Reviewed, UniProtKB/Swiss-Prot P08037 (B4GT1_BOVIN)

Names and origin

Protein names

Recommended 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-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
    UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
Cleaved into the following chain:
    1- Recommended name:
            Processed beta-1,4-galactosyltransferase 1
Including the following 4 domains:
    1- Recommended name:
            Lactose synthase A protein
              EC=2.4.1.22
    2- Recommended name:
            N-acetyllactosamine synthase
              EC=2.4.1.90
        Alternative name(s):
            Nal synthetase
    3- Recommended name:
            Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
              EC=2.4.1.38
    4- Recommended name:
            Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
              EC=2.4.1.-

Gene names

Name:	B4GALT1
Synonyms:	GALT, GGTB2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-galactose + D-glucose = UDP + lactose. UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide. UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.
Cofactor	Manganese.
Pathway	Protein modification; protein glycosylation.
Subunit structure	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. Isoform Short: Golgi apparatus › Golgi 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 component	Cell membrane Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative initiation
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	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-KW glycocalyx Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetyllactosamine synthase 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 electronic annotation. Source: UniProtKB-KW protein homodimerization activity 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: 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.

Note: Found in trans cisternae of Golgi.

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.

Note: Found in trans cisternae of Golgi.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 402

402

Beta-1,4-galactosyltransferase 1

PRO_0000012276

Chain

? – 402

Processed beta-1,4-galactosyltransferase 1

PRO_0000296228

Regions

Topological domain

1 – 24

24

Cytoplasmic Potential

Transmembrane

25 – 44

20

Signal-anchor for type II membrane protein Potential

Topological domain

45 – 402

358

Lumenal Potential

Sites

Metal binding

254

1

Manganese

Metal binding

347

1

Manganese

Amino acid modifications

Glycosylation

90

1

N-linked (GlcNAc...) Probable

Glycosylation

117

1

N-linked (GlcNAc...) Potential

Disulfide bond

134 ↔ 176

Ref.9 Ref.10

Disulfide bond

247 ↔ 266

Ref.9 Ref.10

Natural variations

Alternative sequence

1 – 13

13

Missing in isoform Short.

VSP_018801

Experimental info

Mutagenesis

314

1

W → A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%. Ref.13

Sequence conflict

65 – 66

2

HG → QA Ref.7

Sequence conflict

158

1

V → I in CAA32695. Ref.1

Sequence conflict

187

1

P → L in CAA32695. Ref.1

Sequence conflict

205 – 206

2

IL → MV in CAA32695. Ref.1

Sequence conflict

282

1

F → L in AAA30534. Ref.3

Secondary structure

1

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402

Helix Strand Turn

Details...

Helix

155 – 161

7

Turn

167 – 169

3

Beta strand

174 – 177

4

Beta strand

181 – 190

10

Helix

192 – 208

17

Beta strand

212 – 220

9

Beta strand

222 – 224

3

Helix

228 – 239

12

Turn

240 – 242

3

Beta strand

247 – 251

5

Beta strand

255 – 259

5

Helix

278 – 280

3

Beta strand

292 – 297

6

Helix

298 – 303

6

Helix

317 – 327

11

Turn

337 – 340

4

Beta strand

341 – 344

4

Helix

363 – 369

7

Turn

370 – 372

3

Helix

375 – 377

3

Beta strand

381 – 387

7

Beta strand

392 – 397

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (Cell surface) [UniParc]. Last modified October 17, 2006. Version 3. Checksum: FABF94E74E0C6F81	FASTA	402	44,843
	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
	Isoform Short (Golgi complex). Checksum: 6C016BFC25872CCA	FASTA	389	43,484
	10 20 30 40 50 60 MPGASLQRAC RLLVAVCALH LGVTLVYYLA GRDLRRLPQL VGVHPPLQGS SHGAAAIGQP 70 80 90 100 110 120 SGELRLRGVA PPPPLQNSSK PRSRAPSNLD AYSHPGPGPG PGSNLTSAPV PSTTTRSLTA 130 140 150 160 170 180 CPEESPLLVG PMLIEFNIPV DLKLVEQQNP KVKLGGRYTP MDCISPHKVA IIIPFRNRQE 190 200 210 220 230 240 HLKYWLYYLH PILQRQQLDY GIYVINQAGE SMFNRAKLLN VGFKEALKDY DYNCFVFSDV 250 260 270 280 290 300 DLIPMNDHNT YRCFSQPRHI SVAMDKFGFS LPYVQYFGGV SALSKQQFLS INGFPNNYWG 310 320 330 340 350 360 WGGEDDDIYN RLAFRGMSVS RPNAVIGKCR MIRHSRDKKN EPNPQRFDRI AHTKETMLSD 370 380 GLNSLTYMVL EVQRYPLYTK ITVDIGTPS

References

	« Hide 'large scale' referencesShow '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: 2502398] [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: 2419911] [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: 3014508] [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: 2503823] [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: 2105947] [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: 2117606] [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: 1898734] [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: 10393171] [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: 11419947] [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: 12051854] [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: 12927542] [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.

IPI

IPI00685910.
IPI00760476.

PIR

I45897.
S05018.

RefSeq

NP_803478.1.

UniGene

Bt.5141

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FGX	X-ray	2.40	A/B	115-402	[»]
1FR8	X-ray	2.40	A/B	115-402	[»]
1NF5	X-ray	2.00	B/D	130-402	[»]
1NHE	X-ray	2.50	B/D	130-402	[»]
1NKH	X-ray	2.00	B/D	130-402	[»]
1NMM	X-ray	2.00	B/D	130-402	[»]
1NQI	X-ray	2.00	B/D	130-402	[»]
1NWG	X-ray	2.32	B/D	131-402	[»]
1O0R	X-ray	2.30	A/B	130-402	[»]
1O23	X-ray	2.32	B/D	130-402	[»]
1OQM	X-ray	2.10	B/D	130-402	[»]
1PZT	X-ray	1.92	A	130-402	[»]
1PZY	X-ray	2.30	B/D	130-402	[»]
1TVY	X-ray	2.30	A/B	130-402	[»]
1TW1	X-ray	2.30	A/B	130-402	[»]
1TW5	X-ray	2.30	A/B	130-402	[»]
1YRO	X-ray	1.90	B/D	130-402	[»]
2FYC	X-ray	2.00	B/D	130-402	[»]
2FYD	X-ray	2.00	B/D	130-400	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P08037.

Protein family/group databases

CAZy

GT7. Glycosyltransferase Family 7.

Genome annotation databases

Ensembl

ENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249; Bos taurus. [Genome view]

GeneID

281781.

KEGG

bta:281781.

Organism-specific databases

CTD

281781.

Phylogenomic databases

eggNOG

maNOG13322.

HOVERGEN

P08037.

InParanoid

P08037.

OMA

NAVVGRC.

OrthoDB

EOG9HTCCH.

Enzyme and pathway databases

BRENDA

2.4.1.22. 251.
2.4.1.38. 251.
2.4.1.90. 251.

Family and domain databases

InterPro

IPR003859. Galactosyl_T_2.
[Graphical view]

PANTHER

PTHR19300. Galactosyl_T_2. 1 hit.

ProtoNet

Search...

Entry information

Entry name

B4GT1_BOVIN

Accession

Primary (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:	February 9, 2010
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)