Fut7
entrez
14347
canonical
uniprot
Q11131
canonical
ensembl
ENSMUSG00000036587
resolver
ensp
ENSMUSP00000039985
resolver
ensp
ENSMUSP00000097895
resolver
ensp
ENSMUSP00000109917
resolver
ensp
ENSMUSP00000237432
resolver
genesymbol
Fut7
resolver
uniprot
E2D0W5
resolver
uniprot
Q0VGH5
resolver
uniprot
Q3SWS0
resolver
uniprot_entry
E2D0W5_MOUSE
resolver
uniprot_entry
FUT7_MOUSE
resolver
uniprot_entry
Q3SWS0_MOUSE
resolver
uniprot_sec
Q0VGH5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by NaCl. Inhibited by GDP in a concentration dependent manner, with an IC(50) value of 93 uM. Also inhibited by GMP and GTP. Inhibited by N-ethylmaleimide. Activated by poly(ethylene glycol) by enhancing the thermal stability of FUT7. Activated by Mn2+, Ca2+, and Mg2+. Both panosialin A and B inhibit activity with IC(50) values of 4.8 and 5.3 ug/ml, respectively. 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. {ECO:0000250|UniProtKB:Q11130}.
uniprot
proteins
amino_acid_sequence
MPTPCPPACLSTPGTHRLLPFPDWKAPSWESRKEATCNSSSPGPWAEPTVQGYHPTRRLRAWGGLAGGATFMVIWFFWLWGSAPGSAPVPQSTLTILIWHWPFTNRPPELPGDTCTRYGMASCRLSANRSLLASADAVVFHHRELQTRQSLLPLDQRPHGQPWVWASMESPSNTHGLHRFRGIFNWVLSYRRDSDIFVPYGRLEPLSGPTSPLPAKSRMAAWVISNFQERQQRAKLYRQLAPHLQVDVFGRASGRPLCANCLLPTLARYRFYLAFENSQHRDYITEKFWRNALAAGAVPVALGPPRATYEAFVPPDAFVHVDDFSSARELAVFLVSMNESRYRGFFAWRDRLRVRLLGDWRERFCTICARYPYLPRSQVYEDLESWFQA
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:10882744, PubMed:11485743, PubMed:11535629, PubMed:12359718, PubMed:15843584, PubMed:8626519, PubMed:8752218). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (By similarity). 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 (By similarity). 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:10894166, 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:10882744, PubMed:11535629, PubMed:15843584, PubMed:8752218). May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q11130, ECO:0000269|PubMed:10882744, ECO:0000269|PubMed:10894166, ECO:0000269|PubMed:11535629, ECO:0000269|PubMed:12359718, ECO:0000269|PubMed:15843584, ECO:0000269|PubMed:8626519, ECO:0000269|PubMed:8752218}.
uniprot
proteins
mass_dalton
44495
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:11485743}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q11130}.
uniprot
proteins
protein_family
Glycosyltransferase 10 family
uniprot
proteins
pubmed
10882744
uniprot
proteins
pubmed
10894166
uniprot
proteins
pubmed
11485743
uniprot
proteins
pubmed
11535629
uniprot
proteins
pubmed
12359718
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15843584
uniprot
proteins
pubmed
8626519
uniprot
proteins
pubmed
8752218
uniprot
proteins
sequence_length
389
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 56..78; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins