B4GT1_MOUSE
ID B4GT1_MOUSE Reviewed; 399 AA.
AC P15535;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Beta-1,4-galactosyltransferase 1 {ECO:0000305};
DE Short=Beta-1,4-GalTase 1;
DE Short=Beta4Gal-T1;
DE Short=b4Gal-T1;
DE EC=2.4.1.-;
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
DE EC=2.4.1.38;
DE AltName: Full=Lactose synthase A protein;
DE EC=2.4.1.22;
DE AltName: Full=N-acetyllactosamine synthase;
DE EC=2.4.1.90;
DE AltName: Full=Nal synthase;
DE AltName: Full=Neolactotriaosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.275 {ECO:0000250|UniProtKB:P08037};
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1;
DE Contains:
DE RecName: Full=Processed beta-1,4-galactosyltransferase 1 {ECO:0000305};
GN Name=B4galt1 {ECO:0000312|MGI:MGI:95705}; Synonyms=Ggtb, Ggtb2;
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 [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=3134348; DOI=10.1016/s0021-9258(19)81533-8;
RA Shaper N.L., Hollis G.F., Douglas J.G., Kirsch I.R., Shaper J.H.;
RT "Characterization of the full length cDNA for murine beta-1,4-
RT galactosyltransferase. Novel features at the 5'-end predict two
RT translational start sites at two in-frame AUGs.";
RL J. Biol. Chem. 263:10420-10428(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1689054; DOI=10.1073/pnas.87.2.791;
RA Shaper N.L., Wright W.W., Sharper J.H.;
RT "Murine beta 1,4-galactosyltransferase: both the amounts and structure of
RT the mRNA are regulated during spermatogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:791-795(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2504153; DOI=10.1016/0006-291x(89)90782-1;
RA Hollis G.F., Douglas J.G., Shaper N.L., Shaper J.H., Stafford-Hollis J.M.,
RA Evans R.J., Kirsch I.R.;
RT "Genomic structure of murine beta-1,4-galactosyltransferase.";
RL Biochem. Biophys. Res. Commun. 162:1069-1075(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3141392; DOI=10.1093/oxfordjournals.jbchem.a122434;
RA Nakazawa K., Ando T., Kimura T., Narimatsu H.;
RT "Cloning and sequencing of a full-length cDNA of mouse N-acetylglucosamine
RT (beta 1-4)galactosyltransferase.";
RL J. Biochem. 104:165-168(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-63, AND SUBCELLULAR LOCATION (ISOFORM SHORT).
RX PubMed=3149531; DOI=10.1016/0300-9084(88)90303-3;
RA Shaper J.H., Hollis G.F., Shaper N.L.;
RT "Evidence for two forms of murine beta-1,4-galactosyltransferase based on
RT cloning studies.";
RL Biochimie 70:1683-1688(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 1-20.
RC STRAIN=BALB/cJ;
RX PubMed=1384819; DOI=10.1093/glycob/2.4.361;
RA Harduin-Lepers A., Shaper N.L., Mahoney J.A., Shaper J.H.;
RT "Murine beta 1,4-galactosyltransferase: round spermatid transcripts are
RT characterized by an extended 5'-untranslated region.";
RL Glycobiology 2:361-368(1992).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-20.
RC STRAIN=BALB/cJ;
RX PubMed=8314795; DOI=10.1016/s0021-9258(19)85247-x;
RA Harduin-Lepers A., Shaper J.H., Shaper N.L.;
RT "Characterization of two cis-regulatory regions in the murine beta 1,4-
RT galactosyltransferase gene. Evidence for a negative regulatory element that
RT controls initiation at the proximal site.";
RL J. Biol. Chem. 268:14348-14359(1993).
RN [9]
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11145975; DOI=10.1046/j.1471-4159.2001.00004.x;
RA Nakamura N., Yamakawa N., Sato T., Tojo H., Tachi C., Furukawa K.;
RT "Differential gene expression of beta-1,4-galactosyltransferases I, II and
RT V during mouse brain development.";
RL J. Neurochem. 76:29-38(2001).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2Q1.
RX PubMed=18511602; DOI=10.1634/stemcells.2007-1080;
RA Wassler M.J., Shur B.D., Zhou W., Geng Y.J.;
RT "Characterization of a novel ubiquitin-conjugating enzyme that regulates
RT beta1,4-galactosyltransferase-1 in embryonic stem cells.";
RL Stem Cells 26:2006-2018(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form
CC catalyzes the production of lactose in the lactating mammary gland and
CC could also be responsible for the synthesis of complex-type N-linked
CC oligosaccharides in many glycoproteins as well as the carbohydrate
CC moieties of glycolipids. {ECO:0000250|UniProtKB:P08037}.
CC -!- FUNCTION: [Processed beta-1,4-galactosyltransferase 1]: The cell
CC surface form functions as a recognition molecule during a variety of
CC cell to cell and cell to matrix interactions, as those occurring during
CC development and egg fertilization, by binding to specific
CC oligosaccharide ligands on opposing cells or in the extracellular
CC matrix. The secreted form is responsible for the synthesis of complex-
CC type to N-linked oligosaccharides in many glycoproteins as well as the
CC carbohydrate moieties of glycolipids. {ECO:0000250|UniProtKB:P08037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP;
CC Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133507; EC=2.4.1.38;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC EC=2.4.1.90; Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000250|UniProtKB:P08037};
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 neolactoside
CC nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP;
CC Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-
CC galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H(+) +
CC UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P15291};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form
CC lactose synthase (By similarity). Interacts (via N-terminal cytoplasmic
CC domain) with UBE2Q1 (via N-terminus); the interaction is direct
CC (PubMed:18511602). {ECO:0000250|UniProtKB:P15291,
CC ECO:0000269|PubMed:18511602}.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Golgi apparatus, Golgi stack
CC membrane {ECO:0000269|PubMed:18511602}; Single-pass type II membrane
CC protein. Cell membrane; Single-pass type II membrane protein. Cell
CC surface. Cell projection, filopodium {ECO:0000269|PubMed:18511602}.
CC Note=Found in trans cisternae of Golgi. B4GALT1 cell surface expression
CC is regulated by UBE2Q1 (PubMed:18511602).
CC {ECO:0000269|PubMed:18511602}.
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Golgi apparatus, Golgi stack
CC membrane {ECO:0000269|PubMed:3149531}; Single-pass type II membrane
CC protein {ECO:0000269|PubMed:3149531}. Note=Found in trans cisternae of
CC Golgi. {ECO:0000269|PubMed:3149531}.
CC -!- SUBCELLULAR LOCATION: [Processed beta-1,4-galactosyltransferase 1]:
CC Secreted {ECO:0000250|UniProtKB:P15291}. Note=Soluble form found in
CC body fluids. {ECO:0000250|UniProtKB:P15291}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long; Synonyms=Cell surface;
CC IsoId=P15535-1; Sequence=Displayed;
CC Name=Short; Synonyms=Golgi complex;
CC IsoId=P15535-2; Sequence=VSP_018803;
CC -!- DEVELOPMENTAL STAGE: In the brain, highest levels of expression are
CC found at 11.5 dpc with decreased expression thereafter.
CC {ECO:0000269|PubMed:11145975}.
CC -!- PTM: The soluble form derives from the membrane forms by proteolytic
CC processing.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b4GalT1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_460";
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DR EMBL; J03880; AAA37297.1; -; mRNA.
DR EMBL; D00314; BAA00216.1; -; mRNA.
DR EMBL; M27922; AAA58745.1; -; Genomic_DNA.
DR EMBL; M27917; AAA58745.1; JOINED; Genomic_DNA.
DR EMBL; M27918; AAA58745.1; JOINED; Genomic_DNA.
DR EMBL; M27919; AAA58745.1; JOINED; Genomic_DNA.
DR EMBL; M27920; AAA58745.1; JOINED; Genomic_DNA.
DR EMBL; M27921; AAA58745.1; JOINED; Genomic_DNA.
DR EMBL; M27922; AAA58744.1; -; Genomic_DNA.
DR EMBL; M27917; AAA58744.1; JOINED; Genomic_DNA.
DR EMBL; M27918; AAA58744.1; JOINED; Genomic_DNA.
DR EMBL; M27919; AAA58744.1; JOINED; Genomic_DNA.
DR EMBL; M27920; AAA58744.1; JOINED; Genomic_DNA.
DR EMBL; M27921; AAA58744.1; JOINED; Genomic_DNA.
DR EMBL; BC053006; AAH53006.1; -; mRNA.
DR EMBL; M36289; AAA37294.1; -; mRNA.
DR EMBL; L16840; AAA62340.1; -; mRNA.
DR CCDS; CCDS18051.1; -. [P15535-1]
DR PIR; A33396; A33396.
DR RefSeq; NP_071641.1; NM_022305.4. [P15535-1]
DR AlphaFoldDB; P15535; -.
DR SMR; P15535; -.
DR BioGRID; 199912; 13.
DR IntAct; P15535; 11.
DR STRING; 10090.ENSMUSP00000030121; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; P15535; 1 site.
DR PhosphoSitePlus; P15535; -.
DR SwissPalm; P15535; -.
DR CPTAC; non-CPTAC-3561; -.
DR EPD; P15535; -.
DR MaxQB; P15535; -.
DR PaxDb; P15535; -.
DR PeptideAtlas; P15535; -.
DR PRIDE; P15535; -.
DR ProteomicsDB; 273458; -. [P15535-1]
DR ProteomicsDB; 273459; -. [P15535-2]
DR Antibodypedia; 2256; 181 antibodies from 27 providers.
DR DNASU; 14595; -.
DR Ensembl; ENSMUST00000030121; ENSMUSP00000030121; ENSMUSG00000028413. [P15535-1]
DR GeneID; 14595; -.
DR KEGG; mmu:14595; -.
DR UCSC; uc008shw.2; mouse. [P15535-1]
DR CTD; 2683; -.
DR MGI; MGI:95705; B4galt1.
DR VEuPathDB; HostDB:ENSMUSG00000028413; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000155244; -.
DR HOGENOM; CLU_044391_0_0_1; -.
DR InParanoid; P15535; -.
DR OMA; VTVFFYV; -.
DR PhylomeDB; P15535; -.
DR TreeFam; TF312834; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR Reactome; R-MMU-5653890; Lactose synthesis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 14595; 9 hits in 79 CRISPR screens.
DR ChiTaRS; B4galt1; mouse.
DR PRO; PR:P15535; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P15535; protein.
DR Bgee; ENSMUSG00000028413; Expressed in lacrimal gland and 229 other tissues.
DR ExpressionAtlas; P15535; baseline and differential.
DR Genevisible; P15535; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0030057; C:desmosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004461; F:lactose synthase activity; IMP:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISO:MGI.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0002526; P:acute inflammatory response; IMP:MGI.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0045136; P:development of secondary sexual characteristics; IMP:MGI.
DR GO; GO:0002064; P:epithelial cell development; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0006012; P:galactose metabolic process; IDA:MGI.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:MGI.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0005989; P:lactose biosynthetic process; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1905517; P:macrophage migration; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
DR GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; IMP:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0060046; P:regulation of acrosome reaction; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Manganese; Membrane; Metal-binding; Reference proteome; Secreted;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..399
FT /note="Beta-1,4-galactosyltransferase 1"
FT /id="PRO_0000012280"
FT CHAIN ?..398
FT /note="Processed beta-1,4-galactosyltransferase 1"
FT /id="PRO_0000296230"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..44
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..399
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 61..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..188
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 223..225
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 250..251
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 313..316
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT BINDING 344..346
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 131..173
FT /evidence="ECO:0000250"
FT DISULFID 244..263
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018803"
SQ SEQUENCE 399 AA; 44411 MW; 084E3437115F4BDD CRC64;
MRFREQFLGG SAAMPGATLQ RACRLLVAVC ALHLGVTLVY YLSGRDLSRL PQLVGVSSTL
QGGTNGAAAS KQPPGEQRPR GARPPPPLGV SPKPRPGLDS SPGAASGPGL KSNLSSLPVP
TTTGLLSLPA CPEESPLLVG PMLIDFNIAV DLELLAKKNP EIKTGGRYSP KDCVSPHKVA
IIIPFRNRQE HLKYWLYYLH PILQRQQLDY GIYVINQAGD TMFNRAKLLN IGFQEALKDY
DYNCFVFSDV DLIPMDDRNA YRCFSQPRHI SVAMDKFGFS LPYVQYFGGV SALSKQQFLA
INGFPNNYWG WGGEDDDIFN RLVHKGMSIS RPNAVVGRCR MIRHSRDKKN EPNPQRFDRI
AHTKETMRFD GLNSLTYKVL DVQRYPLYTQ ITVDIGTPR
