FUT2_BOVIN
ID FUT2_BOVIN Reviewed; 344 AA.
AC Q28113;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 2 {ECO:0000250|UniProtKB:Q10981};
DE AltName: Full=Alpha(1,2)FT 2;
DE AltName: Full=Fucosyltransferase 2;
DE AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2;
DE AltName: Full=Secretor factor;
DE Short=Se {ECO:0000303|PubMed:10814703};
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000250|UniProtKB:Q10981};
DE EC=2.4.1.69 {ECO:0000250|UniProtKB:Q9JL27};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000250|UniProtKB:Q10981};
DE EC=2.4.1.344 {ECO:0000250|UniProtKB:Q9JL27};
GN Name=FUT2 {ECO:0000250|UniProtKB:Q10981};
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].
RA Petit J.-M.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=10814703; DOI=10.1093/glycob/10.6.611;
RA Barreaud J.P., Saunier K., Souchaire J., Delourme D., Oulmouden A.,
RA Oriol R., Leveziel H., Julien R., Petit J.M.;
RT "Three bovine alpha2-fucosyltransferase genes encode enzymes that
RT preferentially transfer fucose on Galbeta1-3GalNAc acceptor substrates.";
RL Glycobiology 10:611-621(2000).
RN [3]
RP FUNCTION.
RX PubMed=20506485; DOI=10.1002/jcb.22692;
RA Palumberi D., Aldi S., Ermini L., Ziche M., Finetti F., Donnini S.,
RA Rosati F.;
RT "RNA-mediated gene silencing of FUT1 and FUT2 influences expression and
RT activities of bovine and human fucosylated nucleolin and inhibits cell
RT adhesion and proliferation.";
RL J. Cell. Biochem. 111:229-238(2010).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-
CC linked glycans chains of cell surface glycoproteins and glycolipids and
CC the resulting epitope regulates several processes such as cell-cell
CC interaction including host-microbe interaction, cell surface expression
CC and cell proliferation (PubMed:10814703). Preferentially fucosylates
CC gangliosides GA1 and GM1 in the antrum, cecum and colon and in the
CC female reproductive organs. Fucosylated host glycoproteins or
CC glycolipids mediate interaction with intestinal microbiota influencing
CC its composition (By similarity). Creates a soluble precursor
CC oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is
CC an essential substrate for the final step in the soluble ABO blood
CC group antigen synthesis pathway (PubMed:20506485).
CC {ECO:0000250|UniProtKB:Q9JL27, ECO:0000269|PubMed:10814703,
CC ECO:0000269|PubMed:20506485}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->3)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50664,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:133506, ChEBI:CHEBI:133509; EC=2.4.1.69;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + GDP-beta-L-fucose = an alpha-L-Fuc-(1->2)-beta-D-Gal-
CC (1->4)-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:50668,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:133507, ChEBI:CHEBI:133510; EC=2.4.1.344;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM1 + GDP-beta-L-fucose = ganglioside Fuc-GM1 +
CC GDP + H(+); Xref=Rhea:RHEA:48292, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82639,
CC ChEBI:CHEBI:90189; Evidence={ECO:0000269|PubMed:10814703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC Evidence={ECO:0000305|PubMed:10814703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer + GDP-beta-L-fucose = a neolactoside
CC IV(2)-alpha-Fuc-nLc4Cer + GDP + H(+); Xref=Rhea:RHEA:48800,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:90376, ChEBI:CHEBI:90803;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48801;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + GDP-beta-L-fucose = a
CC neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + GDP + H(+);
CC Xref=Rhea:RHEA:48304, ChEBI:CHEBI:15378, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:28691, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GA1 + GDP-beta-L-fucose = ganglioside Fuc-GA1 +
CC GDP + H(+); Xref=Rhea:RHEA:48320, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88069,
CC ChEBI:CHEBI:90262; Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + Lc4Cer = alpha-L-fucosyl-(1->2)-beta-D-
CC galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + GDP + H(+);
CC Xref=Rhea:RHEA:48792, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90800, ChEBI:CHEBI:90802;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48793;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
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 = alpha-L-
CC fucosyl-(1->2)- beta-D-galactosyl-(1->3)-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-
CC (1<->1')-N-acylsphing-4-enine + GDP + H(+); Xref=Rhea:RHEA:32175,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:28743,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189; EC=2.4.1.69;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GD1b + GDP-beta-L-fucose = ganglioside Fuc-GD1b +
CC GDP + H(+); Xref=Rhea:RHEA:48324, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:82939,
CC ChEBI:CHEBI:90265; Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48325;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM1 (d18:1(4E)) + GDP-beta-L-fucose =
CC gangliosideFuc-GM1 (d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:42040,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:77709, ChEBI:CHEBI:78607;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42041;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-beta-L-fucose + globoside GalGb4Cer (d18:1(4E)) = GDP +
CC globoside Globo-H (d18:1(4E)) + H(+); Xref=Rhea:RHEA:42044,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:62571, ChEBI:CHEBI:62649;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42045;
CC Evidence={ECO:0000250|UniProtKB:Q10984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lactoside III(4)-a-Fuc-Lc4Cer + GDP-beta-L-fucose = a
CC lactoside IV(2),III(4)-a-[Fuc]2-Lc4Cer + GDP + H(+);
CC Xref=Rhea:RHEA:62616, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273,
CC ChEBI:CHEBI:58189, ChEBI:CHEBI:90811, ChEBI:CHEBI:142612;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62617;
CC Evidence={ECO:0000250|UniProtKB:Q9JL27};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-galactosamine + GDP-beta-
CC L-fucose = alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-
CC D-galactosamine + GDP + H(+); Xref=Rhea:RHEA:62964,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:84728, ChEBI:CHEBI:546807;
CC Evidence={ECO:0000269|PubMed:10814703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965;
CC Evidence={ECO:0000305|PubMed:10814703};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 uM for galacto-N-biose {ECO:0000269|PubMed:10814703};
CC KM=1.42 uM for GM1 {ECO:0000269|PubMed:10814703};
CC Vmax=15.6 pmol/min/mg enzyme towards galacto-N-biose
CC {ECO:0000269|PubMed:10814703};
CC Vmax=31.1 pmol/min/mg enzyme towards GM1
CC {ECO:0000269|PubMed:10814703};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9JL27}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, lung, intestin and
CC kidney. {ECO:0000269|PubMed:10814703}.
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DR EMBL; X99620; CAA67931.1; -; Genomic_DNA.
DR RefSeq; NP_803466.1; NM_177500.1.
DR AlphaFoldDB; Q28113; -.
DR STRING; 9913.ENSBTAP00000028720; -.
DR SwissLipids; SLP:000001422; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR PaxDb; Q28113; -.
DR GeneID; 281175; -.
DR KEGG; bta:281175; -.
DR CTD; 2524; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR InParanoid; Q28113; -.
DR OrthoDB; 1006406at2759; -.
DR BRENDA; 2.4.1.69; 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:0031127; F:alpha-(1,2)-fucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0036065; P:fucosylation; IDA:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; IMP:UniProtKB.
DR InterPro; IPR002516; Glyco_trans_11.
DR PANTHER; PTHR11927; PTHR11927; 1.
DR Pfam; PF01531; Glyco_transf_11; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..344
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 2"
FT /id="PRO_0000149106"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..344
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 344 AA; 39320 MW; F35AC33F1B7B9F68 CRC64;
MFSTQTFFFF PTAPFILFVF TASTIFHLHQ RLEKMQPTWE LEALEPATME TPSRPQPRPQ
LKGMWTINAI GRLGNQMGEY ATLYALAKMN GRAAFIPPQM HSTLAPIFRI TLPVLHDATA
RSVPWQNYHL NDWMEEQYRH IPGEYVRLTG YPCSWTFYHH LRAEILQEFT LHAHVREEAQ
NFLRGLRVNG SRPSTYVGVH VRRGDYVHVM PNVWKGVVAD RRYLEQALDW FRARYSAPIF
VVSSNGMAWC RENINASRGD VVFAGNGNEG SPAKDFALLT QCNHTIMTIG TFGIWAAYLA
GGETIYLANY TLPDSPFLKI FKPEAAFLPK WIGIPADLSP LLKH
