Gene name: FUT7

Uniprot entry:

Q11130

Protein names:

Alpha-(1,3)-fucosyltransferase 7 (EC 2.4.1.-) (Fucosyltransferase 7) (Fucosyltransferase VII) (Fuc-TVII) (FucT-VII) (Galactoside 3-L-fucosyltransferase) (Selectin ligand synthase)

Protein sequence:

1_MNNAG 6_ HGPTR 11_ RLRGL 16_ GVLAG 21_ VALLA 26_ ALWLL 31_ WLLGS 36_ APRGT 41_ PAPQP 46_ TITIL 51_ VWHWP 56_ FTDQP 61_ PELPS 66_ DTCTR 71_ YGIAR 76_ CHLSA 81_ NRSLL 86_ ASADA 91_ VVFHH 96_ RELQT 101_ RRSHL 106_ PLAQR 111_ PRGQP 116_ WVWAS 121_ MESPS 126_ HTHGL 131_ SHLRG 136_ IFNWV 141_ LSYRR 146_ DSDIF 151_ VPYGR 156_ LEPHW 161_ GPSPP 166_ LPAKS 171_ RVAAW 176_ VVSNF 181_ QERQL 186_ RARLY 191_ RQLAP 196_ HLRVD 201_ VFGRA 206_ NGRPL 211_ CASCL 216_ VPTVA 221_ QYRFY 226_ LSFEN 231_ SQHRD 236_ YITEK 241_ FWRNA 246_ LVAGT 251_ VPVVL 256_ GPPRA 261_ TYEAF 266_ VPADA 271_ FVHVD 276_ DFGSA 281_ RELAA 286_ FLTGM 291_ NESRY 296_ QRFFA 301_ WRDRL 306_ RVRLF 311_ TDWRE 316_ RFCAI 321_ CDRYP 326_ HLPRS 331_ QVYED 336_LEGWF

Protein annotations

Protein functions:

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 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)