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 B4GT1_MOUSE             Reviewed;         399 AA.
P15535;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
30-AUG-2017, entry version 181.
RecName: Full=Beta-1,4-galactosyltransferase 1;
Short=Beta-1,4-GalTase 1;
Short=Beta4Gal-T1;
Short=b4Gal-T1;
EC=2.4.1.-;
AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1;
Includes:
RecName: Full=Lactose synthase A protein;
EC=2.4.1.22;
Includes:
RecName: Full=N-acetyllactosamine synthase;
EC=2.4.1.90;
AltName: Full=Nal synthase;
Includes:
RecName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
EC=2.4.1.38;
Includes:
RecName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
EC=2.4.1.-;
Contains:
RecName: Full=Processed beta-1,4-galactosyltransferase 1;
Name=B4galt1; Synonyms=Ggtb, Ggtb2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=3134348;
Shaper N.L., Hollis G.F., Douglas J.G., Kirsch I.R., Shaper J.H.;
"Characterization of the full length cDNA for murine beta-1,4-
galactosyltransferase. Novel features at the 5'-end predict two
translational start sites at two in-frame AUGs.";
J. Biol. Chem. 263:10420-10428(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1689054; DOI=10.1073/pnas.87.2.791;
Shaper N.L., Wright W.W., Sharper J.H.;
"Murine beta 1,4-galactosyltransferase: both the amounts and structure
of the mRNA are regulated during spermatogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 87:791-795(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2504153; DOI=10.1016/0006-291X(89)90782-1;
Hollis G.F., Douglas J.G., Shaper N.L., Shaper J.H.,
Stafford-Hollis J.M., Evans R.J., Kirsch I.R.;
"Genomic structure of murine beta-1,4-galactosyltransferase.";
Biochem. Biophys. Res. Commun. 162:1069-1075(1989).
[4]
NUCLEOTIDE SEQUENCE.
PubMed=3141392;
Nakazawa K., Ando T., Kimura T., Narimatsu H.;
"Cloning and sequencing of a full-length cDNA of mouse N-
acetylglucosamine (beta 1-4)galactosyltransferase.";
J. Biochem. 104:165-168(1988).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE OF 1-63, AND SUBCELLULAR LOCATION (ISOFORM SHORT).
PubMed=3149531; DOI=10.1016/0300-9084(88)90303-3;
Shaper J.H., Hollis G.F., Shaper N.L.;
"Evidence for two forms of murine beta-1,4-galactosyltransferase based
on cloning studies.";
Biochimie 70:1683-1688(1988).
[7]
NUCLEOTIDE SEQUENCE OF 1-20.
STRAIN=BALB/cJ;
PubMed=1384819; DOI=10.1093/glycob/2.4.361;
Harduin-Lepers A., Shaper N.L., Mahoney J.A., Shaper J.H.;
"Murine beta 1,4-galactosyltransferase: round spermatid transcripts
are characterized by an extended 5'-untranslated region.";
Glycobiology 2:361-368(1992).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-20.
STRAIN=BALB/cJ;
PubMed=8314795;
Harduin-Lepers A., Shaper J.H., Shaper N.L.;
"Characterization of two cis-regulatory regions in the murine beta
1,4-galactosyltransferase gene. Evidence for a negative regulatory
element that controls initiation at the proximal site.";
J. Biol. Chem. 268:14348-14359(1993).
[9]
DEVELOPMENTAL STAGE.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=11145975; DOI=10.1046/j.1471-4159.2001.00004.x;
Nakamura N., Yamakawa N., Sato T., Tojo H., Tachi C., Furukawa K.;
"Differential gene expression of beta-1,4-galactosyltransferases I, II
and V during mouse brain development.";
J. Neurochem. 76:29-38(2001).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2Q1.
PubMed=18511602; DOI=10.1634/stemcells.2007-1080;
Wassler M.J., Shur B.D., Zhou W., Geng Y.J.;
"Characterization of a novel ubiquitin-conjugating enzyme that
regulates beta1,4-galactosyltransferase-1 in embryonic stem cells.";
Stem Cells 26:2006-2018(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: The Golgi complex form catalyzes the production of
lactose in the lactating mammary gland and could also be
responsible for the synthesis of complex-type N-linked
oligosaccharides in many glycoproteins as well as the carbohydrate
moieties of glycolipids.
-!- FUNCTION: The cell surface form functions as a recognition
molecule during a variety of cell to cell and cell to matrix
interactions, as those occurring during development and egg
fertilization, by binding to specific oligosaccharide ligands on
opposing cells or in the extracellular matrix.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + D-glucose = UDP +
lactose.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-beta-D-
glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-
acetyl-beta-D-glucosaminylglycopeptide.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-galactose + N-acetyl-D-glucosamine
= UDP + N-acetyllactosamine.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form
lactose synthase (By similarity). Interacts (via N-terminal
cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction
is direct (PubMed:18511602). {ECO:0000250|UniProtKB:P15291,
ECO:0000269|PubMed:18511602}.
-!- SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi stack
membrane {ECO:0000269|PubMed:18511602}; Single-pass type II
membrane protein. Cell membrane; Single-pass type II membrane
protein. Cell surface. Cell projection, filopodium
{ECO:0000269|PubMed:18511602}. Note=Found in trans cisternae of
Golgi. B4GALT1 cell surface expression is regulated by UBE2Q1
(PubMed:18511602). {ECO:0000269|PubMed:18511602}.
-!- SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack
membrane {ECO:0000269|PubMed:3149531}; Single-pass type II
membrane protein {ECO:0000269|PubMed:3149531}. Note=Found in trans
cisternae of Golgi. {ECO:0000269|PubMed:3149531}.
-!- SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1:
Secreted {ECO:0000250|UniProtKB:P15291}. Note=Soluble form found
in body fluids. {ECO:0000250|UniProtKB:P15291}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long; Synonyms=Cell surface;
IsoId=P15535-1; Sequence=Displayed;
Name=Short; Synonyms=Golgi complex;
IsoId=P15535-2; Sequence=VSP_018803;
-!- DEVELOPMENTAL STAGE: In the brain, highest levels of expression
are found at 11.5 dpc with decreased expression thereafter.
{ECO:0000269|PubMed:11145975}.
-!- PTM: The soluble form derives from the membrane forms by
proteolytic processing.
-!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=b4GalT1;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_460";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; J03880; AAA37297.1; -; mRNA.
EMBL; D00314; BAA00216.1; -; mRNA.
EMBL; M27922; AAA58745.1; -; Genomic_DNA.
EMBL; M27917; AAA58745.1; JOINED; Genomic_DNA.
EMBL; M27918; AAA58745.1; JOINED; Genomic_DNA.
EMBL; M27919; AAA58745.1; JOINED; Genomic_DNA.
EMBL; M27920; AAA58745.1; JOINED; Genomic_DNA.
EMBL; M27921; AAA58745.1; JOINED; Genomic_DNA.
EMBL; M27922; AAA58744.1; -; Genomic_DNA.
EMBL; M27917; AAA58744.1; JOINED; Genomic_DNA.
EMBL; M27918; AAA58744.1; JOINED; Genomic_DNA.
EMBL; M27919; AAA58744.1; JOINED; Genomic_DNA.
EMBL; M27920; AAA58744.1; JOINED; Genomic_DNA.
EMBL; M27921; AAA58744.1; JOINED; Genomic_DNA.
EMBL; BC053006; AAH53006.1; -; mRNA.
EMBL; M36289; AAA37294.1; -; mRNA.
EMBL; L16840; AAA62340.1; -; mRNA.
CCDS; CCDS18051.1; -. [P15535-1]
PIR; A33396; A33396.
RefSeq; NP_071641.1; NM_022305.4. [P15535-1]
UniGene; Mm.15622; -.
ProteinModelPortal; P15535; -.
SMR; P15535; -.
BioGrid; 199912; 12.
IntAct; P15535; 11.
MINT; MINT-1864544; -.
STRING; 10090.ENSMUSP00000030121; -.
CAZy; GT7; Glycosyltransferase Family 7.
PhosphoSitePlus; P15535; -.
SwissPalm; P15535; -.
PaxDb; P15535; -.
PeptideAtlas; P15535; -.
PRIDE; P15535; -.
Ensembl; ENSMUST00000030121; ENSMUSP00000030121; ENSMUSG00000028413. [P15535-1]
GeneID; 14595; -.
KEGG; mmu:14595; -.
UCSC; uc008shw.2; mouse. [P15535-1]
CTD; 2683; -.
MGI; MGI:95705; B4galt1.
eggNOG; KOG3916; Eukaryota.
eggNOG; ENOG410ZYYA; LUCA.
GeneTree; ENSGT00760000119140; -.
HOGENOM; HOG000231027; -.
HOVERGEN; HBG058334; -.
InParanoid; P15535; -.
KO; K07966; -.
OMA; AHTRETM; -.
OrthoDB; EOG091G0P66; -.
PhylomeDB; P15535; -.
TreeFam; TF312834; -.
Reactome; R-MMU-1300644; Interaction With The Zona Pellucida.
Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
Reactome; R-MMU-5653890; Lactose synthesis.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-975577; N-Glycan antennae elongation.
UniPathway; UPA00378; -.
ChiTaRS; B4galt1; mouse.
PRO; PR:P15535; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028413; -.
ExpressionAtlas; P15535; baseline and differential.
Genevisible; P15535; MM.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0031526; C:brush border membrane; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0030057; C:desmosome; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000138; C:Golgi trans cisterna; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:MGI.
GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
GO; GO:0008378; F:galactosyltransferase activity; IDA:MGI.
GO; GO:0004461; F:lactose synthase activity; ISO:MGI.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0035250; F:UDP-galactosyltransferase activity; ISO:MGI.
GO; GO:0002526; P:acute inflammatory response; IMP:MGI.
GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IGI:MGI.
GO; GO:0045136; P:development of secondary sexual characteristics; IMP:MGI.
GO; GO:0002064; P:epithelial cell development; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0006012; P:galactose metabolic process; IDA:MGI.
GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:MGI.
GO; GO:0005989; P:lactose biosynthetic process; IMP:MGI.
GO; GO:0050900; P:leukocyte migration; IMP:MGI.
GO; GO:0030879; P:mammary gland development; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:MGI.
GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0060058; P:positive regulation of apoptotic process involved in mammary gland involution; IMP:MGI.
GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IMP:MGI.
GO; GO:0006486; P:protein glycosylation; IMP:MGI.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
GO; GO:0060046; P:regulation of acrosome reaction; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0051270; P:regulation of cellular component movement; IDA:MGI.
GO; GO:0042060; P:wound healing; IMP:MGI.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR003859; Galactosyl_T.
InterPro; IPR027791; Galactosyl_T_C.
InterPro; IPR027995; Galactosyl_T_N.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR19300; PTHR19300; 1.
Pfam; PF02709; Glyco_transf_7C; 1.
Pfam; PF13733; Glyco_transf_7N; 1.
PRINTS; PR02050; B14GALTRFASE.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
Alternative initiation; Cell membrane; Cell projection;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Manganese; Membrane; Metal-binding;
Reference proteome; Secreted; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 399 Beta-1,4-galactosyltransferase 1.
/FTId=PRO_0000012280.
CHAIN ? 398 Processed beta-1,4-galactosyltransferase
1.
/FTId=PRO_0000296230.
TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.
TRANSMEM 25 44 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 45 399 Lumenal. {ECO:0000255}.
REGION 184 188 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 223 225 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 250 251 UDP-alpha-D-galactose binding.
{ECO:0000250}.
REGION 313 316 N-acetyl-D-glucosamine binding.
{ECO:0000250}.
REGION 344 346 UDP-alpha-D-galactose binding.
{ECO:0000250}.
METAL 251 251 Manganese. {ECO:0000250}.
METAL 344 344 Manganese; via tele nitrogen.
{ECO:0000250}.
BINDING 311 311 UDP-alpha-D-galactose. {ECO:0000250}.
BINDING 356 356 N-acetyl-D-glucosamine. {ECO:0000250}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 131 173 {ECO:0000250}.
DISULFID 244 263 {ECO:0000250}.
VAR_SEQ 1 13 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_018803.
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


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