UGT50_CAEEL
ID UGT50_CAEEL Reviewed; 523 AA.
AC Q22295; O62371; Q8MPX8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative UDP-glucuronosyltransferase ugt-50;
DE Short=UDPGT 50;
DE EC=2.4.1.17;
DE Flags: Precursor;
GN Name=ugt-50; Synonyms=ugt16; ORFNames=T07C5.1;
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], AND ALTERNATIVE SPLICING.
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-84; ASN-248 AND ASN-283, AND
RP IDENTIFICATION BY MASS 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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=c;
CC IsoId=Q22295-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q22295-2; Sequence=VSP_021638, VSP_021639;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; Z50006; CAA90301.1; -; Genomic_DNA.
DR EMBL; Z50006; CAD44148.1; -; Genomic_DNA.
DR PIR; T24647; T24647.
DR PIR; T24652; T24652.
DR RefSeq; NP_510118.1; NM_077717.3.
DR RefSeq; NP_741913.1; NM_171786.5. [Q22295-1]
DR AlphaFoldDB; Q22295; -.
DR SMR; Q22295; -.
DR BioGRID; 46317; 1.
DR STRING; 6239.T07C5.1c; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR iPTMnet; Q22295; -.
DR EPD; Q22295; -.
DR PaxDb; Q22295; -.
DR PeptideAtlas; Q22295; -.
DR EnsemblMetazoa; T07C5.1b.1; T07C5.1b.1; WBGene00011564. [Q22295-2]
DR EnsemblMetazoa; T07C5.1b.2; T07C5.1b.2; WBGene00011564. [Q22295-2]
DR EnsemblMetazoa; T07C5.1c.1; T07C5.1c.1; WBGene00011564. [Q22295-1]
DR GeneID; 181413; -.
DR KEGG; cel:CELE_T07C5.1; -.
DR UCSC; T07C5.1b; c. elegans. [Q22295-1]
DR CTD; 181413; -.
DR WormBase; T07C5.1b; CE18217; WBGene00011564; ugt-50. [Q22295-2]
DR WormBase; T07C5.1c; CE31603; WBGene00011564; ugt-50. [Q22295-1]
DR eggNOG; KOG1192; Eukaryota.
DR HOGENOM; CLU_012949_1_3_1; -.
DR InParanoid; Q22295; -.
DR OMA; NERAFMP; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q22295; -.
DR Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR Reactome; R-CEL-9753281; Paracetamol ADME.
DR PRO; PR:Q22295; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00011564; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q22295; 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 Alternative splicing; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..523
FT /note="Putative UDP-glucuronosyltransferase ugt-50"
FT /id="PRO_0000036055"
FT TRANSMEM 490..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 182..190
FT /note="LPTLPSYVP -> KPMTTFAES (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_021638"
FT VAR_SEQ 191..523
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_021639"
SQ SEQUENCE 523 AA; 60286 MW; 6D00E382BFF26C4D CRC64;
MHYSQMRWMF FCLTALLHGS FIVNAAKILV YCPSISKSHV LLCSKYADLL HNAGHDTVLF
IPSYSKLLDN YDGAKHAKVW RLHNVTEAYD TKLGTLANVM ENSHIGFIDR LTFDADFWID
MCADLLGKLP EMQHIIDYKF DLVIYNEIDP CTPAIVRLFN IPKTVLLSSE AIMDKVAWNL
GLPTLPSYVP SVEENPNHDR MSFFERMSNV YKFFQSIVVH YLQDIHVLNL FRKEVSSDFP
SIAEIIRNVS LVLVNTDEIF DLPRSYSSKF VYVGMLEAGK DENVTLPKKQ DDYFKKGKSG
SVFVSFGTVT PFRSLPERIQ LSILNAIQKL PDYHFVVKTT ADDESSAQFF STVQNVDLVD
WVPQKAVLRH ANLKLFVSHG GMNSVLETMY YGVPMVIMPV FTDQFRNGRN VERRGAGKMV
LRETVVKETF FDAIHSVLEE KSYSSSVKRI SHLMKNKPFT SEERVTKWID FVLKYETSEH
FDLESNNLSI IEHNHLDLFF YLCIISLLNF VVYRKIFKRK SQS
