FUT5
entrez
2527
canonical
uniprot
Q11128
canonical
ensembl
ENSG00000130383
resolver
ensp
ENSP00000252675
resolver
ensp
ENSP00000466880
resolver
enst
ENST00000252675
resolver
enst
ENST00000588525
resolver
genesymbol
FUT5
resolver
hgnc
HGNC:4016
resolver
uniprot
A8K4X2
resolver
uniprot
K7ENC0
resolver
uniprot_entry
FUT5_HUMAN
resolver
uniprot_sec
A8K4X2
resolver
uniprot_sec
K7ENC0
resolver
amino_acid_sequence
MDPLGPAKPQWLWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPNGSRCQDSMATPAHPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSSVYPQADAVIVHHWDIMYNPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFHWRETLRPRSFSWALAFCKACWKLQQESRYQTVRSIAAWFT
uniprot
proteins
ec_number
2.4.1.152
uniprot
proteins
ec_number
2.4.1.65
uniprot
proteins
function
FUNCTION: Catalyzes preferentially the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an oligosaccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates in the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens (PubMed:14718375, PubMed:1740457, PubMed:17604274, PubMed:29593094, PubMed:7721776, PubMed:9737988, PubMed:9737989). Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate (PubMed:17604274, PubMed:7721776). Also catalyzes to a lesser extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosaccharide via an alpha (1,4) linkage (PubMed:14718375, PubMed:1740457, PubMed:17604274, PubMed:7721776, PubMed:9737988). Preferentially catalyzes sialylated type 2 oligosaccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosaccharide acceptors (PubMed:1740457, PubMed:9737989). Lactose-based structures are also acceptor substrates (PubMed:1740457, PubMed:7721776). {ECO:0000269|PubMed:14718375, ECO:0000269|PubMed:1740457, ECO:0000269|PubMed:17604274, ECO:0000269|PubMed:7721776, ECO:0000269|PubMed:9737988, ECO:0000269|PubMed:9737989}.
uniprot
proteins
mass_dalton
42989
uniprot
proteins
mutagenesis
MUTAGEN 86; /note="N->H: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 oligosaccharide acceptor; when associated with I-87 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 oligosaccharide acceptors; when associated with I-87 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with I-87 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with I-87 and S-92."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 87; /note="T->I: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and S-92."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 87; /note="T->K: Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with R-124; E-125 and V-126. Significantly decreases cell-surface expression of VIM2 antigen; when associated with R-124; E-125 and V-126."; /evidence="ECO:0000269|PubMed:17604274"; MUTAGEN 92; /note="P->S: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and I-87. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and I-87."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 101; /note="A->T: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-105; R-110; K-111 and T-118."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 105; /note="N->H: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; R-110; K-111 and T-118."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 110; /note="S->R: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; K-111 and T-118."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 111; /note="S->K: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and T-118."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 118; /note="A->T: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and K-111."; /evidence="ECO:0000269|PubMed:9737988"; MUTAGEN 124; /note="W->A: Decreases both alpha-(1,3)-fucosyltransferase and alpha-(1,4)-fucosyltransferase activity of 50%."; /evidence="ECO:0000269|PubMed:14718375"; MUTAGEN 124; /note="W->R: Increases alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity. Loss of site-specific fucosylation; when associated with E-125 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; E-125 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; E-125 and V-126."; /evidence="ECO:0000269|PubMed:14718375, ECO:0000269|PubMed:17604274"; MUTAGEN 124; /note="W->V: Does not affect alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity."; /evidence="ECO:0000269|PubMed:14718375"; MUTAGEN 125; /note="D->E: Loss of site-specific fucosylation; when associated with R-124 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and V-126."; /evidence="ECO:0000269|PubMed:17604274"; MUTAGEN 126; /note="I->V: Loss of site-specific fucosylation; when associated with R-124 and E-125. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and E-125. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and E-125."; /evidence="ECO:0000269|PubMed:17604274
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:29593094, ECO:0000269|PubMed:7721776}.
uniprot
proteins
protein_family
Glycosyltransferase 10 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14718375
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1740457
uniprot
proteins
pubmed
17604274
uniprot
proteins
pubmed
29593094
uniprot
proteins
pubmed
7650030
uniprot
proteins
pubmed
7721776
uniprot
proteins
pubmed
9737988
uniprot
proteins
pubmed
9737989
uniprot
proteins
sequence_length
374
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi.
uniprot
proteins
transmembrane_region
TRANSMEM 16..34; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins