNVIAK LIQYFIKSKS SEKND
//
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