C1GLT_CAEEL
ID C1GLT_CAEEL Reviewed; 389 AA.
AC Q18515; Q9GQC5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1;
DE EC=2.4.1.122 {ECO:0000269|PubMed:16762980};
DE AltName: Full=Core 1 O-glycan T-synthase;
DE Short=Ce-T-synthase;
DE AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 1;
DE Short=C1GalT1;
DE Short=Core 1 beta3-Gal-T1;
GN ORFNames=C38H2.2;
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 [MRNA].
RX PubMed=11677243; DOI=10.1074/jbc.m109060200;
RA Ju T., Brewer K., D'Souza A., Cummings R.D., Canfield W.M.;
RT "Cloning and expression of human core 1 beta1,3-galactosyltransferase.";
RL J. Biol. Chem. 277:178-186(2002).
RN [2]
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 [3]
RP FUNCTION, ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=16762980; DOI=10.1093/glycob/cwl008;
RA Ju T., Zheng Q., Cummings R.D.;
RT "Identification of core 1 O-glycan T-synthase from Caenorhabditis
RT elegans.";
RL Glycobiology 16:947-958(2006).
CC -!- FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-
CC beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many
CC extended O-glycans in glycoproteins. {ECO:0000269|PubMed:16762980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000269|PubMed:16762980};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed throughout development.
CC Present in all cells. {ECO:0000269|PubMed:16762980}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF269063; AAG36940.1; -; mRNA.
DR EMBL; Z35641; CAA84707.2; -; Genomic_DNA.
DR PIR; T19837; T19837.
DR RefSeq; NP_499293.2; NM_066892.8.
DR AlphaFoldDB; Q18515; -.
DR SMR; Q18515; -.
DR BioGRID; 41648; 4.
DR STRING; 6239.C38H2.2; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR EPD; Q18515; -.
DR PaxDb; Q18515; -.
DR PeptideAtlas; Q18515; -.
DR EnsemblMetazoa; C38H2.2.1; C38H2.2.1; WBGene00008019.
DR GeneID; 176455; -.
DR KEGG; cel:CELE_C38H2.2; -.
DR UCSC; C38H2.2; c. elegans.
DR CTD; 176455; -.
DR WormBase; C38H2.2; CE32602; WBGene00008019; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000155000; -.
DR HOGENOM; CLU_035857_0_0_1; -.
DR InParanoid; Q18515; -.
DR OMA; PYGIINT; -.
DR OrthoDB; 1407357at2759; -.
DR PhylomeDB; Q18515; -.
DR BRENDA; 2.4.1.122; 1045.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q18515; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00008019; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016267; P:O-glycan processing, core 1; IBA:GO_Central.
DR InterPro; IPR026842; C1GALT1.
DR InterPro; IPR003378; Fringe-like.
DR PANTHER; PTHR23033:SF13; PTHR23033:SF13; 1.
DR Pfam; PF02434; Fringe; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..389
FT /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT galactosyltransferase 1"
FT /id="PRO_0000285071"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..389
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 389 AA; 44123 MW; 7CF57B7415877C98 CRC64;
MANWPRVSPL AYVALGVLLG LTISIISQTG TTTYDAASRI AILRANRGDP QVDEHDHAHG
NDPHGDEEVD DHHANFAPVQ FHSNNSSHSH DGESLIADEV AKKVRVFCWI LTGKQNHDKR
AKHVKATWAK RCNKYVFMSS EEDAELPAIN LNVSEGRDYL WAKTKGAFKY IYDHHLNDYD
WFLKADDDTY VVMENLRFML LAHSPDEPIH FGCKFKPFTQ GGYHSGGAGY VLSREALKKF
IEVALPDKSL CSQNHGGAED AEMGKCLEKV GVKAGDSRDA DGHHRFMPFV PEHHLSPGHV
DPKFWFWQYT YYPMDQGPTC CSDYAVSFHY VNPNLMYVLE YLIYHLKPFG IDRAIRVPKN
ETIIHTAYSI SRSERGQDDA FRDRPEVAV
