FUT7
entrez
2529
canonical
uniprot
Q11130
canonical
ensembl
ENSG00000180549
resolver
ensp
ENSP00000318142
resolver
ensp
ENSP00000544375
resolver
enst
ENST00000314412
resolver
enst
ENST00000874316
resolver
genesymbol
FUT7
resolver
hgnc
HGNC:4018
resolver
uniprot
B2R7U7
resolver
uniprot
Q6DK54
resolver
uniprot_entry
FUT7_HUMAN
resolver
uniprot_sec
B2R7U7
resolver
uniprot_sec
Q6DK54
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by NaCl (Probable). Inhibited by GDP in a concentration dependent manner, with an IC(50) value of 93 uM (PubMed:15632313, PubMed:9405391). Also inhibited by GMP and GTP (PubMed:9405391). Inhibited by N-ethylmaleimide (Probable). Activated by poly(ethylene glycol) by enhancing the thermal stability of FUT7 (PubMed:9405391). Activated by Mn2+, Ca2+, and Mg2+ (PubMed:9405391). Both panosialin A and B inhibit activity with IC(50) values of 4.8 and 5.3 ug/ml, respectively (PubMed:10386892). Inhibited by gallic acid (GA) and (-)-epigallocatechin gallate (EGCG) in a time-dependent and irreversible manner with IC(50) values of 60 and 700 nM, respectively (PubMed:15081893). {ECO:0000269|PubMed:10386892, ECO:0000269|PubMed:15081893, ECO:0000269|PubMed:15632313, ECO:0000269|PubMed:9405391, ECO:0000305|PubMed:9405391}.
uniprot
proteins
amino_acid_sequence
MNNAGHGPTRRLRGLGVLAGVALLAALWLLWLLGSAPRGTPAPQPTITILVWHWPFTDQPPELPSDTCTRYGIARCHLSANRSLLASADAVVFHHRELQTRRSHLPLAQRPRGQPWVWASMESPSHTHGLSHLRGIFNWVLSYRRDSDIFVPYGRLEPHWGPSPPLPAKSRVAAWVVSNFQERQLRARLYRQLAPHLRVDVFGRANGRPLCASCLVPTVAQYRFYLSFENSQHRDYITEKFWRNALVAGTVPVVLGPPRATYEAFVPADAFVHVDDFGSARELAAFLTGMNESRYQRFFAWRDRLRVRLFTDWRERFCAICDRYPHLPRSQVYEDLEGWFQA
uniprot
proteins
ec_number
2.4.1.-
uniprot
proteins
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:11404359, PubMed:15632313, PubMed:15926890, PubMed:18402946, PubMed:18553500, PubMed:29593094, PubMed:8207002, PubMed:8666674, PubMed:8752218, PubMed:9299472, PubMed:9405391, PubMed:9461592, PubMed:9473504, PubMed:9499379). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (PubMed:9499379). 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 (PubMed:9473504, PubMed:9499379). 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 (PubMed:10200296, PubMed:8752218). 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 (PubMed:10386892, PubMed:29138114, PubMed:8666674, PubMed:9473504, PubMed:9834120). May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (PubMed:18402946, PubMed:18553500). 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 (PubMed:17229154). {ECO:0000269|PubMed:10200296, ECO:0000269|PubMed:10386892, ECO:0000269|PubMed:11404359, ECO:0000269|PubMed:15632313, ECO:0000269|PubMed:15926890, ECO:0000269|PubMed:17229154, ECO:0000269|PubMed:18402946, ECO:0000269|PubMed:18553500, ECO:0000269|PubMed:29138114, ECO:0000269|PubMed:8207002, ECO:0000269|PubMed:8666674, ECO:0000269|PubMed:8752218, ECO:0000269|PubMed:9299472, ECO:0000269|PubMed:9405391, ECO:0000269|PubMed:9461592, ECO:0000269|PubMed:9473504, ECO:0000269|PubMed:9499379, ECO:0000269|PubMed:9834120}.
uniprot
proteins
mass_dalton
39239
uniprot
proteins
mutagenesis
MUTAGEN 81; /note="N->Q: Impairs glycosylation. Impairs glycosylation; when associated with Q-291. Does not affect SELP and SELL binding on SELPLG. Does not affect SELP and SELL binding on SELPLG; when associated with Q-291. Abolishes alpha-(1,3)-fucosyltransferase activity. Abolishes alpha-(1,3)-fucosyltransferase activity; when associated with Q-291. Fails to synthetises sLe(x) antigens or to generate SELE binding. Fails to synthetises sLe(x) antigens or to generate SELE binding; when associated with Q-291. Does not affect sLe(x) antigens synthesis or SELE binding only in presence of SELPLG and GCNT1; when associated with Q-291."; /evidence="ECO:0000269|PubMed:15926890"; MUTAGEN 291; /note="N->Q: Slightly affects glycosylation. Impairs glycosylation; when associated with Q-81. Does not affect SELP and SELL binding on SELPLG. Does not affect SELP and SELL binding on SELPLG; when associated with Q-81. Abolishes alpha-(1,3)-fucosyltransferase activity. Abolishes alpha-(1,3)-fucosyltransferase activity; when associated with Q-81. Fails to synthetises sLe(x) antigens or to generate SELE binding. Fails to synthetises sLe(x) antigens or to generate SELE binding; when associated with Q-81. Does not affect sLe(x) antigens synthesis or SELE binding only in presence of SELPLG and GCNT1; when associated with Q-81."; /evidence="ECO:0000269|PubMed:15926890
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:8207002}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:15632313}.
uniprot
proteins
protein_family
Glycosyltransferase 10 family
uniprot
proteins
pubmed
10200296
uniprot
proteins
pubmed
10386892
uniprot
proteins
pubmed
11404359
uniprot
proteins
pubmed
11425803
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15081893
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15632313
uniprot
proteins
pubmed
15926890
uniprot
proteins
pubmed
17229154
uniprot
proteins
pubmed
18402946
uniprot
proteins
pubmed
18553500
uniprot
proteins
pubmed
19455659
uniprot
proteins
pubmed
29138114
uniprot
proteins
pubmed
29593094
uniprot
proteins
pubmed
8051184
uniprot
proteins
pubmed
8182079
uniprot
proteins
pubmed
8207002
uniprot
proteins
pubmed
8666674
uniprot
proteins
pubmed
8752218
uniprot
proteins
pubmed
9299472
uniprot
proteins
pubmed
9405391
uniprot
proteins
pubmed
9461592
uniprot
proteins
pubmed
9473504
uniprot
proteins
pubmed
9499379
uniprot
proteins
pubmed
9834120
uniprot
proteins
pubmed
9858509
uniprot
proteins
sequence_length
342
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 15..36; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins