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Protein

Beta-1,4-galactosyltransferase 1

Gene

B4GALT1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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.

Cofactori

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi254Manganese1
Binding sitei314UDP-alpha-D-galactose1
Metal bindingi347Manganese; via tele nitrogen1
Binding sitei359N-acetyl-D-glucosamine1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.133. 908.
ReactomeiR-BTA-1300644. Interaction With The Zona Pellucida.
R-BTA-2022854. Keratan sulfate biosynthesis.
R-BTA-5653890. Lactose synthesis.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-975577. N-Glycan antennae elongation.
SABIO-RKP08037.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.
MoonProtiP08037.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 1 (EC:2.4.1.-)
Short name:
Beta-1,4-GalTase 1
Short name:
Beta4Gal-T1
Short name:
b4Gal-T1
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:
Including the following 4 domains:
Lactose synthase A protein (EC:2.4.1.22)
N-acetyllactosamine synthase (EC:2.4.1.90)
Alternative name(s):
Nal synthase
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
Gene namesi
Name:B4GALT1
Synonyms:GALT, GGTB2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 8

Subcellular locationi

Isoform Long :
Processed beta-1,4-galactosyltransferase 1 :
  • Secreted

  • Note: Soluble form found in body fluids.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 24CytoplasmicSequence analysisAdd BLAST24
Transmembranei25 – 44Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini45 – 402LumenalSequence analysisAdd BLAST358

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi314W → A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3214.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000296228? – 402Processed beta-1,4-galactosyltransferase 1
ChainiPRO_00000122761 – 402Beta-1,4-galactosyltransferase 1Add BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi90N-linked (GlcNAc...)1 Publication1
Glycosylationi117N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi134 ↔ 176
Disulfide bondi247 ↔ 266

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP08037.
PeptideAtlasiP08037.
PRIDEiP08037.

Expressioni

Gene expression databases

BgeeiENSBTAG00000015249.

Interactioni

Subunit structurei

Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase (PubMed:10393171, PubMed:11419947, PubMed:12051854, PubMed:12927542). Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LalbaP2975210EBI-1031436,EBI-1031454From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

IntActiP08037. 1 interactor.
STRINGi9913.ENSBTAP00000020286.

Chemistry databases

BindingDBiP08037.

Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi149 – 151Combined sources3
Helixi155 – 161Combined sources7
Turni167 – 169Combined sources3
Beta strandi174 – 177Combined sources4
Beta strandi181 – 190Combined sources10
Helixi192 – 208Combined sources17
Beta strandi212 – 220Combined sources9
Beta strandi222 – 224Combined sources3
Helixi228 – 242Combined sources15
Beta strandi247 – 251Combined sources5
Beta strandi255 – 259Combined sources5
Helixi278 – 280Combined sources3
Beta strandi292 – 297Combined sources6
Helixi298 – 303Combined sources6
Beta strandi313 – 316Combined sources4
Helixi317 – 327Combined sources11
Turni337 – 340Combined sources4
Beta strandi341 – 344Combined sources4
Turni347 – 349Combined sources3
Helixi351 – 353Combined sources3
Helixi359 – 364Combined sources6
Helixi366 – 369Combined sources4
Turni370 – 372Combined sources3
Helixi375 – 377Combined sources3
Beta strandi381 – 387Combined sources7
Beta strandi392 – 397Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP08037.
SMRiP08037.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08037.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni187 – 191UDP-alpha-D-galactose binding5
Regioni226 – 228UDP-alpha-D-galactose binding3
Regioni253 – 254UDP-alpha-D-galactose binding2
Regioni316 – 319N-acetyl-D-glucosamine binding4
Regioni347 – 349UDP-alpha-D-galactose binding3

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3916. Eukaryota.
ENOG410ZYYA. LUCA.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiP08037.
KOiK07966.
OMAiAHTRETM.
OrthoDBiEOG091G0P66.
TreeFamiTF312834.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 2 hits.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Long (identifier: P08037-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL
60 70 80 90 100
PQLVGVHPPL QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS
110 120 130 140 150
NLDAYSHPGP GPGPGSNLTS APVPSTTTRS LTACPEESPL LVGPMLIEFN
160 170 180 190 200
IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH KVAIIIPFRN RQEHLKYWLY
210 220 230 240 250
YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL KDYDYNCFVF
260 270 280 290 300
SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ
310 320 330 340 350
FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD
360 370 380 390 400
KKNEPNPQRF DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT

PS
Length:402
Mass (Da):44,843
Last modified:October 17, 2006 - v3
Checksum:iFABF94E74E0C6F81
GO
Isoform Short (identifier: P08037-2) [UniParc]FASTAAdd to basket
Also known as: Golgi complex

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

Show »
Length:389
Mass (Da):43,484
Checksum:i6C016BFC25872CCA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65 – 66HG → QA (PubMed:2105947).Curated2
Sequence conflicti158V → I in CAA32695 (PubMed:2502398).Curated1
Sequence conflicti187P → L in CAA32695 (PubMed:2502398).Curated1
Sequence conflicti205 – 206IL → MV in CAA32695 (PubMed:2502398).Curated2
Sequence conflicti282F → L in AAA30534 (PubMed:2419911).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188011 – 13Missing in isoform Short. CuratedAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI45897.
S05018.
RefSeqiNP_803478.1. NM_177512.2.
UniGeneiBt.5141.

Genome annotation databases

EnsembliENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-2]
GeneIDi281781.
KEGGibta:281781.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiI45897.
S05018.
RefSeqiNP_803478.1. NM_177512.2.
UniGeneiBt.5141.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP08037.
SMRiP08037.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP08037. 1 interactor.
STRINGi9913.ENSBTAP00000020286.

Chemistry databases

BindingDBiP08037.
ChEMBLiCHEMBL3214.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.
MoonProtiP08037.

Proteomic databases

PaxDbiP08037.
PeptideAtlasiP08037.
PRIDEiP08037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-2]
GeneIDi281781.
KEGGibta:281781.

Organism-specific databases

CTDi2683.

Phylogenomic databases

eggNOGiKOG3916. Eukaryota.
ENOG410ZYYA. LUCA.
GeneTreeiENSGT00760000119140.
HOGENOMiHOG000231027.
HOVERGENiHBG058334.
InParanoidiP08037.
KOiK07966.
OMAiAHTRETM.
OrthoDBiEOG091G0P66.
TreeFamiTF312834.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.133. 908.
ReactomeiR-BTA-1300644. Interaction With The Zona Pellucida.
R-BTA-2022854. Keratan sulfate biosynthesis.
R-BTA-5653890. Lactose synthesis.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-975577. N-Glycan antennae elongation.
SABIO-RKP08037.

Miscellaneous databases

EvolutionaryTraceiP08037.

Gene expression databases

BgeeiENSBTAG00000015249.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 2 hits.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiB4GT1_BOVIN
AccessioniPrimary (citable) accession number: P08037
Secondary accession number(s): Q0VC05, Q8MIG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.