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P14769

- GGTA1_BOVIN

UniProt

P14769 - GGTA1_BOVIN

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
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    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

    Manganese.

    Pathwayi

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein galactosylation at cell surface Source: UniProtKB

    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.

    GO - Cellular componenti

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

    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.

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14769.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini23 – 368346LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2216Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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

    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...
    MobiDBi 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: October 1, 2014
    This is version 126 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