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P08037 (B4GT1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. 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·Interactions·Alt products·Sequence annotation·Sequences·References·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:GALT, GGTB2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

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.

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 term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from electronic annotation. Source: Ensembl

angiogenesis involved in wound healing

Inferred from electronic annotation. Source: Ensembl

binding of sperm to zona pellucida

Inferred from electronic annotation. Source: Ensembl

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: Ensembl

development of secondary sexual characteristics

Inferred from electronic annotation. Source: Ensembl

epithelial cell development

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

galactose metabolic process

Inferred from electronic annotation. Source: Ensembl

lactose biosynthetic process

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Inferred from electronic annotation. Source: Ensembl

mammary gland development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

oligosaccharide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

penetration of zona pellucida

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process involved in mammary gland involution

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation involved in wound healing

Inferred from electronic annotation. Source: Ensembl

protein N-linked glycosylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of acrosome reaction

Inferred from electronic annotation. Source: Ensembl

regulation of cellular component movement

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from sequence or structural similarity. Source: UniProtKB

Golgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi trans cisterna

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

brush border membrane

Inferred from sequence or structural similarity. Source: UniProtKB

desmosome

Inferred from sequence or structural similarity. Source: UniProtKB

external side of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

glycocalyx

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionN-acetyllactosamine synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

UDP-galactosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

alpha-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from sequence or structural similarity. Source: UniProtKB

beta-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

lactose synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

manganese ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11PubMed 11485999PubMed 11916963Ref.13PubMed 15736931. Source: IntAct

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LalbaP2975210EBI-1031436,EBI-1031454From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Long (identifier: P08037-1)

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: P08037-2)

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 – 402402Beta-1,4-galactosyltransferase 1
PRO_0000012276
Chain? – 402Processed beta-1,4-galactosyltransferase 1PRO_0000296228

Regions

Topological domain1 – 2424Cytoplasmic Potential
Transmembrane25 – 4420Helical; Signal-anchor for type II membrane protein; Potential
Topological domain45 – 402358Lumenal Potential
Region187 – 1915UDP-alpha-D-galactose binding
Region226 – 2283UDP-alpha-D-galactose binding
Region253 – 2542UDP-alpha-D-galactose binding
Region316 – 3194N-acetyl-D-glucosamine binding
Region347 – 3493UDP-alpha-D-galactose binding

Sites

Metal binding2541Manganese
Metal binding3471Manganese; via tele nitrogen
Binding site3141UDP-alpha-D-galactose
Binding site3591N-acetyl-D-glucosamine

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Probable
Glycosylation1171N-linked (GlcNAc...) Potential
Disulfide bond134 ↔ 176 Ref.9 Ref.10
Disulfide bond247 ↔ 266 Ref.9 Ref.10

Natural variations

Alternative sequence1 – 1313Missing in isoform Short.
VSP_018801

Experimental info

Mutagenesis3141W → A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%. Ref.13
Sequence conflict65 – 662HG → QA Ref.7
Sequence conflict1581V → I in CAA32695. Ref.1
Sequence conflict1871P → L in CAA32695. Ref.1
Sequence conflict205 – 2062IL → MV in CAA32695. Ref.1
Sequence conflict2821F → L in AAA30534. Ref.3

Secondary structure

................................................. 402
Helix Strand Turn

Details...

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: FABF94E74E0C6F81

FASTA40244,843
        10         20         30         40         50         60 
MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL PQLVGVHPPL 

        70         80         90        100        110        120 
QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS NLDAYSHPGP GPGPGSNLTS 

       130        140        150        160        170        180 
APVPSTTTRS LTACPEESPL LVGPMLIEFN IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH 

       190        200        210        220        230        240 
KVAIIIPFRN RQEHLKYWLY YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL 

       250        260        270        280        290        300 
KDYDYNCFVF SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ 

       310        320        330        340        350        360 
FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD KKNEPNPQRF 

       370        380        390        400 
DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT PS 

« Hide

Isoform Short (Golgi complex) [UniParc].

Checksum: 6C016BFC25872CCA
Show »

FASTA38943,484

References

« Hide 'large scale' references
[1]"Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-galactosyltransferase."
D'Agostaro G., Bendiak B., Tropak M.
Eur. J. Biochem. 183:211-217(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal skin.
[3]"Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library."
Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., Hollis G.F.
Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-402.
[4]"Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase."
Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.
Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 74-402.
[5]Qasba P.K., Narimatsu H., Masibay A.S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 164; 256 AND 265.
[6]"Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells."
Masibay A.S., Qasba P.K.
Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-77.
[7]"Bovine beta 1-->4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins."
Russo R.N., Shaper N.L., Shaper J.H.
J. Biol. Chem. 265:3324-3331(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165.
[8]"Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling."
Yadav S.P., Brew K.
J. Biol. Chem. 265:14163-14169(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-90.
[9]"Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond."
Yadav S.P., Brew K.
J. Biol. Chem. 266:698-703(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BOND.
[10]"Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose."
Gastinel L.N., Cambillau C., Bourne Y.
EMBO J. 18:3546-3557(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH SUBSTRATE, DISULFIDE BONDS.
[11]"Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I."
Ramakrishnan B., Qasba P.K.
J. Mol. Biol. 310:205-218(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS.
[12]"Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site."
Ramakrishnan B., Balaji P.V., Qasba P.K.
J. Mol. Biol. 318:491-502(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS.
[13]"The role of tryptophan 314 in the conformational changes of beta1,4-galactosyltransferase-I."
Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.
J. Mol. Biol. 331:1065-1076(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS, MUTAGENESIS OF TRP-314.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14558 mRNA. Translation: CAA32695.1.
BC120415 mRNA. Translation: AAI20416.1.
M13214 mRNA. Translation: AAA30534.1.
AF515786 mRNA. Translation: AAM54035.2.
M25398 Genomic DNA. Translation: AAA30533.1.
J05217 mRNA. Translation: AAA30559.1.
PIRI45897.
S05018.
RefSeqNP_803478.1. NM_177512.2.
UniGeneBt.5141.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FGXX-ray2.40A/B115-402[»]
1FR8X-ray2.40A/B115-402[»]
1NF5X-ray2.00B/D130-402[»]
1NHEX-ray2.50B/D130-402[»]
1NKHX-ray2.00B/D130-402[»]
1NMMX-ray2.00B/D130-402[»]
1NQIX-ray2.00B/D130-402[»]
1NWGX-ray2.32B/D130-402[»]
1O0RX-ray2.30A/B130-402[»]
1O23X-ray2.32B/D130-402[»]
1OQMX-ray2.10B/D130-402[»]
1PZTX-ray1.92A130-402[»]
1PZYX-ray2.30B/D130-402[»]
1TVYX-ray2.30A/B130-402[»]
1TW1X-ray2.30A/B130-402[»]
1TW5X-ray2.30A/B130-402[»]
1YROX-ray1.90B/D130-402[»]
2FYCX-ray2.00B/D130-402[»]
2FYDX-ray2.00B/D130-400[»]
4KRVX-ray2.40A/B130-402[»]
ProteinModelPortalP08037.
SMRP08037. Positions 131-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP08037. 1 interaction.

Chemistry

BindingDBP08037.
ChEMBLCHEMBL3214.

Protein family/group databases

CAZyGT7. Glycosyltransferase Family 7.

Proteomic databases

PaxDbP08037.
PRIDEP08037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-2]
GeneID281781.
KEGGbta:281781.

Organism-specific databases

CTD2683.

Phylogenomic databases

eggNOGNOG327897.
GeneTreeENSGT00740000115031.
HOGENOMHOG000231027.
HOVERGENHBG058334.
InParanoidP08037.
KOK07966.
OMAVGGRYTP.
OrthoDBEOG7060R0.
TreeFamTF312834.

Enzyme and pathway databases

SABIO-RKP08037.
UniPathwayUPA00378.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR19300. PTHR19300. 1 hit.
PfamPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSPR02050. B14GALTRFASE.
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP08037.
NextBio20805694.

Entry information

Entry nameB4GT1_BOVIN
AccessionPrimary (citable) accession number: P08037
Secondary accession number(s): Q0VC05, Q8MIG0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 158 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways