FUT9
entrez
10690
canonical
uniprot
Q9Y231
canonical
ensembl
ENSG00000172461
resolver
ensp
ENSP00000302599
resolver
ensp
ENSP00000557240
resolver
ensp
ENSP00000557241
resolver
ensp
ENSP00000557242
resolver
ensp
ENSP00000557243
resolver
ensp
ENSP00000583846
resolver
enst
ENST00000302103
resolver
enst
ENST00000887181
resolver
enst
ENST00000887182
resolver
enst
ENST00000887183
resolver
enst
ENST00000887184
resolver
enst
ENST00000913787
resolver
genesymbol
FUT9
resolver
hgnc
HGNC:4020
resolver
uniprot
Q5Q0U2
resolver
uniprot
Q5T0W4
resolver
uniprot_entry
FUT9_HUMAN
resolver
uniprot_entry
Q5Q0U2_HUMAN
resolver
uniprot_sec
Q5T0W4
resolver
activity_regulation
ACTIVITY REGULATION: Activated by Mn2+. {ECO:0000269|PubMed:18395013}.
uniprot
proteins
amino_acid_sequence
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWIFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDYNSPSELAKYLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
uniprot
proteins
ec_number
2.4.1.152
uniprot
proteins
function
FUNCTION: Catalyzes alpha(1->3) linkage of fucosyl moiety transferred from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2 lactosamine (LacNAc, beta-D-Gal-(1->4)-beta-D-GlcNAc-) glycan attached to glycolipids and N- or O-linked glycoproteins. Fucosylates distal type 2 LacNAc and its fucosylated (H-type 2 LacNAc) and sialylated (sialyl-type 2 LacNAc) derivatives to form Lewis x (Lex) (CD15) and Lewis y (Ley) antigenic epitopes involved in cell adhesion and differentiation (PubMed:10386598, PubMed:10622713, PubMed:11278338, PubMed:12107078, PubMed:16282604, PubMed:17335083, PubMed:18395013, PubMed:23192350, PubMed:23263199, PubMed:29593094, PubMed:37202521). Generates Lex epitopes in the brain, presumably playing a role in the maintenance of neuronal stemness and neurite outgrowth in progenitor neural cells (By similarity) (PubMed:17335083, PubMed:23000574). Fucosylates the internal type 2 LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE (PubMed:23192350). Can also modify milk oligosaccharides, in particular type 2 tetrasaccharide LNnT (PubMed:37202521). {ECO:0000250|UniProtKB:O88819, ECO:0000269|PubMed:10386598, ECO:0000269|PubMed:10622713, ECO:0000269|PubMed:11278338, ECO:0000269|PubMed:12107078, ECO:0000269|PubMed:16282604, ECO:0000269|PubMed:17335083, ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:23000574, ECO:0000269|PubMed:23192350, ECO:0000269|PubMed:23263199, ECO:0000269|PubMed:29593094, ECO:0000269|PubMed:37202521}.
uniprot
proteins
mass_dalton
42071
uniprot
proteins
mutagenesis
MUTAGEN 2..9; /note="Missing: Does not affect glycosylation. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity. Affects subcellular location."; /evidence="ECO:0000269|PubMed:18395013"; MUTAGEN 2..5; /note="Missing: Does not affect glycosylation. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity. Affects subcellular location."; /evidence="ECO:0000269|PubMed:18395013"; MUTAGEN 3; /note="S->A: Does not affect glycosylation; when associated with A-5. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with A-5. Does not affect subcellular location; when associated with A-5."; /evidence="ECO:0000269|PubMed:18395013"; MUTAGEN 5; /note="S->A: Does not affect glycosylation; when associated with A-3. Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with A-3. Does not affect subcellular location; when associated with A-3."; /evidence="ECO:0000269|PubMed:18395013"; MUTAGEN 62; /note="N->Q: Weakly decreases alpha 1,3-fucosyltransferase activity. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-101. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-153. Loss of catalytic efficiency."; /evidence="ECO:0000269|PubMed:23263199"; MUTAGEN 73; /note="F->A: Complete loss of alpha 1,3-fucosyltransferase activity toward LNnT and H-type 2 LacNAc."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 75; /note="Q->A: Decreases catalytic efficiency toward LNnT, H-type 2 LacNAc and type 2 LacNAc by 35-fold, 68-fold and 69-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 101; /note="N->Q: Significantly decreases alpha 1,3-fucosyltransferase activity. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-62. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-153. Loss of catalytic efficiency."; /evidence="ECO:0000269|PubMed:23263199"; MUTAGEN 111; /note="R->A: Decreases catalytic efficiency toward LNnT and H-type 2 LacNAc by 10-fold and 27-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 111; /note="R->W: Decreases catalytic efficiency toward LNnT and H-type 2 LacNAc by 93-fold and 89-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 137; /note="E->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 1180-fold, 2400-fold and 2870-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 137; /note="E->Q: Complete loss of alpha 1,3-fucosyltransferase activity toward LNnT and H-type 2 LacNAc."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 141; /note="H->A: Decreases catalytic efficiency toward LNnT and H-type 2 LacNAc by 57-fold and 97-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 141; /note="H->N: Decreases catalytic efficiency toward LNnT and H-type 2 LacNAc by 5-fold and 8-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 153; /note="N->Q: Almost complete loss of alpha 1,3-fucosyltransferase activity. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-62. Almost complete loss of alpha 1,3-fucosyltransferase activity; when associated with Q-101."; /evidence="ECO:0000269|PubMed:23263199"; MUTAGEN 194; /note="S->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 2180-fold, 296-fold and 458-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 195; /note="N->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 82-fold, 52-fold and 123-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 197; /note="N->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 179-fold, 18-fold and 47-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 200; /note="H->A: Decreases catalytic efficiency toward H-type 2 LacNAc by 2-fold. Decreases catalytic efficiency toward GDP-beta-L-fucose by 4-fold. Does not affect the catalytic efficiency toward LNnT."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 202; /note="R->A,K: Complete loss of alpha 1,3-fucosyltransferase activity toward LNnT and H-type 2 LacNAc."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 228; /note="D->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 39-fold, 9-fold and 25-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 228; /note="D->K: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 19-fold, 3-fold and 19-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 241; /note="Y->A: Decreases expression."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 246; /note="N->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 70-fold, 30-fold and 109-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 252; /note="Y->A: Decreases expression."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 254; /note="T->A: Decreases catalytic efficiency toward LNnT and H-type 2 LacNAc by 270-fold and 394-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 255; /note="E->A: Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 288-fold, 112-fold and 367-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 256; /note="K->A: Complete loss of alpha 1,3-fucosyltransferase activity toward LNnT and H-type 2 LacNAc."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 327; /note="P->F: Decreases catalytic efficiency toward type 2 LacNAc, LNnT and H-type 2 LacNAc by 3320-fold, 1280-fold and 3060-fold, respectively; when associated with S-328 and F-329 del."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 328; /note="R->S: Decreases catalytic efficiency toward type 2 LacNAc, LNnT and H-type 2 LacNAc by 3320-fold, 1280-fold and 3060-fold, respectively; when associated with F-327 and F-329 del."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 329; /note="F->A: Decreases catalytic efficiency toward type 2 LacNAc, LNnT and H-type 2 LacNAc by 369-fold, 90-fold and 421-fold, respectively."; /evidence="ECO:0000269|PubMed:37202521"; MUTAGEN 329; /note="Missing: Decreases catalytic efficiency toward type 2 LacNAc, LNnT and H-type 2 LacNAc by 3320-fold, 1280-fold and 3060-fold, respectively; when associated with F-327 and S-328."; /evidence="ECO:0000269|PubMed:37202521
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:16282604, ECO:0000269|PubMed:29593094}.; PATHWAY: Glycolipid biosynthesis. {ECO:0000250|UniProtKB:O88819}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated with complex-type N-glycans. The glycan alpha-D-Man-(1->3)-beta-D-Man-(1->4)-GlcNAc-(1->4)-GlcNAc is attached at Asn-153. {ECO:0000269|PubMed:18395013, ECO:0000269|PubMed:37202521}.
uniprot
proteins
protein_family
Glycosyltransferase 10 family
uniprot
proteins
pubmed
10386598
uniprot
proteins
pubmed
10622713
uniprot
proteins
pubmed
10929005
uniprot
proteins
pubmed
11278338
uniprot
proteins
pubmed
12107078
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16282604
uniprot
proteins
pubmed
17335083
uniprot
proteins
pubmed
18395013
uniprot
proteins
pubmed
23000574
uniprot
proteins
pubmed
23192350
uniprot
proteins
pubmed
23263199
uniprot
proteins
pubmed
29593094
uniprot
proteins
pubmed
37202521
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:18395013}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O88819}.
uniprot
proteins
transmembrane_region
TRANSMEM 12..32; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins