ID   B3GL1_MUSSI             Reviewed;         331 AA.
AC   Q793U7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1;
DE            Short=Beta-1,3-GalNAc-T1;
DE            EC=2.4.1.79 {ECO:0000250|UniProtKB:O75752};
DE   AltName: Full=Beta-1,3-galactosyltransferase 3;
DE            Short=Beta-1,3-GalTase 3;
DE            Short=Beta3Gal-T3;
DE            Short=Beta3GalT3;
DE            Short=b3Gal-T3;
DE   AltName: Full=Beta-3-Gx-T3;
DE   AltName: Full=Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase;
DE   AltName: Full=Globoside synthase;
DE   AltName: Full=UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase;
GN   Name=B3galnt1; Synonyms=B3galt3, B3gt3;
OS   Mus spicilegus (Steppe mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ZBN;
RA   Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.;
RT   "Conspicuous differences among gene genealogies of 21 nuclear genes of five
RT   Mus musculus subspecies.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers N-acetylgalactosamine onto globotriaosylceramide.
CC       Plays a critical role in preimplantation stage embryonic development.
CC       {ECO:0000250|UniProtKB:O75752, ECO:0000250|UniProtKB:Q920V1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a globoside Gb3Cer (d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         galactosamine = a globoside Gb4Cer (d18:1(4E)) + H(+) + UDP;
CC         Xref=Rhea:RHEA:22252, ChEBI:CHEBI:15378, ChEBI:CHEBI:18259,
CC         ChEBI:CHEBI:18313, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.79;
CC         Evidence={ECO:0000250|UniProtKB:O75752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22253;
CC         Evidence={ECO:0000250|UniProtKB:O75752};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O75752};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:O75752}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:O75752}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
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DR   EMBL; AB039163; BAB68687.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q793U7; -.
DR   SMR; Q793U7; -.
DR   GlyCosmos; Q793U7; 5 sites, No reported glycans.
DR   Ensembl; ENSMSIT00000036623.1; ENSMSIP00000029052.1; ENSMSIG00000024414.1.
DR   GeneTree; ENSGT00940000162252; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000694415; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047273; F:galactosylgalactosylglucosylceramide beta-D-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IEA:Ensembl.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009312; P:oligosaccharide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF153; UDP-GALNAC:BETA-1,3-N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW   Magnesium; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..331
FT                   /note="UDP-GalNAc:beta-1,3-N-
FT                   acetylgalactosaminyltransferase 1"
FT                   /id="PRO_0000219155"
FT   TOPO_DOM        1..20
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..43
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        44..331
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  39371 MW;  387E8B0C75FC282D CRC64;
     MAPAVLTALP NRMSLRSLKW SLLLLSLLSF LVIWYLSLPH YNVIERVNWM YFYEYEPIYR
     QDFRFTLREH SNCSHQNPFL VILVTSRPSD VKARQAIRVT WGEKKSWWGY EVLTFFLLGQ
     QAEREDKTLA LSLEDEHVLY GDIIRQDFLD TYNNLTLKTI MAFRWVMEFC PNAKYIMKTD
     TDVFINTGNL VKYLLNLNHS EKFFTGYPLI DNYSYRGFFH KNHISYQEYP FKVFPPYCSG
     LGYIMSGDLV PRVYEMMSHV KPIKFEDVYV GICLNLLKVD IHIPEDTNLF FLYRIHLDVC
     QLRRVIAAHG FSSKEIITFW QVMLRNTTCH Y
//