Reviewed, UniProtKB/Swiss-Prot P14769 (GGTA1_BOVIN)

Names and origin

Protein names

Recommended name:
    N-acetyllactosaminide alpha-1,3-galactosyltransferase
    EC=2.4.1.87
Alternative name(s):
    UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase
      Short name=Galactosyltransferase

Gene names

Name:

GGTA1

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	368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Transfer of galactose from UDP-galactose to an acceptor molecule (R).
Catalytic activity	UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.
Cofactor	Manganese.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Note: Membrane-bound form in trans cisternae of Golgi.
Domain	The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.
Sequence similarities	Belongs to the glycosyltransferase 6 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N-acetyllactosaminide 3-alpha-galactosyltransferase activity Inferred from electronic annotation. Source: EC manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 368

368

N-acetyllactosaminide alpha-1,3-galactosyltransferase

PRO_0000157298

Regions

Topological domain

1 – 6

6

Cytoplasmic Potential

Transmembrane

7 – 22

16

Signal-anchor for type II membrane protein Potential

Topological domain

23 – 368

346

Lumenal Potential

Sites

Metal binding

225

1

Manganese

Metal binding

227

1

Manganese

Amino acid modifications

Glycosylation

293

1

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

365

1

R → K: Strongly reduces catalytic efficiency. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

368

Helix Strand Turn

Details...

Helix

85 – 88

4

Helix

91 – 93

3

Beta strand

106 – 108

3

Helix

115 – 125

11

Beta strand

129 – 135

7

Helix

139 – 154

16

Beta strand

161 – 168

8

Helix

170 – 172

3

Beta strand

182 – 188

7

Helix

195 – 212

18

Helix

214 – 217

4

Beta strand

219 – 224

6

Beta strand

226 – 230

5

Helix

236 – 238

3

Beta strand

241 – 246

6

Turn

248 – 252

5

Helix

255 – 257

3

Beta strand

279 – 286

8

Helix

288 – 307

20

Helix

315 – 326

12

Beta strand

330 – 333

4

Helix

335 – 337

3

Helix

341 – 343

3

Beta strand

353 – 356

4

Helix

361 – 364

4

Sequences

	Sequence		Length	Mass (Da)
	P14769-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 5BC50D6737BDDC33	FASTA	368	43,247
	10 20 30 40 50 60 MNVKGKVILS MLVVSTVIVV FWEYIHSPEG SLFWINPSRN PEVGGSSIQK GWWLPRWFNN 70 80 90 100 110 120 GYHEEDGDIN EEKEQRNEDE SKLKLSDWFN PFKRPEVVTM TKWKAPVVWE GTYNRAVLDN 130 140 150 160 170 180 YYAKQKITVG LTVFAVGRYI EHYLEEFLTS ANKHFMVGHP VIFYIMVDDV SRMPLIELGP 190 200 210 220 230 240 LRSFKVFKIK PEKRWQDISM MRMKTIGEHI VAHIQHEVDF LFCMDVDQVF QDKFGVETLG 250 260 270 280 290 300 ESVAQLQAWW YKADPNDFTY ERRKESAAYI PFGEGDFYYH AAIFGGTPTQ VLNITQECFK 310 320 330 340 350 360 GILKDKKNDI EAQWHDESHL NKYFLLNKPT KILSPEYCWD YHIGLPADIK LVKMSWQTKE YNVVRNNV

References

[1]	"Bovine alpha 1-->3-galactosyltransferase: isolation and characterization of a cDNA clone. Identification of homologous sequences in human genomic DNA." Joziasse D.H., Shaper J.H., van den Eijnden D.H., van Tunen A.J., Shaper N.L. J. Biol. Chem. 264:14290-14297(1989) [PubMed: 2503516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Bovine alpha1,3-galactosyltransferase catalytic domain structure and its relationship with ABO histo-blood group and glycosphingolipid glycosyltransferases." Gastinel L.N., Bignon C., Misra A.K., Hindsgaul O., Shaper J.H., Joziasse D.H. EMBO J. 20:638-649(2001) [PubMed: 11179209] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 80-368, METAL-BINDING.
[3]	"Structure of UDP complex of UDP-galactose:beta-galactoside-alpha-1,3-galactosyltransferase at 1.53-A resolution reveals a conformational change in the catalytically important C-terminus." Boix E., Swaminathan G.J., Zhang Y., Natesh R., Brew K., Acharya K.R. J. Biol. Chem. 276:48608-48614(2001) [PubMed: 11592969] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 80-368, MUTAGENESIS OF ARG-365, METAL-BINDING.
[4]	"Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, alpha-1,3-galactosyltransferase." Boix E., Zhang Y., Swaminathan G.J., Brew K., Acharya K.R. J. Biol. Chem. 277:28310-28318(2002) [PubMed: 12011052] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 80-368, METAL-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J04989 mRNA. Translation: AAA30558.1.

IPI

IPI00710502.

PIR

A44785.

RefSeq

NP_803477.1.

UniGene

Bt.53385

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FG5	X-ray	2.80	N	80-368	[»]
1G8O	X-ray	2.30	A	80-368	[»]
1G93	X-ray	2.50	A	80-368	[»]
1GWV	X-ray	2.50	A/B	80-368	[»]
1GWW	X-ray	1.80	A/B	80-368	[»]
1GX0	X-ray	1.80	A/B	80-368	[»]
1GX4	X-ray	1.46	A/B	80-368	[»]
1K4V	X-ray	1.53	A/B	80-368	[»]
1O7O	X-ray	1.97	A/B	80-368	[»]
1O7Q	X-ray	1.30	A/B	80-368	[»]
1VZT	X-ray	2.00	A/B	80-368	[»]
1VZU	X-ray	1.97	A/B	80-368	[»]
1VZX	X-ray	1.97	A/B	80-368	[»]
2JCJ	X-ray	2.02	A	80-365	[»]
2JCK	X-ray	1.80	A	80-368	[»]
2JCL	X-ray	3.29	A/B	80-368	[»]
2JCO	X-ray	2.57	A	80-368	[»]
2VFZ	X-ray	2.40	A/B	80-368	[»]
2VS3	X-ray	2.20	A/B	80-368	[»]
2VS4	X-ray	1.77	A/B	80-368	[»]
2VS5	X-ray	1.82	A/B	80-365	[»]
2VXL	X-ray	2.70	A	82-358	[»]
2VXM	X-ray	2.82	A/B/C/D	82-354	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT6. Glycosyltransferase Family 6.

Genome annotation databases

Ensembl

ENSBTAG00000012090. Bos taurus. [Contig view]

GeneID

281780.

KEGG

bta:281780.

Phylogenomic databases

HOVERGEN

P14769.

OMA

P14769. AQLQAWW.

Enzyme and pathway databases

BRENDA

2.4.1.87. 251.

Family and domain databases

InterPro

IPR005076. Glyco_trans_6.
[Graphical view]

PANTHER

PTHR10462. Glyco_trans_6. 1 hit.

Pfam

PF03414. Glyco_transf_6. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GGTA1_BOVIN

Accession

Primary (citable) accession number: P14769

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)