FUT3_BOVIN
ID FUT3_BOVIN Reviewed; 365 AA.
AC Q11126; Q4LDG4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3 {ECO:0000250|UniProtKB:P21217};
DE EC=2.4.1.65 {ECO:0000250|UniProtKB:P21217};
DE AltName: Full=4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase;
DE EC=2.4.1.152 {ECO:0000250|UniProtKB:P21217};
DE AltName: Full=Alpha-3-fucosyltransferase FUT3 {ECO:0000250|UniProtKB:P21217};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:P21217};
DE AltName: Full=Blood group Lewis alpha-4-fucosyltransferase;
DE Short=Lewis FT;
DE AltName: Full=FUTB {ECO:0000303|PubMed:9079712};
DE AltName: Full=Fucosyltransferase 3;
DE AltName: Full=Fucosyltransferase III;
DE Short=FucT-III;
GN Name=FUT3 {ECO:0000250|UniProtKB:P21217};
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 [GENOMIC DNA].
RX PubMed=9079712; DOI=10.1074/jbc.272.13.8764;
RA Oulmouden A., Wierinckx A., Petit J.-M., Costache M., Palcic M.M.,
RA Mollicone R., Oriol R., Julien R.;
RT "Molecular cloning and expression of a bovine alpha(1,3)-fucosyltransferase
RT gene homologous to a putative ancestor gene of the human FUT3-FUT5-FUT6
RT cluster.";
RL J. Biol. Chem. 272:8764-8773(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10555285; DOI=10.1093/oxfordjournals.molbev.a026066;
RA Wierinckx A., Mercier D., Oulmouden A., Petit J.-M., Julien R.;
RT "Complete genomic organization of futb encoding a bovine alpha 3-
RT fucosyltransferase: exons in human orthologous genes emerged from ancestral
RT intronic sequences.";
RL Mol. Biol. Evol. 16:1535-1547(1999).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine
CC (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids
CC and oligosaccharides via an alpha(1,4) linkage, and the subterminal
CC glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-
CC GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of
CC the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal
CC galactose of these acceptors and participates in the blood groups Lewis
CC determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis
CC x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens. Also catalyzes the
CC transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-
CC lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl
CC Lewis a via an alpha(1,4) linkage and therefore may regulate cell
CC surface sialyl Lewis a expression and consequently regulates adhesive
CC properties to E-selectin, cell proliferation and migration. Catalyzes
CC the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an
CC alpha(1,3) linkage, which allows the formation of sialyl-Lewis x
CC structure and therefore may regulate the sialyl-Lewis x surface antigen
CC expression and consequently adhesive properties to E-selectin. Prefers
CC type 1 chain over type 2 acceptors. Type 1 tetrasaccharide is a better
CC acceptor than type 1 disaccharide suggesting that a beta anomeric
CC configuration of GlcNAc in the substrate is preferred. Lewis-positive
CC (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-))
CC individuals have an inactive enzyme. {ECO:0000250|UniProtKB:P21217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-
CC fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304;
CC EC=2.4.1.65; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23629;
CC Evidence={ECO:0000250|UniProtKB:P21217};
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:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-
CC fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+);
CC Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941;
CC EC=2.4.1.152; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258;
CC Evidence={ECO:0000250|UniProtKB:P21217};
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:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + Lc4Cer = a lactoside III(4)-a-Fuc-Lc4Cer +
CC GDP + H(+); Xref=Rhea:RHEA:48824, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90800,
CC ChEBI:CHEBI:90811; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48825;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = GDP + H(+) +
CC III(4)-a-Fuc-Lc4Cer(d18:1(4E)); Xref=Rhea:RHEA:48328,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90292;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48329;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acyl-sphing-4-enine = GDP + H(+) + N-acetyl-alpha-
CC neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-alpha-L-fucosyl-(1->4)-
CC [N-acetyl-alpha-neuraminosyl-(2->6)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)]-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-
CC sphing-4-enine; Xref=Rhea:RHEA:47892, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88079,
CC ChEBI:CHEBI:88089; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47893;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-
CC galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine =
CC GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-
CC (1->3)-alpha-L-fucosyl-(1->4)-[N-acetyl-beta-D-glucosaminyl-(1->3)]-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-
CC enine; Xref=Rhea:RHEA:47888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:88073, ChEBI:CHEBI:88088;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47889;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-
CC D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27707, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:62265; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62845;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc + GDP-beta-L-
CC fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-
CC GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:59440,
CC ChEBI:CHEBI:62259; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62897;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc + GDP-beta-L-
CC fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-
CC GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62900, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62263,
CC ChEBI:CHEBI:62507; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62901;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + GDP-beta-L-
CC fucose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-
CC D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62824, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60152,
CC ChEBI:CHEBI:62287; Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62825;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + lactose = beta-D-galactosyl-(1->4)-[alpha-
CC L-fucosyl-(1->3)]-D-glucose + GDP + H(+); Xref=Rhea:RHEA:62888,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90065;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62889;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative +
CC GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-
CC L-Fuc-(1->4)]-beta-D-GlcNAc derivative + GDP + H(+);
CC Xref=Rhea:RHEA:62904, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:146021, ChEBI:CHEBI:146022;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62905;
CC Evidence={ECO:0000250|UniProtKB:P21217};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P21217}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P21217}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P21217}. Note=Membrane-bound form in trans
CC cisternae of Golgi. {ECO:0000250|UniProtKB:P21217}.
CC -!- TISSUE SPECIFICITY: Liver, kidney, lung and brain.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P21217}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 10 family.
CC {ECO:0000305}.
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DR EMBL; X87810; CAA61079.1; -; Genomic_DNA.
DR EMBL; AJ132772; CAA10771.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11126; -.
DR STRING; 9913.ENSBTAP00000000529; -.
DR CAZy; GT10; Glycosyltransferase Family 10.
DR PaxDb; Q11126; -.
DR eggNOG; KOG2619; Eukaryota.
DR InParanoid; Q11126; -.
DR BRENDA; 2.4.1.65; 908.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0017060; F:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0036065; P:fucosylation; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..365
FT /note="3-galactosyl-N-acetylglucosaminide 4-alpha-L-
FT fucosyltransferase FUT3"
FT /id="PRO_0000221095"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250|UniProtKB:P21217, ECO:0000255"
FT TOPO_DOM 35..365
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 42654 MW; 18715A361B0025D3 CRC64;
MYPPGCAKVK CSWHHCLPGL LLQLLLALCF FSYLRMSQEK PKPKPMWVSE LGAPSQATEG
SSAHLPLRVL LWTWPFNQPV ALSRCSELWP GTADCQLTVN RSEYPQADAV LVHHREVSHR
PQMQLPPSPR PPGQRWVWFS MESPSNCLKL KDLDGYFNLT MSYRRDSDIF MPYGWLEPWP
SQPVETLLNI SAKTKLVAWV VSNWNTDSIR VQYYKLLKPH LQVDVYGRFH TPLPHALMAK
QLSQYKFYLA FENSLHPDYI TEKLWKNALQ AWAVPVVLGP SRVNYEQFLP PKAFIHVEDF
QSPKDLAQYL LALDKDYASY LNYFRWRETL RPRSFSWALM FCKACWKLQQ EPRYQTVPSI
ASWFQ
