Q712G6 · FUT7_RAT

  • Protein
    Alpha-(1,3)-fucosyltransferase 7
  • Gene
    Fut7
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization (PubMed:16218937).
In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors. However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc. Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation. May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium. May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (By similarity).

Catalytic activity

  • an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H+
    This reaction proceeds in the forward direction.
  • a neolactoside IV3-alpha-NeuAc-nLc4Cer + GDP-beta-L-fucose = a neolactoside IV3-alpha-NeuNAc,III3-alpha-Fuc-nLc4Cer + GDP + H+
    This reaction proceeds in the forward direction.
  • N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP-beta-L-fucose = N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H+
    This reaction proceeds in the forward direction.
  • an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H+
    This reaction proceeds in the forward direction.
  • an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H+
    This reaction proceeds in the forward direction.
  • alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + GDP + H+
    This reaction proceeds in the forward direction.
  • alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H+
    This reaction proceeds in the forward direction.
  • alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H+
    This reaction proceeds in the forward direction.

Activity regulation

Inhibited by NaCl. Inhibited by GDP in a concentration dependent manner, with an IC50 value of 93 uM. Also inhibited by GMP and GTP. Inhibited by N-ethylmaleimide. Activated by poly(ethylene glycol) by enhancing the thermal stability of FUT7. Activated by Mn2+, Ca2+, and Mg2+. Both panosialin A and B inhibit activity with IC50 values of 4.8 and 5.3 ug/ml, respectively. Inhibited by gallic acid (GA) and --epigallocatechin gallate (EGCG) in a time-dependent and irreversible manner with IC50 values of 60 and 700 nM, respectively.

Pathway

Protein modification; protein glycosylation.

GO annotations

AspectTerm
Cellular ComponentGolgi cisterna membrane
Cellular Componenttrans-Golgi network
Molecular Function4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity
Molecular Functionalpha-(1->3)-fucosyltransferase activity
Molecular Functionfucosyltransferase activity
Biological ProcessCD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation
Biological Processceramide metabolic process
Biological Processembryo implantation
Biological Processfucosylation
Biological Processinflammatory response
Biological Processleukocyte migration involved in immune response
Biological Processleukocyte migration involved in inflammatory response
Biological Processlymphocyte migration into lymph node
Biological Processlymphocyte migration into lymphoid organs
Biological Processpositive regulation of cell adhesion
Biological Processpositive regulation of cell-cell adhesion
Biological Processpositive regulation of leukocyte adhesion to vascular endothelial cell
Biological Processpositive regulation of leukocyte tethering or rolling
Biological Processpositive regulation of neutrophil migration
Biological Processprotein glycosylation
Biological Processregulation of cell adhesion molecule production
Biological Processregulation of cell-cell adhesion
Biological Processregulation of insulin receptor signaling pathway
Biological Processregulation of leukocyte adhesion to vascular endothelial cell
Biological Processregulation of leukocyte cell-cell adhesion
Biological Processregulation of leukocyte tethering or rolling
Biological Processregulation of neutrophil extravasation
Biological Processregulation of type IV hypersensitivity
Biological ProcessT cell migration

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-(1,3)-fucosyltransferase 7
  • EC number
  • Alternative names
    • Fucosyltransferase 7
    • Fucosyltransferase VII
      (Fuc-TVII
      ; FucT-VII)
    • Galactoside 3-L-fucosyltransferase
    • Selectin ligand synthase

Gene names

    • Name
      Fut7

Organism names

  • Taxonomic identifier
  • Strain
    • Brown Norway
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q712G6

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-36Cytoplasmic
Transmembrane37-59Helical; Signal-anchor for type II membrane protein
Topological domain60-370Lumenal

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond.

Type
IDPosition(s)Description
ChainPRO_00004491231-370Alpha-(1,3)-fucosyltransferase 7
Glycosylation86N-linked (GlcNAc...) asparagine
Disulfide bond96↔104
Glycosylation109N-linked (GlcNAc...) asparagine
Disulfide bond239↔242
Glycosylation319N-linked (GlcNAc...) asparagine
Disulfide bond346↔349

Post-translational modification

N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in lymph node and kidney.

Induction

Strongly induced in kidney allograft during rejection.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 10 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    370
  • Mass (Da)
    42,958
  • Last updated
    2004-07-05 v1
  • Checksum
    7CA9F59A01E9B957
MVQGCLCWRGCCDLKTSFPWVTNSRRLWMNCIGCNPVWRLRAWGCLAGGTTLMVIWLFWLLRSVPGGAPAPQPTLTILIWHWPFTNRSPELSSDTCTRYGMASCHLSANRSLLASADAVVFHHRELQTRHSRLPLDQRPHGQPWVWATMESPSNTHGLRHFRGIFNWVLSYRRDSDIFVPYGRLEPFSGPTPPLPAKSRMAAWVVSNFQERQQRAKLYRQLAPHLKVDVFGRASGRPLCPNCLLPTVARYRFYLSFENSQHRDYITEKFWRNALAAGAVPVVLGPPRTTYEAFVPPDAFIHVDDFSSARELAVFLVSMNESRYRGFFAWRDRLRVRLLNDWRERFCTICARYPYLPRSQVYEDLESWFQA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ276068
EMBL· GenBank· DDBJ
CAC81972.2
EMBL· GenBank· DDBJ
mRNA
AABR07051241
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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