ID   UGT48_CAEEL             Reviewed;         526 AA.
AC   Q18081;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 3.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Putative UDP-glucuronosyltransferase ugt-48;
DE            Short=UDPGT 48;
DE            EC=2.4.1.17;
DE   Flags: Precursor;
GN   Name=ugt-48; Synonyms=ugt15; ORFNames=C18C4.3;
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-58, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Bristol N2;
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).
RN   [3]
RP   INTERACTION WITH CMD-1.
RX   PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
RA   Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C., Liu R.;
RT   "Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
RL   Cell Calcium 43:444-456(2008).
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   -!- SUBUNIT: Interacts with cmd-1 in the presence of Ca(2+).
CC       {ECO:0000269|PubMed:17854888}.
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; FO080608; CCD65106.1; -; Genomic_DNA.
DR   RefSeq; NP_504464.2; NM_072063.5.
DR   AlphaFoldDB; Q18081; -.
DR   SMR; Q18081; -.
DR   BioGRID; 43989; 3.
DR   STRING; 6239.C18C4.3.1; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   iPTMnet; Q18081; -.
DR   EPD; Q18081; -.
DR   PaxDb; Q18081; -.
DR   PeptideAtlas; Q18081; -.
DR   EnsemblMetazoa; C18C4.3.1; C18C4.3.1; WBGene00015965.
DR   GeneID; 178940; -.
DR   KEGG; cel:CELE_C18C4.3; -.
DR   UCSC; C18C4.3.1; c. elegans.
DR   CTD; 178940; -.
DR   WormBase; C18C4.3; CE38487; WBGene00015965; ugt-48.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00970000196182; -.
DR   HOGENOM; CLU_012949_1_3_1; -.
DR   InParanoid; Q18081; -.
DR   OMA; ASKSHMI; -.
DR   OrthoDB; 508327at2759; -.
DR   PhylomeDB; Q18081; -.
DR   Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-CEL-9753281; Paracetamol ADME.
DR   PRO; PR:Q18081; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00015965; Expressed in larva and 3 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; 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   Calmodulin-binding; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..526
FT                   /note="Putative UDP-glucuronosyltransferase ugt-48"
FT                   /id="PRO_0000036054"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761667"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   526 AA;  59627 MW;  C291099EE08F9FB5 CRC64;
     MLLRILTFLA VCQVTTSHKI LMFSPTASKS HMISQGRIAD ELANAGHEVV NFEPDFLNLT
     DKFVPCKKCR RWPVTGLNNY KFKKIQNGLS GDVFQQSSIW SKIFNTDSDP YQDEYTNMCE
     EMVTNKELIE KLKKEKFDAY FGEQIHLCGM GLAHLIGIKH RFWIASCTMS VSMRDSLGIP
     TPSSLIPFMS TLDATPAPFW QRAKNFVLQM AHIRDEYRDV VLTNDMFKKN FGSDFPCVEF
     LAKTSDLIFV STDELLEIQA PTLSNVVHIG GLGLSSEGGG LDEKFVKIME KGKGVILFSL
     GTIANTTNLP PTIMENLMKI TQKFKDYEFI IKVDKFDRRS FDLAEGLSNV LVVDWVPQTA
     VLAHPRLKAF ITHAGYNSLM ESAYAGVPVI LIPFMFDQPR NGRSVERKGW GILRDRFQLI
     KDPDAIEGAI KEILVNPTYQ EKANRLKKLM RSKPQSASER LVKMTNWVLE NDGVEELQYE
     GKHMDFFTFY NLDIIITAAS IPVLIFIVLR ISNISIITSS PKNKKD