Beta-1,4-GalTase 1
Beta4Gal-T1
b4Gal-T1
EC 2.4.1.-
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1

Includes

Lactose synthase A protein
     (EC 2.4.1.22)
N-acetyllactosamine synthase
     (EC 2.4.1.90)
     (Nal synthetase)
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
     (EC 2.4.1.38)
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
     (EC 2.4.1.-)

Contains

Processed beta-1,4-galactosyltransferase 1

Gene name

	Name:	B4GALT1
	Synonyms:	GALT, GGTB2

From

Bos taurus (Bovine)

[TaxID: 9913]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1111/j.1432-1033.1989.tb14915.x; PubMed=2502398 [NCBI, ExPASy, EBI, Israel, Japan] D'Agostaro G., Bendiak B., Tropak M.; "Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-galactosyltransferase."; Eur. J. Biochem. 183:211-217(1989).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Fetal skin; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 69-402. PubMed=2419911 [NCBI, ExPASy, EBI, Israel, Japan] Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., Hollis G.F.; "Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library."; Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986).
[4]	NUCLEOTIDE SEQUENCE OF 74-402. PubMed=3014508 [NCBI, ExPASy, EBI, Israel, Japan] Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.; "Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase."; Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986).
[5]	SEQUENCE REVISION TO 164; 256 AND 265. Qasba P.K., Narimatsu H., Masibay A.S.; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-77. PubMed=2503823 [NCBI, ExPASy, EBI, Israel, Japan] Masibay A.S., Qasba P.K.; "Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells."; Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-165. PubMed=2105947 [NCBI, ExPASy, EBI, Israel, Japan] Russo R.N., Shaper N.L., Shaper J.H.; "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."; J. Biol. Chem. 265:3324-3331(1990).
[8]	PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-90. PubMed=2117606 [NCBI, ExPASy, EBI, Israel, Japan] Yadav S.P., Brew K.; "Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling."; J. Biol. Chem. 265:14163-14169(1990).
[9]	DISULFIDE BOND. PubMed=1898734 [NCBI, ExPASy, EBI, Israel, Japan] Yadav S.P., Brew K.; "Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond."; J. Biol. Chem. 266:698-703(1991).
[10]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH SUBSTRATE, AND DISULFIDE BONDS. DOI=10.1093/emboj/18.13.3546; PubMed=10393171 [NCBI, ExPASy, EBI, Israel, Japan] Gastinel L.N., Cambillau C., Bourne Y.; "Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose."; EMBO J. 18:3546-3557(1999).
[11]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS. DOI=10.1006/jmbi.2001.4757; PubMed=11419947 [NCBI, ExPASy, EBI, Israel, Japan] Ramakrishnan B., Qasba P.K.; "Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I."; J. Mol. Biol. 310:205-218(2001).
[12]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS. DOI=10.1016/S0022-2836(02)00020-7; PubMed=12051854 [NCBI, ExPASy, EBI, Israel, Japan] Ramakrishnan B., Balaji P.V., Qasba P.K.; "Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site."; J. Mol. Biol. 318:491-502(2002).
[13]	X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS, AND MUTAGENESIS OF TRP-314. DOI=10.1016/S0022-2836(03)00790-3; PubMed=12927542 [NCBI, ExPASy, EBI, Israel, Japan] Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.; "The role of tryptophan 314 in the conformational changes of beta1,4-galactosyltransferase-I."; J. Mol. Biol. 331:1065-1076(2003).

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.
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-galactose + D-glucose = UDP + lactose.
CATALYTIC ACTIVITY: UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.
CATALYTIC ACTIVITY: UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.
COFACTOR: Manganese.
PATHWAY: Protein modification; protein glycosylation .
SUBUNIT: Homodimer; and heterodimer with alpha-lactabulmin to form lactose synthase.
SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi 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.
SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Found in trans cisternae of Golgi.
SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1: Secreted. Note=Soluble form found in body fluids.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative initiation.

Name	Long
Synonyms	Cell surface
Isoform ID	P08037-1
This is the isoform sequence displayed in this entry.

Name	Short
Synonyms	Golgi complex
Isoform ID	P08037-2
Features which should be applied to build the isoform sequence: VSP_018801.

PTM: The soluble form derives from the membrane forms by proteolytic processing.
SIMILARITY: Belongs to the glycosyltransferase 7 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X14558; CAA32695.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC120415; AAI20416.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M13214; AAA30534.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF515786; AAM54035.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M25398; AAA30533.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J05217; AAA30559.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I45897; I45897.
S05018; S05018.

RefSeq

NP_803478.1; -.

UniGene

Bt.5141

3D structure databases

PDB

1FGX; X-ray; 2.40 A; A/B=115-402.	[ExPASy / RCSB / EBI]
1FR8; X-ray; 2.40 A; A/B=115-402.	[ExPASy / RCSB / EBI]
1NF5; X-ray; 2.00 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1NHE; X-ray; 2.50 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1NKH; X-ray; 2.00 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1NMM; X-ray; 2.00 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1NQI; X-ray; 2.00 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1NWG; X-ray; 2.32 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1O0R; X-ray; 2.30 A; A/B=130-402.	[ExPASy / RCSB / EBI]
1O23; X-ray; 2.32 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1OQM; X-ray; 2.10 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1PZT; X-ray; 1.92 A; A=130-402.	[ExPASy / RCSB / EBI]
1PZY; X-ray; 2.30 A; B/D=130-402.	[ExPASy / RCSB / EBI]
1TVY; X-ray; 2.30 A; A/B=130-402.	[ExPASy / RCSB / EBI]
1TW1; X-ray; 2.30 A; A/B=130-402.	[ExPASy / RCSB / EBI]
1TW5; X-ray; 2.30 A; A/B=130-402.	[ExPASy / RCSB / EBI]
1YRO; X-ray; 1.90 A; B/D=130-402.	[ExPASy / RCSB / EBI]
2FYC; X-ray; 2.00 A; B/D=130-402.	[ExPASy / RCSB / EBI]
2FYD; X-ray; 2.00 A; B/D=130-402.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FGX; -.
1FR8; -.
1NF5; -.
1NHE; -.
1NKH; -.
1NMM; -.
1NQI; -.
1NWG; -.
1O0R; -.
1O23; -.
1OQM; -.
1PZT; -.
1PZY; -.
1TVY; -.
1TW1; -.
1TW5; -.
1YRO; -.
2FYC; -.
2FYD; -.

ModBase

P08037.

Ontologies

GO:0016323;	Cellular component: basolateral plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0031526;	Cellular component: brush border membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0030057;	Cellular component: desmosome (inferred from sequence or structural similarity from UniProtKB).
GO:0009897;	Cellular component: external side of plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0030112;	Cellular component: glycocalyx (inferred from sequence or structural similarity from UniProtKB).
GO:0000138;	Cellular component: Golgi trans cisterna (inferred from sequence or structural similarity from UniProtKB).
GO:0003831;	Molecular function: beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0004461;	Molecular function: lactose synthase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0003945;	Molecular function: N-acetyllactosamine synthase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0009312;	Biological process: oligosaccharide biosynthetic process (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003859; Galactosyl_T_2.
Graphical view of domain structure.

PANTHER

PTHR19300; Galactosyl_T_2; 1.

Pfam

PF02709; Galactosyl_T_2; 1.
Pfam graphical view of domain structure.

Genome annotation databases

Ensembl

ENSBTAG00000015249; Bos taurus. [Contig view]

GeneID

281781; -.

KEGG

bta:281781; -.

Phylogenomic databases

HOVERGEN

P08037; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative initiation; Cell membrane; Direct protein sequencing; Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding; Secreted; Signal-anchor; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 402`	`402`	`Beta-1,4-galactosyltransferase 1.`	`PRO_0000012276`
`CHAIN`	`? 402`		`Processed beta-1,4-galactosyltransferase 1.`	`PRO_0000296228`
`TOPO_DOM`	`1 24`	`24`	`Cytoplasmic (Potential).`
`TRANSMEM`	`25 44`	`20`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`45 402`	`358`	`Lumenal (Potential).`
`METAL`	`254 254`		`Manganese.`
`METAL`	`347 347`		`Manganese.`
`CARBOHYD`	`90 90`		`N-linked (GlcNAc...) (Probable).`
`CARBOHYD`	`117 117`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`134 176`
`DISULFID`	`247 266`
`VAR_SEQ`	`1 13`		`Missing (in isoform Short).`	`VSP_018801`
`MUTAGEN`	`314 314`		`W->A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%.`
`CONFLICT`	`65 66`		`HG -> QA (in Ref. 7).`
`CONFLICT`	`158 158`		`V -> I (in Ref. 1; CAA32695).`
`CONFLICT`	`187 187`		`P -> L (in Ref. 1; CAA32695).`
`CONFLICT`	`205 206`		`IL -> MV (in Ref. 1; CAA32695).`
`CONFLICT`	`282 282`		`F -> L (in Ref. 3; AAA30534).`
`HELIX`	`155 161`	`7`
`TURN`	`167 169`	`3`
`STRAND`	`174 177`	`4`
`STRAND`	`181 190`	`10`
`HELIX`	`192 208`	`17`
`STRAND`	`212 220`	`9`
`STRAND`	`222 224`	`3`
`HELIX`	`228 239`	`12`
`TURN`	`240 242`	`3`
`STRAND`	`247 251`	`5`
`STRAND`	`255 259`	`5`
`HELIX`	`278 280`	`3`
`STRAND`	`292 297`	`6`
`HELIX`	`298 303`	`6`
`HELIX`	`317 327`	`11`
`TURN`	`337 340`	`4`
`STRAND`	`341 344`	`4`
`HELIX`	`363 369`	`7`
`TURN`	`370 372`	`3`
`HELIX`	`375 377`	`3`
`STRAND`	`381 387`	`7`
`STRAND`	`392 397`	`6`

Sequence information

Length: 402 AA [This is the length of the unprocessed precursor]

Molecular weight: 44843 Da [This is the MW of the unprocessed precursor]

CRC64: FABF94E74E0C6F81 [This is a checksum on the sequence]

        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

P08037 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools