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Database: UniProt
Entry: Q23323_CAEEL
LinkDB: Q23323_CAEEL
Original site: Q23323_CAEEL 
ID   Q23323_CAEEL            Unreviewed;       533 AA.
AC   Q23323;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=UDP-glucuronosyltransferase {ECO:0000256|RuleBase:RU362059};
DE            EC=2.4.1.17 {ECO:0000256|RuleBase:RU362059};
GN   Name=ugt-18 {ECO:0000313|EMBL:CAA99950.2,
GN   ECO:0000313|WormBase:ZC443.5};
GN   ORFNames=CELE_ZC443.5 {ECO:0000313|EMBL:CAA99950.2}, ZC443.5
GN   {ECO:0000313|WormBase:ZC443.5};
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:CAA99950.2, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAA99950.2, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA99950.2,
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; CAA99950.2; -; Genomic_DNA.
DR   PIR; T27578; T27578.
DR   RefSeq; NP_506209.2; NM_073808.4.
DR   AlphaFoldDB; Q23323; -.
DR   STRING; 6239.ZC443.5.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   EPD; Q23323; -.
DR   PaxDb; 6239-ZC443-5; -.
DR   PeptideAtlas; Q23323; -.
DR   EnsemblMetazoa; ZC443.5.1; ZC443.5.1; WBGene00013900.
DR   GeneID; 179759; -.
DR   KEGG; cel:CELE_ZC443.5; -.
DR   UCSC; ZC443.5; c. elegans.
DR   AGR; WB:WBGene00013900; -.
DR   WormBase; ZC443.5; CE30714; WBGene00013900; ugt-18.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00970000196118; -.
DR   HOGENOM; CLU_012949_1_1_1; -.
DR   InParanoid; Q23323; -.
DR   OMA; NIFTMQF; -.
DR   OrthoDB; 382054at2759; -.
DR   PhylomeDB; Q23323; -.
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; WBGene00013900; Expressed in larva and 3 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   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:SF55; UDP-GLUCURONOSYLTRANSFERASE; 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:Q23323,
KW   ECO:0007829|PeptideAtlas:Q23323};
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..17
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT   CHAIN           18..533
FT                   /note="UDP-glucuronosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
FT                   /id="PRO_5005142808"
FT   TRANSMEM        499..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362059"
SQ   SEQUENCE   533 AA;  61011 MW;  8F06AAEFA1635FB3 CRC64;
     MKFALILFFV LIHSTLTYKV LVFNPAYGAS HSNFLGKISD ILIDAGHNVT MLIPEYLITK
     KDFVGSKKVK DVVRIGRDER AGKLFEEEGI EHMGRARVWR MDPEMMSLVT IVGSMNLAIG
     YQCEYIFQQK DIIDRLRNEH FDLAITESLF ACPFALFDHI GIKNVINAES NLFKDAVKYA
     HGEPAAISYY PGLFSPHDDK MSFVARVKNM ITMLFTKYLY GSRYEKELEM IKPYYNGTET
     WEDLFTGVAF NLINSNQYID YPSPALPKTV FVGGMQVNTN EAKTKLSDEW NNILNIRKQN
     VLISFGSNAF SSEMPEEFKK SFLYVFGNMP EITFIWKYEE ANATLTSHLP NVKLTTWMPQ
     NDLLADDRLT LFVTHGGLGS TMELAYQGKP ALIIPLMADQ PRNAHMLKRH GGCLQYHKTM
     LGDSEQLLKA FKTVLTERKY SENAQRLARI LRDQPVSPKD LVLKHCEFAV EHGALNSLNS
     RGRYLNTFQF YSFDIASSIV MLALLVLVFI YFTLLFIFKL VARIFLSQKT KME
//
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