ID   C1GLT_XENLA             Reviewed;         360 AA.
AC   Q6GNL1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1;
DE            EC=2.4.1.122 {ECO:0000250|UniProtKB:Q9NS00};
DE   AltName: Full=Core 1 O-glycan 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   Name=c1galt1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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:0000250|UniProtKB:Q9NS00};
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   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC073496; AAH73496.1; -; mRNA.
DR   RefSeq; NP_001085899.1; NM_001092430.1.
DR   AlphaFoldDB; Q6GNL1; -.
DR   SMR; Q6GNL1; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   DNASU; 444326; -.
DR   GeneID; 444326; -.
DR   KEGG; xla:444326; -.
DR   CTD; 444326; -.
DR   Xenbase; XB-GENE-5871035; XB5871033.L.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 444326; Expressed in stomach and 7 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR   GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR   GO; GO:0016266; P:O-glycan processing; IEA:InterPro.
DR   InterPro; IPR026842; C1GALT1.
DR   InterPro; IPR003378; Fringe-like.
DR   PANTHER; PTHR23033:SF9; PTHR23033:SF9; 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..360
FT                   /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT                   galactosyltransferase 1"
FT                   /id="PRO_0000285070"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..360
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   360 AA;  41742 MW;  EB1D3D7DB6A7DC14 CRC64;
     MSIICAKVAW LPLTLGTAMG FLITFYLART LLERNSQPPL ALRSWNNMEL LPEVGMSHFH
     LPEDNSVSEE LSKKVRVLCW IMTGPTNLKT KAIHVKNSWT RHCNVALFMS SITDEDFPAI
     GLGTGEGRDK LYWKTIRAFH YAHKYYLNET EWFFKADDDT YVIMDNLRWM LSNYTADQPI
     YFGKRFKPYI KQGYMSGGAG YVLSREALIR FVEGFRTGVC KHTTSTEDVA IGNCMQLMGV
     IAGDSRDTEK RETFHPFPPE HHLTMKFSES KSFWYWSYCV YPIVEGPQCC SDLAISFHYI
     SPEDMYTLEY FIYHLRAHGY QYRYQPPLSD NADNLPVYIE NETVKPNRTI SDFLEPPMES