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P14769

- GGTA1_BOVIN

UniProt

P14769 - GGTA1_BOVIN

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Protein
N-acetyllactosaminide alpha-1,3-galactosyltransferase
Gene
GGTA1
Organism
Bos taurus (Bovine)
Status
Reviewed - 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.

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

Manganese.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi225 – 2251Manganese
Metal bindingi227 – 2271Manganese

GO - Molecular functioni

  1. N-acetyllactosaminide 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. protein galactosylation at cell surface Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

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: Chromosome 11

Subcellular locationi

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein
Note: Membrane-bound form in trans cisternae of Golgi.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2216Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini23 – 368346Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi cisterna Source: UniProtKB
  2. Golgi cisterna membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
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-galactosyltransferase
PRO_0000157298Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP14769.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016033.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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

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

MNVKGKVILS MLVVSTVIVV FWEYIHSPEG SLFWINPSRN PEVGGSSIQK    50
GWWLPRWFNN GYHEEDGDIN EEKEQRNEDE SKLKLSDWFN PFKRPEVVTM 100
TKWKAPVVWE GTYNRAVLDN YYAKQKITVG LTVFAVGRYI EHYLEEFLTS 150
ANKHFMVGHP VIFYIMVDDV SRMPLIELGP LRSFKVFKIK PEKRWQDISM 200
MRMKTIGEHI VAHIQHEVDF LFCMDVDQVF QDKFGVETLG ESVAQLQAWW 250
YKADPNDFTY ERRKESAAYI PFGEGDFYYH AAIFGGTPTQ VLNITQECFK 300
GILKDKKNDI EAQWHDESHL NKYFLLNKPT KILSPEYCWD YHIGLPADIK 350
LVKMSWQTKE YNVVRNNV 368
Length:368
Mass (Da):43,247
Last modified:April 1, 1990 - v1
Checksum:i5BC50D6737BDDC33
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04989 mRNA. Translation: AAA30558.1.
PIRiA44785.
RefSeqiNP_803477.1. NM_177511.2.
XP_005212980.1. XM_005212923.1.
XP_005212981.1. XM_005212924.1.
XP_005212982.1. XM_005212925.1.
UniGeneiBt.53385.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04989 mRNA. Translation: AAA30558.1 .
PIRi A44785.
RefSeqi NP_803477.1. NM_177511.2.
XP_005212980.1. XM_005212923.1.
XP_005212981.1. XM_005212924.1.
XP_005212982.1. XM_005212925.1.
UniGenei Bt.53385.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2.01 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 [» ]
2WGZ X-ray 2.12 A/B 80-368 [» ]
ProteinModelPortali P14769.
SMRi P14769. Positions 81-367.
ModBasei Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000016033.

Chemistry

ChEMBLi CHEMBL2069158.

Protein family/group databases

CAZyi GT6. Glycosyltransferase Family 6.

Proteomic databases

PRIDEi P14769.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000016033 ; ENSBTAP00000016033 ; ENSBTAG00000012090 .
GeneIDi 281780.
KEGGi bta:281780.

Organism-specific databases

CTDi 14594.

Phylogenomic databases

eggNOGi NOG75444.
GeneTreei ENSGT00400000022032.
HOGENOMi HOG000234339.
HOVERGENi HBG003563.
InParanoidi P14769.
KOi K00743.
OMAi AQLQAWW.
OrthoDBi EOG7SV0VK.
TreeFami TF330991.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

EvolutionaryTracei P14769.
NextBioi 20805693.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR005076. Glyco_trans_6.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR10462. PTHR10462. 1 hit.
Pfami PF03414. Glyco_transf_6. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

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: June 11, 2014
This is version 125 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

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