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P14769 (GGTA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 115. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfer of galactose from UDP-galactose to an acceptor molecule (R).

Catalytic activity

UDP-alpha-D-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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368N-acetyllactosaminide alpha-1,3-galactosyltransferase
PRO_0000157298

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2216Helical; Signal-anchor for type II membrane protein; Potential
Topological domain23 – 368346Lumenal Potential

Sites

Metal binding2251Manganese
Metal binding2271Manganese

Amino acid modifications

Glycosylation2931N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis3651R → K: Strongly reduces catalytic efficiency. Ref.3

Secondary structure

1 ............................................................ 368
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14769 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 5BC50D6737BDDC33

FASTA36843,247
        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

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) OF 80-368, METAL-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04989 mRNA. Translation: AAA30558.1.
IPIIPI00710502.
PIRA44785.
RefSeqNP_803477.1. NM_177511.2.
UniGeneBt.53385.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FG5X-ray2.80N80-368[»]
1G8OX-ray2.30A80-368[»]
1G93X-ray2.50A80-368[»]
1GWVX-ray2.50A/B80-368[»]
1GWWX-ray1.80A/B80-368[»]
1GX0X-ray1.80A/B80-368[»]
1GX4X-ray1.46A/B80-368[»]
1K4VX-ray1.53A/B80-368[»]
1O7OX-ray1.97A/B80-368[»]
1O7QX-ray1.30A/B80-368[»]
1VZTX-ray2.00A/B80-368[»]
1VZUX-ray1.97A/B80-368[»]
1VZXX-ray1.97A/B80-368[»]
2JCJX-ray2.01A80-365[»]
2JCKX-ray1.80A80-368[»]
2JCLX-ray3.29A/B80-368[»]
2JCOX-ray2.57A80-368[»]
2VFZX-ray2.40A/B80-368[»]
2VS3X-ray2.20A/B80-368[»]
2VS4X-ray1.77A/B80-368[»]
2VS5X-ray1.82A/B80-365[»]
2VXLX-ray2.70A82-358[»]
2VXMX-ray2.82A/B/C/D82-354[»]
2WGZX-ray2.12A/B80-368[»]
ProteinModelPortalP14769.
SMRP14769. Positions 81-367.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000016033.

Protein family/group databases

CAZyGT6. Glycosyltransferase Family 6.

Proteomic databases

PRIDEP14769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000016033; ENSBTAP00000016033; ENSBTAG00000012090.
GeneID281780.
KEGGbta:281780.

Organism-specific databases

CTD14594.

Phylogenomic databases

eggNOGNOG75444.
GeneTreeENSGT00400000022032.
HOGENOMHOG000234339.
HOVERGENHBG003563.
InParanoidP14769.
KOK00743.
OMAAQLQAWW.
OrthoDBEOG4C5CK3.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressP14769.

Family and domain databases

InterProIPR005076. Glyco_trans_6.
[Graphical view]
PANTHERPTHR10462. PTHR10462. 1 hit.
PfamPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14769.
NextBio20805693.

Entry information

Entry nameGGTA1_BOVIN
AccessionPrimary (citable) accession number: P14769
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 3, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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