G5EEE1 · FUTE_CAEEL
- ProteinAlpha-(1,3)-fucosyltransferase fut-6
- Genefut-6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids392 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the fucosylation of N-glycans (PubMed:15364955, PubMed:17369288, PubMed:23754284, PubMed:26002521, PubMed:26538210).
Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the distal GlcNAc residue in N-glycans (PubMed:23754284).
Catalyzes the transfer of fucose to Gal-beta-1-4-GlcNAc-alpha-pNP (LN-pNP) and Gal-beta-1-4-GlcNAc-beta-1-3-Gal-beta-1-4-Glc (LNnT) (PubMed:17369288).
Unlike alpha-(1,3)-fucosyltransferase fut-1, does not transfer fucose to Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc-beta-1-Asn (M3), Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (M3F6) and GlcNAc-beta-1-2-Man-alpha-1-3-(GlcNAc-beta-1-2-Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (GnM3F6) (PubMed:17369288).
Preferentially catalyzes the addition of fucose in alpha 1-3 linkage to the distal GlcNAc residue in N-glycans (PubMed:23754284).
Catalyzes the transfer of fucose to Gal-beta-1-4-GlcNAc-alpha-pNP (LN-pNP) and Gal-beta-1-4-GlcNAc-beta-1-3-Gal-beta-1-4-Glc (LNnT) (PubMed:17369288).
Unlike alpha-(1,3)-fucosyltransferase fut-1, does not transfer fucose to Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-GlcNAc-beta-1-Asn (M3), Man-alpha-1-3-(Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4-(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (M3F6) and GlcNAc-beta-1-2-Man-alpha-1-3-(GlcNAc-beta-1-2-Man-alpha-1-6)-Man-beta-1-4-GlcNAc-beta-1-4(Fuc-alpha-1-6)-GlcNAc-beta-1-Asn (GnM3F6) (PubMed:17369288).
Cofactor
Note: Unlike other alpha-(1,3)-fucosyltransferases, appears not to require a divalent metal cation as cofactor.
Activity regulation
Inhibited by divalent metal cations.
Temperature Dependence
Optimum temperature is 23 degrees Celsius. Very low activity at 37 degrees Celsius.
Pathway
Protein modification; protein glycosylation.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi cisterna membrane | |
Molecular Function | alpha-(1->3)-fucosyltransferase activity | |
Molecular Function | fucosyltransferase activity | |
Biological Process | fucosylation | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-(1,3)-fucosyltransferase fut-6
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionG5EEE1
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-12 | Cytoplasmic | ||||
Sequence: MSQIGGATCTWR | ||||||
Transmembrane | 13-35 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: YLGRFVTLGIYASVALFVWYTLV | ||||||
Topological domain | 36-392 | Lumenal | ||||
Sequence: PTRSKHKDSIAINNNNADPATALIPVHTKNVVIYAATKFFGHPITTERFLATCPDVQNYCRITQEESEFDNADAVLFHNADYRGSTDKFKKMKSQRKPGVPYVLWSLESPTNDMFRPDSHMINWTMTYRTDSDVWAPYGTIVKLKNPVEVDLNAIWEGKTKTATWLASNCITQNHRFDLIKKIIDNGFEIDIWGNCGKQVSQCAGVDNQESPCVLELIKPYKFYISMENSNCKDYVTEKFWKALNDRMTIPIVLARKYYKDLGVPDSAYIAVDDYATLDEFLAHVKKVNKEKDLFLSYHQWRKEWKVIIGSGFSGWCTLCNKLQDKDYILKNPKSYKDVAWWHSFEMCNNQIASKYL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype (PubMed:17369288).
Loss of several tetra-fucosylated N-glycans (PubMed:15364955).
Loss of tetra- and tri-fucosylated N-glycans in a fut-8 or fut-1 mutant background (PubMed:26538210).
fut-1, fut-6 and fut-8 triple mutants lack all N-glycan core fucose with only one fucose present in the bisecting galactose, thus resulting in the loss of tetra-, tri- and bi-fucosylated N-glycans (PubMed:26002521).
Loss of several tetra-fucosylated N-glycans (PubMed:15364955).
Loss of tetra- and tri-fucosylated N-glycans in a fut-8 or fut-1 mutant background (PubMed:26538210).
fut-1, fut-6 and fut-8 triple mutants lack all N-glycan core fucose with only one fucose present in the bisecting galactose, thus resulting in the loss of tetra-, tri- and bi-fucosylated N-glycans (PubMed:26002521).
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000438422 | 1-392 | Alpha-(1,3)-fucosyltransferase fut-6 | |||
Sequence: MSQIGGATCTWRYLGRFVTLGIYASVALFVWYTLVPTRSKHKDSIAINNNNADPATALIPVHTKNVVIYAATKFFGHPITTERFLATCPDVQNYCRITQEESEFDNADAVLFHNADYRGSTDKFKKMKSQRKPGVPYVLWSLESPTNDMFRPDSHMINWTMTYRTDSDVWAPYGTIVKLKNPVEVDLNAIWEGKTKTATWLASNCITQNHRFDLIKKIIDNGFEIDIWGNCGKQVSQCAGVDNQESPCVLELIKPYKFYISMENSNCKDYVTEKFWKALNDRMTIPIVLARKYYKDLGVPDSAYIAVDDYATLDEFLAHVKKVNKEKDLFLSYHQWRKEWKVIIGSGFSGWCTLCNKLQDKDYILKNPKSYKDVAWWHSFEMCNNQIASKYL | ||||||
Glycosylation | 158 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length392
- Mass (Da)45,226
- Last updated2011-12-14 v1
- Checksum8B2E9B7D969D3E43
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ745074 EMBL· GenBank· DDBJ | CAG32980.1 EMBL· GenBank· DDBJ | mRNA | ||
BX284602 EMBL· GenBank· DDBJ | CCD69223.1 EMBL· GenBank· DDBJ | Genomic DNA |