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Protein

N-acetyllactosaminide alpha-1,3-galactosyltransferase

Gene

GGTA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. Preferentially glycosylates proteins, can synthesize galactose-alpha(1,3)-galactose on glycoproteins but cannot synthesize the glycolipid called isoglobotrihexosylceramide or isogloboside 3 (iGb3) (By similarity).By similarity

Catalytic activityi

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.

Cofactori

Pathway:iprotein 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi225 – 2251Manganese
Metal bindingi227 – 2271Manganese

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.87. 908.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

Names & Taxonomyi

Protein namesi
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 namesi
Name:GGTA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 11

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2216Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini23 – 368346LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3651R → K: Strongly reduces catalytic efficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368N-acetyllactosaminide alpha-1,3-galactosyltransferasePRO_0000157298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP14769.

Expressioni

Gene expression databases

ExpressionAtlasiP14769. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016033.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi85 – 884Combined sources
Helixi91 – 933Combined sources
Beta strandi95 – 973Combined sources
Beta strandi106 – 1083Combined sources
Turni110 – 1123Combined sources
Helixi115 – 12511Combined sources
Beta strandi129 – 1357Combined sources
Helixi139 – 15416Combined sources
Turni156 – 1583Combined sources
Beta strandi161 – 1688Combined sources
Helixi170 – 1723Combined sources
Beta strandi182 – 1887Combined sources
Helixi195 – 21218Combined sources
Helixi214 – 2174Combined sources
Beta strandi219 – 2246Combined sources
Beta strandi226 – 2305Combined sources
Helixi236 – 2383Combined sources
Beta strandi240 – 2467Combined sources
Turni248 – 2525Combined sources
Helixi255 – 2573Combined sources
Beta strandi279 – 2868Combined sources
Helixi288 – 30720Combined sources
Turni313 – 3153Combined sources
Helixi316 – 32611Combined sources
Beta strandi330 – 3334Combined sources
Helixi335 – 3373Combined sources
Helixi341 – 3433Combined sources
Beta strandi347 – 3504Combined sources
Beta strandi353 – 3564Combined sources
Helixi361 – 3644Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14769.
SMRiP14769. Positions 81-367.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14769.

Family & Domainsi

Domaini

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 similaritiesi

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG75444.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiP14769.
KOiK00743.
OMAiAQLQAWW.
OrthoDBiEOG7SV0VK.
TreeFamiTF330991.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P14769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVKGKVILS MLVVSTVIVV FWEYIHSPEG SLFWINPSRN PEVGGSSIQK
60 70 80 90 100
GWWLPRWFNN GYHEEDGDIN EEKEQRNEDE SKLKLSDWFN PFKRPEVVTM
110 120 130 140 150
TKWKAPVVWE GTYNRAVLDN YYAKQKITVG LTVFAVGRYI EHYLEEFLTS
160 170 180 190 200
ANKHFMVGHP VIFYIMVDDV SRMPLIELGP LRSFKVFKIK PEKRWQDISM
210 220 230 240 250
MRMKTIGEHI VAHIQHEVDF LFCMDVDQVF QDKFGVETLG ESVAQLQAWW
260 270 280 290 300
YKADPNDFTY ERRKESAAYI PFGEGDFYYH AAIFGGTPTQ VLNITQECFK
310 320 330 340 350
GILKDKKNDI EAQWHDESHL NKYFLLNKPT KILSPEYCWD YHIGLPADIK
360
LVKMSWQTKE YNVVRNNV
Length:368
Mass (Da):43,247
Last modified:April 1, 1990 - v1
Checksum:i5BC50D6737BDDC33
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04989 mRNA. Translation: AAA30558.1.
PIRiA44785.
RefSeqiNP_803477.1. NM_177511.2.
XP_005212980.1. XM_005212923.2.
XP_005212981.1. XM_005212924.2.
UniGeneiBt.53385.

Genome annotation databases

EnsembliENSBTAT00000016033; ENSBTAP00000016033; ENSBTAG00000012090.
GeneIDi281780.
KEGGibta:281780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04989 mRNA. Translation: AAA30558.1.
PIRiA44785.
RefSeqiNP_803477.1. NM_177511.2.
XP_005212980.1. XM_005212923.2.
XP_005212981.1. XM_005212924.2.
UniGeneiBt.53385.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP14769.
SMRiP14769. Positions 81-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016033.

Chemistry

BindingDBiP14769.
ChEMBLiCHEMBL2069158.

Protein family/group databases

CAZyiGT6. Glycosyltransferase Family 6.

Proteomic databases

PRIDEiP14769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016033; ENSBTAP00000016033; ENSBTAG00000012090.
GeneIDi281780.
KEGGibta:281780.

Organism-specific databases

CTDi14594.

Phylogenomic databases

eggNOGiNOG75444.
GeneTreeiENSGT00400000022032.
HOGENOMiHOG000234339.
HOVERGENiHBG003563.
InParanoidiP14769.
KOiK00743.
OMAiAQLQAWW.
OrthoDBiEOG7SV0VK.
TreeFamiTF330991.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.87. 908.

Miscellaneous databases

EvolutionaryTraceiP14769.
NextBioi20805693.
PROiP14769.

Gene expression databases

ExpressionAtlasiP14769. baseline and differential.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10462. PTHR10462. 1 hit.
PfamiPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGGTA1_BOVIN
AccessioniPrimary (citable) accession number: P14769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 27, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3

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 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.