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P15535 (B4GT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-1,4-galactosyltransferase 1

Short name=Beta-1,4-GalTase 1
Short name=Beta4Gal-T1
Short name=b4Gal-T1
EC=2.4.1.-
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1

Cleaved into the following chain:

  1. Processed beta-1,4-galactosyltransferase 1

Including the following 4 domains:

  1. Lactose synthase A protein
    EC=2.4.1.22
  2. N-acetyllactosamine synthase
    EC=2.4.1.90
    Alternative name(s):
    Nal synthase
  3. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
    EC=2.4.1.38
  4. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
    EC=2.4.1.-
Gene names
Name:B4galt1
Synonyms:Ggtb, Ggtb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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.

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.

UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.

UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase.

Subcellular location

Isoform Long: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Note: Found in trans cisternae of Golgi.

Isoform Short: Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Note: Found in trans cisternae of Golgi.

Processed beta-1,4-galactosyltransferase 1: Secreted. Note: Soluble form found in body fluids.

Developmental stage

In the brain, highest levels of expression are found at 11.5 dpc with decreased expression thereafter. Ref.9

Post-translational modification

The soluble form derives from the membrane forms by proteolytic processing.

Sequence similarities

Belongs to the glycosyltransferase 7 family.

Ontologies

Keywords
   Cellular componentCell membrane
Golgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative initiation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandManganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from mutant phenotype PubMed 12714507. Source: MGI

angiogenesis involved in wound healing

Inferred from mutant phenotype PubMed 15039218. Source: MGI

binding of sperm to zona pellucida

Inferred from mutant phenotype PubMed 9374408. Source: MGI

branching morphogenesis of an epithelial tube

Inferred from mutant phenotype PubMed 11900463PubMed 15282149. Source: MGI

cell adhesion

Inferred from genetic interaction PubMed 12714507. Source: MGI

development of secondary sexual characteristics

Inferred from mutant phenotype PubMed 11900463. Source: MGI

epithelial cell development

Inferred from mutant phenotype PubMed 9155011. Source: MGI

extracellular matrix organization

Inferred from mutant phenotype PubMed 11900463PubMed 8787759. Source: MGI

galactose metabolic process

Inferred from direct assay PubMed 9813328. Source: MGI

glycoprotein biosynthetic process

Inferred from mutant phenotype PubMed 10381349PubMed 11463354PubMed 12714507PubMed 15158676. Source: MGI

lactose biosynthetic process

Inferred from mutant phenotype PubMed 9155011. Source: MGI

leukocyte migration

Inferred from mutant phenotype PubMed 15039218. Source: MGI

mammary gland development

Inferred from mutant phenotype PubMed 11900463. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 9155011. Source: MGI

oligosaccharide biosynthetic process

Inferred from direct assay PubMed 9813328. Source: MGI

penetration of zona pellucida

Inferred from mutant phenotype PubMed 9374408. Source: MGI

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 15282149. Source: MGI

positive regulation of apoptotic process involved in mammary gland involution

Inferred from mutant phenotype PubMed 15282149. Source: MGI

positive regulation of epithelial cell proliferation involved in wound healing

Inferred from mutant phenotype PubMed 15039218. Source: MGI

protein N-linked glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein glycosylation

Inferred from mutant phenotype PubMed 9155011. Source: MGI

regulation of acrosome reaction

Inferred from mutant phenotype PubMed 9374408. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 7641815. Source: MGI

regulation of cellular component movement

Inferred from direct assay PubMed 8134355. Source: MGI

wound healing

Inferred from mutant phenotype PubMed 15039218. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11375348PubMed 2503706. Source: MGI

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi trans cisterna

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

brush border membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 7641815PubMed 8089187PubMed 8134355PubMed 9374408. Source: MGI

desmosome

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

glycocalyx

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 11375348PubMed 2503706. Source: MGI

   Molecular_functionN-acetyllactosamine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity

Inferred from direct assay PubMed 7641815PubMed 9813328. Source: MGI

cytoskeletal protein binding

Inferred from direct assay PubMed 7641815PubMed 8134355. Source: MGI

galactosyltransferase activity

Inferred from direct assay PubMed 7641815PubMed 8089187PubMed 8134355. Source: MGI

lactose synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

manganese ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Long (identifier: P15535-1)

Also known as: Cell surface;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P15535-2)

Also known as: Golgi complex;

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Beta-1,4-galactosyltransferase 1
PRO_0000012280
Chain? – 398Processed beta-1,4-galactosyltransferase 1PRO_0000296230

Regions

Topological domain1 – 2424Cytoplasmic Potential
Transmembrane25 – 4420Helical; Signal-anchor for type II membrane protein; Potential
Topological domain45 – 399355Lumenal Potential
Region184 – 1885UDP-alpha-D-galactose binding By similarity
Region223 – 2253UDP-alpha-D-galactose binding By similarity
Region250 – 2512UDP-alpha-D-galactose binding By similarity
Region313 – 3164N-acetyl-D-glucosamine binding By similarity
Region344 – 3463UDP-alpha-D-galactose binding By similarity

Sites

Metal binding2511Manganese By similarity
Metal binding3441Manganese; via tele nitrogen By similarity
Binding site3111UDP-alpha-D-galactose By similarity
Binding site3561N-acetyl-D-glucosamine By similarity

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential
Disulfide bond131 ↔ 173 By similarity
Disulfide bond244 ↔ 263 By similarity

Natural variations

Alternative sequence1 – 1313Missing in isoform Short.
VSP_018803

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (Cell surface) [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 084E3437115F4BDD

FASTA39944,411
        10         20         30         40         50         60 
MRFREQFLGG SAAMPGATLQ RACRLLVAVC ALHLGVTLVY YLSGRDLSRL PQLVGVSSTL 

        70         80         90        100        110        120 
QGGTNGAAAS KQPPGEQRPR GARPPPPLGV SPKPRPGLDS SPGAASGPGL KSNLSSLPVP 

       130        140        150        160        170        180 
TTTGLLSLPA CPEESPLLVG PMLIDFNIAV DLELLAKKNP EIKTGGRYSP KDCVSPHKVA 

       190        200        210        220        230        240 
IIIPFRNRQE HLKYWLYYLH PILQRQQLDY GIYVINQAGD TMFNRAKLLN IGFQEALKDY 

       250        260        270        280        290        300 
DYNCFVFSDV DLIPMDDRNA YRCFSQPRHI SVAMDKFGFS LPYVQYFGGV SALSKQQFLA 

       310        320        330        340        350        360 
INGFPNNYWG WGGEDDDIFN RLVHKGMSIS RPNAVVGRCR MIRHSRDKKN EPNPQRFDRI 

       370        380        390 
AHTKETMRFD GLNSLTYKVL DVQRYPLYTQ ITVDIGTPR 

« Hide

Isoform Short (Golgi complex) [UniParc].

Checksum: 18D2F0BAF5387AAC
Show »

FASTA38642,959

References

« Hide 'large scale' references
[1]"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."
Shaper N.L., Hollis G.F., Douglas J.G., Kirsch I.R., Shaper J.H.
J. Biol. Chem. 263:10420-10428(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Murine beta 1,4-galactosyltransferase: both the amounts and structure of the mRNA are regulated during spermatogenesis."
Shaper N.L., Wright W.W., Sharper J.H.
Proc. Natl. Acad. Sci. U.S.A. 87:791-795(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic structure of murine beta-1,4-galactosyltransferase."
Hollis G.F., Douglas J.G., Shaper N.L., Shaper J.H., Stafford-Hollis J.M., Evans R.J., Kirsch I.R.
Biochem. Biophys. Res. Commun. 162:1069-1075(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Cloning and sequencing of a full-length cDNA of mouse N-acetylglucosamine (beta 1-4)galactosyltransferase."
Nakazawa K., Ando T., Kimura T., Narimatsu H.
J. Biochem. 104:165-168(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[6]"Evidence for two forms of murine beta-1,4-galactosyltransferase based on cloning studies."
Shaper J.H., Hollis G.F., Shaper N.L.
Biochimie 70:1683-1688(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-63.
[7]"Murine beta 1,4-galactosyltransferase: round spermatid transcripts are characterized by an extended 5'-untranslated region."
Harduin-Lepers A., Shaper N.L., Mahoney J.A., Shaper J.H.
Glycobiology 2:361-368(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-20.
Strain: BALB/c.
[8]"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."
Harduin-Lepers A., Shaper J.H., Shaper N.L.
J. Biol. Chem. 268:14348-14359(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-20.
Strain: BALB/c.
[9]"Differential gene expression of beta-1,4-galactosyltransferases I, II and V during mouse brain development."
Nakamura N., Yamakawa N., Sato T., Tojo H., Tachi C., Furukawa K.
J. Neurochem. 76:29-38(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
Strain: BALB/c.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03880 mRNA. Translation: AAA37297.1.
D00314 mRNA. Translation: BAA00216.1.
M27922 expand/collapse EMBL AC list , M27917, M27918, M27919, M27920, M27921 Genomic DNA. Translation: AAA58745.1.
M27922 expand/collapse EMBL AC list , M27917, M27918, M27919, M27920, M27921 Genomic DNA. Translation: AAA58744.1.
BC053006 mRNA. Translation: AAH53006.1.
M36289 mRNA. Translation: AAA37294.1.
L16840 mRNA. Translation: AAA62340.1.
PIRA33396.
RefSeqNP_071641.1. NM_022305.4.
UniGeneMm.15622.

3D structure databases

ProteinModelPortalP15535.
SMRP15535. Positions 127-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199912. 2 interactions.
IntActP15535. 1 interaction.
MINTMINT-1864544.

Protein family/group databases

CAZyGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteP15535.

Proteomic databases

PaxDbP15535.
PRIDEP15535.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030121; ENSMUSP00000030121; ENSMUSG00000028413. [P15535-1]
GeneID14595.
KEGGmmu:14595.
UCSCuc008shw.1. mouse. [P15535-1]

Organism-specific databases

CTD2683.
MGIMGI:95705. B4galt1.

Phylogenomic databases

eggNOGNOG327897.
HOGENOMHOG000231027.
HOVERGENHBG058334.
InParanoidP15535.
KOK07966.
OMAMSVSRPN.
OrthoDBEOG7060R0.
PhylomeDBP15535.
TreeFamTF312834.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressP15535.
BgeeP15535.
GenevestigatorP15535.

Family and domain databases

InterProIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
[Graphical view]
PANTHERPTHR19300. PTHR19300. 1 hit.
PfamPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSPR02050. B14GALTRFASE.
ProtoNetSearch...

Other

ChiTaRSB4GALT1. mouse.
NextBio286356.
PROP15535.
SOURCESearch...

Entry information

Entry nameB4GT1_MOUSE
AccessionPrimary (citable) accession number: P15535
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot