ID   UGT47_CAEEL             Reviewed;         536 AA.
AC   Q21706;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Putative UDP-glucuronosyltransferase ugt-47;
DE            Short=UDPGT 47;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=ugt-47; ORFNames=R04B5.9;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|EMBL:CAA94845.2}
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] {ECO:0000305}
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2 {ECO:0000269|PubMed:17761667};
RX   PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA   Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA   Taoka M., Takahashi N., Isobe T.;
RT   "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT   elegans and suggests an atypical translocation mechanism for integral
RT   membrane proteins.";
RL   Mol. Cell. Proteomics 6:2100-2109(2007).
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:0000250|UniProtKB:Q9BY64};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000255}.
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DR   EMBL; Z70782; CAA94845.2; -; Genomic_DNA.
DR   PIR; T23893; T23893.
DR   RefSeq; NP_505595.2; NM_073194.4.
DR   AlphaFoldDB; Q21706; -.
DR   SMR; Q21706; -.
DR   STRING; 6239.R04B5.9; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q21706; -.
DR   EPD; Q21706; -.
DR   PaxDb; Q21706; -.
DR   PeptideAtlas; Q21706; -.
DR   EnsemblMetazoa; R04B5.9.1; R04B5.9.1; WBGene00011006.
DR   GeneID; 187570; -.
DR   KEGG; cel:CELE_R04B5.9; -.
DR   UCSC; R04B5.9; c. elegans.
DR   CTD; 187570; -.
DR   WormBase; R04B5.9; CE37984; WBGene00011006; ugt-47.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00970000196182; -.
DR   HOGENOM; CLU_012949_1_3_1; -.
DR   InParanoid; Q21706; -.
DR   OMA; WKFESDE; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q21706; -.
DR   Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-CEL-9753281; Paracetamol ADME.
DR   PRO; PR:Q21706; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00011006; Expressed in adult organism and 1 other tissue.
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   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..536
FT                   /note="Putative UDP-glucuronosyltransferase ugt-47"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000396643"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   536 AA;  61449 MW;  F83E5FCD6A3690EE CRC64;
     MFRYHSILLL AILYFFEYGL AYKILVFSPA TSKSHLISNG RIADELAKAG HNVTLLEIDF
     LGIVDSTKSA KLVKKTIVRV PKKMQGFKNV IQSFSEGVME DEGLFELLKG NIAYQTVYND
     LCEEFLENEV MFNKLKDENF DAFFAEQLNI CGFGYAKALG IQRKFLISSC PFFSHVYDYT
     SHPAPYASVP FISDMSPEPT YLERTNNLLR GITINTFFYF SHNRLTSIFR KKFGDDFPAI
     TEIVRNVDII FLATDEIIDF SSPTLPNLVH VGGLGVDDDT TEMGPVFEAE MKKGDKGVIY
     FSLGTIANTS TIDKKVMESF LEIVKKFPDY HFLIRADKND KNTKDKATEI SNVFVSDWLP
     QPAILHHPRL RTFITHAGYN GLMEAALAGV PLITIPFMFD QNLNSRAIEK KGWGIRRDKK
     QFLTEPNAIE EAIREMLTNP SYTKQAHRVR DLMRNKPMGA RDRFIKTTEW VIQNGGVHEL
     LTEGRDLSII KYYNLDIIVP CFFVAFYFII FPFFKLFGGF YYYSCFGHIE SKYKKD