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Database: UniProt/SWISS-PROT
Entry: B3GT1_MOUSE
LinkDB: B3GT1_MOUSE
Original site: 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   25-APR-2018, entry version 129.
DE   RecName: Full=Beta-1,3-galactosyltransferase 1;
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-12, FUNCTION, CATALYTIC
RP   ACTIVITY, COFACTOR, AND TISSUE SPECIFICITY.
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
RT   five Mus musculus subspecies.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose
CC       from UDP-alpha-D-galactose to substrates with a terminal beta-N-
CC       acetylglucosamine (beta-GlcNAc) residue. Involved in the
CC       biosynthesis of the carbohydrate moieties of glycolipids and
CC       glycoproteins. {ECO:0000269|PubMed:9417047}.
CC   -!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-beta-D-
CC       glucosaminyl-R = UDP + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC       glucosaminyl-R. {ECO:0000269|PubMed:9417047}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:9417047};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305};
CC       Single-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;
CC       Note=b3GalT1;
CC       URL="http://www.functionalglycomics.org/glycomics/search/jsp/landing.jsp?query=gt_mou_454";
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   UniGene; Mm.226435; -.
DR   UniGene; Mm.490783; -.
DR   ProteinModelPortal; O54904; -.
DR   SMR; O54904; -.
DR   STRING; 10090.ENSMUSP00000041343; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PhosphoSitePlus; O54904; -.
DR   PaxDb; O54904; -.
DR   PRIDE; O54904; -.
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   eggNOG; KOG2287; Eukaryota.
DR   eggNOG; ENOG410ZZ1B; LUCA.
DR   GeneTree; ENSGT00760000118879; -.
DR   HOGENOM; HOG000059604; -.
DR   HOVERGEN; HBG101354; -.
DR   InParanoid; O54904; -.
DR   KO; K07819; -.
DR   OMA; HPYQNSG; -.
DR   OrthoDB; EOG091G0AXM; -.
DR   PhylomeDB; O54904; -.
DR   TreeFam; TF318639; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:O54904; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000034780; -.
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:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IDA:MGI.
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   Complete proteome; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Manganese; Membrane; Polymorphism; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    326       Beta-1,3-galactosyltransferase 1.
FT                                /FTId=PRO_0000219146.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     26       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     27    326       Lumenal. {ECO:0000255}.
FT   CARBOHYD     47     47       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT      12     12       T -> S (in strain: 129/SvJ).
FT                                {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
//
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