ID   UGT46_CAEEL             Reviewed;         531 AA.
AC   Q10941;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Putative UDP-glucuronosyltransferase ugt-46;
DE            Short=UDPGT 46;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=ugt-46; Synonyms=ugt14; ORFNames=B0310.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-304, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA   Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT   "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT   elegans.";
RL   Glycobiology 15:952-964(2005).
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 membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FO080169; CCD61751.1; -; Genomic_DNA.
DR   PIR; T15329; T15329.
DR   RefSeq; NP_508112.1; NM_075711.5.
DR   AlphaFoldDB; Q10941; -.
DR   SMR; Q10941; -.
DR   BioGRID; 45357; 2.
DR   DIP; DIP-26251N; -.
DR   IntAct; Q10941; 2.
DR   STRING; 6239.B0310.5; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q10941; -.
DR   EPD; Q10941; -.
DR   PaxDb; Q10941; -.
DR   PeptideAtlas; Q10941; -.
DR   PRIDE; Q10941; -.
DR   EnsemblMetazoa; B0310.5a.1; B0310.5a.1; WBGene00015141.
DR   GeneID; 180404; -.
DR   KEGG; cel:CELE_B0310.5; -.
DR   UCSC; B0310.5; c. elegans.
DR   CTD; 180404; -.
DR   WormBase; B0310.5a; CE03878; WBGene00015141; ugt-46.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00970000196182; -.
DR   HOGENOM; CLU_012949_1_3_1; -.
DR   InParanoid; Q10941; -.
DR   OMA; IPTIFGW; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q10941; -.
DR   Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-CEL-9753281; Paracetamol ADME.
DR   PRO; PR:Q10941; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00015141; Expressed in larva and 4 other tissues.
DR   ExpressionAtlas; Q10941; baseline and differential.
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   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..531
FT                   /note="Putative UDP-glucuronosyltransferase ugt-46"
FT                   /id="PRO_0000036053"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:15888633"
SQ   SEQUENCE   531 AA;  60204 MW;  1C498A4385E272C4 CRC64;
     MRLIFVLLAT FVNAAFSYKI LVFSPATSKS HLISNGRLAD ELARAGHDVT VLELDFLGIS
     QTTNSVKVAK KRIIDGFQES TNFKNVLHGF SETVMEEPSF TDEIKGWWAY QNVYNDLCAE
     FLKMDDIFNE LKNAKFDGFF AEQINLCGFG YAHALEIPRH FLISSCPFAA PVYDFTGLPM
     PTSTVAFAAD LSISPTYTER ARNLFVAVLT KLEFTLLNNR LQAHFQHKFG EHFPSLYSVT
     SDVDVIFVAT DEIIDISTTT LQNIVHVGGL GVDDDVAEMD NVFASEMSKG KEGVIYFSLG
     TIANTTKIDS KVMRTVLDIV KKFPDYHFVI RADKYDLSTR EYAKSVSNAF VSDWLPQPAI
     LHHPRLKLFI THSGYNSIVE AARAGVPLIN IPFMFDQNLN SRAVEKKGWG IRRHKKQLLT
     EPEEIEKAIS EIIHNKKYSL KAQRIRDLIK SKPLSSSQLL IKTTEWAIKN HGLDEIKFES
     RGQTTWTYYN LDVIIPVFWL SISLVIPTIF GWYKFSCFGH VEEKKGKSKR D