FUT6
entrez
2528
canonical
uniprot
P51993
canonical
ensembl
ENSG00000156413
resolver
ensp
ENSP00000286955
resolver
ensp
ENSP00000313398
resolver
ensp
ENSP00000432954
resolver
ensp
ENSP00000521072
resolver
ensp
ENSP00000575078
resolver
ensp
ENSP00000575079
resolver
ensp
ENSP00000575080
resolver
genesymbol
FUT6
resolver
genesymbol_syn
FCT3A
resolver
hgnc
HGNC:4017
resolver
uniprot
A6NEX0
resolver
uniprot
D6W637
resolver
uniprot
Q6P7E6
resolver
uniprot
Q9UND8
resolver
uniprot_entry
FUT6_HUMAN
resolver
uniprot_entry
Q6P7E6_HUMAN
resolver
uniprot_sec
A6NEX0
resolver
uniprot_sec
D6W637
resolver
uniprot_sec
Q9UND8
resolver
amino_acid_sequence
MDPLGPAKPQWSWRCCLTTLLFQLLMAVCFFSYLRVSQDDPTVYPNGSRFPDSTGTPAHSIPLILLWTWPFNKPIALPRCSEMVPGTADCNITADRKVYPQADAVIVHHREVMYNPSAQLPRSPRRQGQRWIWFSMESPSHCWQLKAMDGYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWGPNSARVRYYQSLQAHLKVDVYGRSHKPLPQGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQEESRYQTRGIAAWFT
uniprot
proteins
ec_number
2.4.1.152
uniprot
proteins
function
FUNCTION: [Isoform 1]: 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 or of a distal or internal lactosamine unit of a neutral glycoprotein- or a glycolipid-linked polylactosamines chain through an alpha-1,3 glycosidic linkage and participates in surface expression of the sialyl Lewis X (sLe(x)), Lewis X (Le(x)) and non sialylated VIM2 determinants (PubMed:10728707, PubMed:1339443, PubMed:1520296, PubMed:17604274, PubMed:29593094, PubMed:7650030, PubMed:9363434, PubMed:9451035). Moreover transfers fucose to H-type 2 (Fucalpha1-2Galbeta1-4GlcNAc) chain acceptor substrates and participates in difucosylated sialyl Lewis x determinants (PubMed:1339443, PubMed:17604274). Also fucosylates a polylactosamine substrate having a 6 sulfate modification at the GlcNAc moiety and gives rise to sialyl and non-sialyl 6-sulfo lewis X (PubMed:10728707). Does not have activity towards type 1 ((Galbeta1-3GlcNAc)) and H-type 1 chain (Fucalpha1-2Galbeta1-3GlcNAc) acceptors substrates (PubMed:1339443, PubMed:17604274, PubMed:9363434). {ECO:0000269|PubMed:10728707, ECO:0000269|PubMed:1339443, ECO:0000269|PubMed:1520296, ECO:0000269|PubMed:17604274, ECO:0000269|PubMed:7650030, ECO:0000269|PubMed:9363434, ECO:0000269|PubMed:9451035}.; FUNCTION: [Isoform 2]: Does not have alpha(1,3)-fucosyltransferase activity. {ECO:0000269|PubMed:7650030}.
uniprot
proteins
mass_dalton
41860
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="K->T: Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with W-110; D-111 and I-112. Increases VIM2 glycolipid product; when associated with W-110; D-111 and I-112."; /evidence="ECO:0000269|PubMed:17604274"; MUTAGEN 110; /note="R->W: Reduces dramatically alpha(1,3)fucosyltransferase activity towards type 2 chain acceptors. Loss of site-specific fucosylation leading to generation of approximately equal amounts of VIM2 and sialyl-lewis x. Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; D-111 and I-112. Increases VIM2 glycolipid product; when associated with T-73; D-111 and I-112."; /evidence="ECO:0000269|PubMed:17604274"; MUTAGEN 111; /note="E->D: Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; W-110 and I-112. Increases VIM2 glycolipid product; when associated with T-73; W-110 and I-112."; /evidence="ECO:0000269|PubMed:17604274"; MUTAGEN 112; /note="V->I: Reverse the site-specific fucosylation pattern leading to generation of VIM2 predominantly instead of sialyl-lewis x; when associated with T-73; W-110 and D-111. Increases VIM2 glycolipid product; when associated with T-73; W-110 and D-111."; /evidence="ECO:0000269|PubMed:17604274
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:29593094, ECO:0000269|PubMed:9363434}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:9451035}.; PTM: Proteolytic cleavage releases a secreted glycoform of 43 kDa. {ECO:0000269|PubMed:9451035}.
uniprot
proteins
protein_family
Glycosyltransferase 10 family
uniprot
proteins
pubmed
10728707
uniprot
proteins
pubmed
11102976
uniprot
proteins
pubmed
1339443
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
1520296
uniprot
proteins
pubmed
17604274
uniprot
proteins
pubmed
27535533
uniprot
proteins
pubmed
29593094
uniprot
proteins
pubmed
7650030
uniprot
proteins
pubmed
8175676
uniprot
proteins
pubmed
9363434
uniprot
proteins
pubmed
9451035
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Golgi apparatus {ECO:0000269|PubMed:9451035}. Secreted {ECO:0000269|PubMed:9451035}. Note=Membrane-bound form in trans cisternae of Golgi.
uniprot
proteins
transmembrane_region
TRANSMEM 15..34; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins