FUT7_BOVIN
ID FUT7_BOVIN Reviewed; 342 AA.
AC G3MZR2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 2.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Alpha-(1,3)-fucosyltransferase 7 {ECO:0000250|UniProtKB:Q11130};
DE Short=bfut7 {ECO:0000303|PubMed:22909383};
DE EC=2.4.1.- {ECO:0000269|PubMed:22909383};
DE AltName: Full=Fucosyltransferase 7;
DE AltName: Full=Fucosyltransferase VII {ECO:0000250|UniProtKB:Q11130};
DE Short=Fuc-TVII {ECO:0000250|UniProtKB:Q11130};
DE Short=FucT-VII;
DE AltName: Full=Galactoside 3-L-fucosyltransferase;
DE AltName: Full=Selectin ligand synthase;
GN Name=FUT7 {ECO:0000250|UniProtKB:Q11130};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22909383; DOI=10.1186/1471-2156-13-74;
RA Laporte B., Petit D., Rocha D., Boussaha M., Grohs C., Maftah A.,
RA Petit J.M.;
RT "Characterization of bovine FUT7 furthers understanding of FUT7 evolution
RT in mammals.";
RL BMC Genet. 13:74-74(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a
CC distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a
CC glycolipid-linked sialopolylactosamines chain through an alpha-1,3
CC glycosidic linkage and participates in the final fucosylation step in
CC the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate
CC involved in cell and matrix adhesion during leukocyte trafficking and
CC fertilization (PubMed:22909383). In vitro, also synthesizes sialyl-
CC dimeric-Lex structures, from VIM-2 structures and both di-fucosylated
CC and trifucosylated structures from mono-fucosylated precursors. However
CC does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3
CC fucosylation is present in polylactosamine chain and the fucosylation
CC rate of the internal GlcNAc residues is reduced once fucose has been
CC added to the distal GlcNAc. Also catalyzes the transfer of a fucose
CC from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to
CC produce 6-sulfo sLex mediating significant L-selectin-dependent cell
CC adhesion. Through sialyl-Lewis(x) biosynthesis, can control SELE- and
CC SELP-mediated cell adhesion with leukocytes and allows leukocytes
CC tethering and rolling along the endothelial tissue thereby enabling the
CC leukocytes to accumulate at a site of inflammation. May enhance embryo
CC implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo
CC cells to endometrium. May affect insulin signaling by up-regulating the
CC phosphorylation and expression of some signaling molecules involved in
CC the insulin-signaling pathway through SLe(x) which is present on the
CC glycans of the INSRR alpha subunit (By similarity).
CC {ECO:0000250|UniProtKB:Q11130, ECO:0000269|PubMed:22909383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-
CC N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an
CC alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-
CC GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:136545, ChEBI:CHEBI:139509;
CC Evidence={ECO:0000269|PubMed:22909383};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000305|PubMed:22909383};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-NeuAc-nLc4Cer + GDP-beta-L-fucose =
CC GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48392, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90390, ChEBI:CHEBI:90392;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48393;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = GDP + H(+) + N-
CC acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide;
CC Xref=Rhea:RHEA:48356, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90336, ChEBI:CHEBI:90339;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48357;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-
CC L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-
CC (1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145342, ChEBI:CHEBI:145343;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc6S
CC derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-
CC (1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc6S derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62004, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145344, ChEBI:CHEBI:145345;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62005;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-D-Glc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-D-Glc + GDP + H(+); Xref=Rhea:RHEA:62008,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145346, ChEBI:CHEBI:145347;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62009;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-beta-D-GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-
CC beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-
CC Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62060,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:145400, ChEBI:CHEBI:145401;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62061;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-
CC beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc + GDP-beta-L-fucose = alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-
CC [alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc + GDP + H(+);
CC Xref=Rhea:RHEA:62056, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:145398, ChEBI:CHEBI:145399;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62057;
CC Evidence={ECO:0000250|UniProtKB:Q11130};
CC -!- ACTIVITY REGULATION: Inhibited by NaCl. Inhibited by GDP in a
CC concentration dependent manner, with an IC(50) value of 93 uM. Also
CC inhibited by GMP and GTP. Inhibited by N-ethylmaleimide. Activated by
CC poly(ethylene glycol) by enhancing the thermal stability of FUT7.
CC Activated by Mn2+, Ca2+, and Mg2+. Both panosialin A and B inhibit
CC activity with IC(50) values of 4.8 and 5.3 ug/ml, respectively.
CC Inhibited by gallic acid (GA) and (-)-epigallocatechin gallate (EGCG)
CC in a time-dependent and irreversible manner with IC(50) values of 60
CC and 700 nM, respectively. {ECO:0000250|UniProtKB:Q11130}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q11130}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in thymus, spleen, liver and lung. Highly
CC expressed in the thymus and lower expressed in the lung.
CC {ECO:0000269|PubMed:22909383}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q11130}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family. {ECO:0000255,
CC ECO:0000255|RuleBase:RU003832}.
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DR EMBL; DAAA02032436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3MZR2; -.
DR STRING; 9913.ENSBTAP00000055065; -.
DR PaxDb; G3MZR2; -.
DR Ensembl; ENSBTAT00000066072; ENSBTAP00000055065; ENSBTAG00000046516.
DR VEuPathDB; HostDB:ENSBTAG00000046516; -.
DR VGNC; VGNC:29151; FUT7.
DR eggNOG; KOG2619; Eukaryota.
DR GeneTree; ENSGT00940000161618; -.
DR InParanoid; G3MZR2; -.
DR OMA; WPSKQVP; -.
DR TreeFam; TF316348; -.
DR Reactome; R-BTA-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000046516; Expressed in neutrophil and 72 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0017083; F:4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046920; F:alpha-(1->3)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl.
DR GO; GO:0006672; P:ceramide metabolic process; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0036065; P:fucosylation; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0002522; P:leukocyte migration involved in immune response; IEA:Ensembl.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:0097022; P:lymphocyte migration into lymph node; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISS:UniProtKB.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0060353; P:regulation of cell adhesion molecule production; IEA:Ensembl.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000389; P:regulation of neutrophil extravasation; IEA:Ensembl.
DR GO; GO:0001807; P:regulation of type IV hypersensitivity; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; IEA:Ensembl.
DR Gene3D; 3.40.50.11660; -; 1.
DR InterPro; IPR031481; Glyco_tran_10_N.
DR InterPro; IPR001503; Glyco_trans_10.
DR InterPro; IPR038577; GT10-like_C_sf.
DR PANTHER; PTHR11929; PTHR11929; 1.
DR Pfam; PF17039; Glyco_tran_10_N; 1.
DR Pfam; PF00852; Glyco_transf_10; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..342
FT /note="Alpha-(1,3)-fucosyltransferase 7"
FT /id="PRO_0000449122"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..342
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 68..76
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT DISULFID 211..214
FT /evidence="ECO:0000250|UniProtKB:Q11130"
FT DISULFID 318..321
FT /evidence="ECO:0000250|UniProtKB:Q11130"
SQ SEQUENCE 342 AA; 38746 MW; 1D7983FA601A0A5B CRC64;
MQNAGLSPTP SLRALGGLAM AALLSTVWLW WRLGAAPGGA PAPQPTTTIL VWHWPFASQP
PELPGDTCTR YGVARCRLTV NRSLLAGADA VVFHHRELQT QQARLPLAER PRGQPWVWAS
MESPSHTRGL GRLRGVFNWV LSYRRDSDIF VPYGRLEPRE GPAPPLPAKR GLAAWVVSNF
QKRQRRVQLY RQLALHLRVD VFGRAAGQPL CASCLLRAVA GYRFYLSFEN SEHRDYITEK
FWRNALLAGA VPVVLGPPRA AYEAVAPPDA FVHVDDFGSA RELAAFLTSM NESCYRRYFA
WRDRFRVRLF SDWRERFCAI CARFPQLPRG QVYQDLEGWF QA
