B3GT1_MOUSE
ID B3GT1_MOUSE Reviewed; 326 AA.
AC O54904; Q91V52;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Beta-1,3-galactosyltransferase 1 {ECO:0000305};
DE Short=Beta-1,3-GalTase 1;
DE Short=Beta3Gal-T1;
DE Short=Beta3GalT1;
DE EC=2.4.1.86 {ECO:0000269|PubMed:9417047};
DE AltName: Full=UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase-I;
DE AltName: Full=UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1;
GN Name=B3galt1 {ECO:0000312|MGI:MGI:1349403};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-12, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=129/SvJ;
RX PubMed=9417047; DOI=10.1074/jbc.273.1.58;
RA Hennet T., Dinter A., Kuhnert P., Mattu T.S., Rudd P.M., Berger E.G.;
RT "Genomic cloning and expression of three murine UDP-galactose: beta-N-
RT acetylglucosamine beta1,3-galactosyltransferase genes.";
RL J. Biol. Chem. 273:58-65(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-316.
RC STRAIN=BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/EiJ, HMI/Msf, MSM/Msf,
RC NJL/Msf, Pgn2, and SWN/Msf;
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: Beta-1,3-galactosyltransferase that transfers galactose from
CC UDP-alpha-D-galactose to substrates with a terminal beta-N-
CC acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis
CC of the carbohydrate moieties of glycolipids and glycoproteins.
CC {ECO:0000269|PubMed:9417047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133506; EC=2.4.1.86;
CC Evidence={ECO:0000269|PubMed:9417047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53433;
CC Evidence={ECO:0000269|PubMed:9417047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC Cer(d18:1(4E)) + UDP-alpha-D-galactose = a beta-D-Gal-(1->3)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:16045, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17103, ChEBI:CHEBI:17292, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914; EC=2.4.1.86;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16046;
CC Evidence={ECO:0000250|UniProtKB:Q9Y5Z6};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9417047};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.3 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9417047};
CC KM=11.8 mM for GlcNAc-beta-pNP {ECO:0000269|PubMed:9417047};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9417047}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b3GalT1;
CC URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_454";
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DR EMBL; AF029790; AAC53523.1; -; Genomic_DNA.
DR EMBL; AB039134; BAB68658.1; -; Genomic_DNA.
DR EMBL; AB039135; BAB68659.1; -; Genomic_DNA.
DR EMBL; AB039136; BAB68660.1; -; Genomic_DNA.
DR EMBL; AB039137; BAB68661.1; -; Genomic_DNA.
DR EMBL; AB039138; BAB68662.1; -; Genomic_DNA.
DR EMBL; AB039139; BAB68663.1; -; Genomic_DNA.
DR EMBL; AB039140; BAB68664.1; -; Genomic_DNA.
DR EMBL; AB039141; BAB68665.1; -; Genomic_DNA.
DR EMBL; AB039142; BAB68666.1; -; Genomic_DNA.
DR CCDS; CCDS16083.1; -.
DR RefSeq; NP_064679.2; NM_020283.4.
DR RefSeq; XP_006499654.1; XM_006499591.3.
DR RefSeq; XP_011237873.1; XM_011239571.2.
DR RefSeq; XP_011237874.1; XM_011239572.2.
DR RefSeq; XP_011237875.1; XM_011239573.2.
DR RefSeq; XP_017174164.1; XM_017318675.1.
DR AlphaFoldDB; O54904; -.
DR SMR; O54904; -.
DR STRING; 10090.ENSMUSP00000107965; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; O54904; 2 sites.
DR PhosphoSitePlus; O54904; -.
DR PaxDb; O54904; -.
DR PRIDE; O54904; -.
DR ProteomicsDB; 265192; -.
DR Antibodypedia; 33791; 92 antibodies from 20 providers.
DR DNASU; 26877; -.
DR Ensembl; ENSMUST00000042456; ENSMUSP00000041343; ENSMUSG00000034780.
DR Ensembl; ENSMUST00000112346; ENSMUSP00000107965; ENSMUSG00000034780.
DR GeneID; 26877; -.
DR KEGG; mmu:26877; -.
DR UCSC; uc008jxm.3; mouse.
DR CTD; 8708; -.
DR MGI; MGI:1349403; B3galt1.
DR VEuPathDB; HostDB:ENSMUSG00000034780; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000156219; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; O54904; -.
DR OMA; CEKNAPF; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; O54904; -.
DR TreeFam; TF318639; -.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 26877; 0 hits in 76 CRISPR screens.
DR ChiTaRS; B3galt1; mouse.
DR PRO; PR:O54904; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O54904; protein.
DR Bgee; ENSMUSG00000034780; Expressed in cortical plate and 175 other tissues.
DR ExpressionAtlas; O54904; baseline and differential.
DR Genevisible; O54904; MM.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047275; F:glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:MGI.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; ISO:MGI.
DR GO; GO:0030259; P:lipid glycosylation; ISO:MGI.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Manganese; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Beta-1,3-galactosyltransferase 1"
FT /id="PRO_0000219146"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..326
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 12
FT /note="T -> S (in strain: 129/SvJ)"
FT /evidence="ECO:0000269|PubMed:9417047"
SQ SEQUENCE 326 AA; 37993 MW; 83271E99B2EE74F5 CRC64;
MASKVSCLYV LTVVCWASAL WYLSITRPTS SYTGSKPFSH LTVARKNFTF GNIRTRPINP
HSFEFLINEP NKCEKNIPFL VILISTTHKE FDARQAIRET WGDENNFKGI KIATLFLLGK
NADPVLNQMV EQESQIFHDI IVEDFIDSYH NLTLKTLMGM RWVATFCSKA KYVMKTDSDI
FVNMDNLIYK LLKPSTKPRR RYFTGYVING GPIRDVRSKW YMPRDLYPDS NYPPFCSGTG
YIFSADVAEL IYKTSLHTRL LHLEDVYVGL CLRKLGIHPF QNSGFNHWKM AYSLCRYRRV
ITVHQISPEE MHRIWNDMSS KKHLRC
