FUT2_PIG
ID FUT2_PIG Reviewed; 340 AA.
AC Q10982; O19100; Q29044;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 03-AUG-2022, entry version 119.
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=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000250|UniProtKB:Q10981};
DE EC=2.4.1.69 {ECO:0000269|PubMed:11132149, ECO:0000269|PubMed:7592879};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000250|UniProtKB:Q10981};
DE EC=2.4.1.344 {ECO:0000269|PubMed:11132149, ECO:0000269|PubMed:7592879};
GN Name=FUT2 {ECO:0000250|UniProtKB:Q10981};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9321466; DOI=10.1007/s003359900556;
RA Meijerink E., Fries R., Voegeli P., Masabanda J., Wigger G., Stricker C.,
RA Neuenschwander S., Bertschinger H.U., Stranzinger G.;
RT "Two alpha(1,2) fucosyltransferase genes on porcine chromosome 6q11 are
RT closely linked to the blood group inhibitor (S) and Escherichia coli F18
RT receptor (ECF18R) loci.";
RL Mamm. Genome 8:736-741(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Cohney S., Mouhtouris E., McKenzie I.F.C., Sandrin M.S.;
RT "Molecular cloning and characterization of the pig secretor type
RT alpha(1,2)fucosyltransferase.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Small intestine;
RX PubMed=11132149; DOI=10.1007/s002510000263;
RA Meijerink E., Neuenschwander S., Fries R., Dinter A., Bertschinger H.U.,
RA Stranzinger G., Vogeli P.;
RT "A DNA polymorphism influencing alpha(1,2)fucosyltransferase activity of
RT the pig FUT1 enzyme determines susceptibility of small intestinal
RT epithelium to Escherichia coli F18 adhesion.";
RL Immunogenetics 52:129-136(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 69-334.
RA Petit J.-M.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 69-80; 119-133 AND 316-334, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Submandibular gland;
RX PubMed=7592879; DOI=10.1074/jbc.270.44.26577;
RA Thurin J., Blaszczyk-Thurin M.;
RT "Porcine submaxillary gland GDP-L-fucose: beta-D-galactoside alpha-2-L-
RT fucosyltransferase is likely a counterpart of the human Secretor gene-
RT encoded blood group transferase.";
RL J. Biol. Chem. 270:26577-26580(1995).
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:11132149, PubMed:7592879).
CC Preferentially fucosylates gangliosides GA1 and GM1 in the antrum,
CC cecum and colon and in the female reproductive organs. Fucosylated host
CC glycoproteins or glycolipids mediate interaction with intestinal
CC microbiota influencing its composition. 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JL27, ECO:0000269|PubMed:11132149,
CC ECO:0000269|PubMed:7592879}.
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:0000269|PubMed:11132149, ECO:0000269|PubMed:7592879};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665;
CC Evidence={ECO:0000305|PubMed:11132149, ECO:0000305|PubMed:7592879};
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:0000269|PubMed:11132149, ECO:0000269|PubMed:7592879};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669;
CC Evidence={ECO:0000305|PubMed:11132149, ECO:0000305|PubMed:7592879};
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 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:0000250|UniProtKB:Q9JL27};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
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:0000250|UniProtKB:Q28113};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965;
CC Evidence={ECO:0000250|UniProtKB:Q28113};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11132149, ECO:0000269|PubMed:7592879}.
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}.
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DR EMBL; U70881; AAB81883.1; -; Genomic_DNA.
DR EMBL; AF027304; AAC09170.1; -; Genomic_DNA.
DR EMBL; AF136895; AAF59832.1; -; mRNA.
DR EMBL; X99621; CAA67932.1; -; Genomic_DNA.
DR RefSeq; NP_999234.1; NM_214069.1.
DR AlphaFoldDB; Q10982; -.
DR STRING; 9823.ENSSSCP00000003406; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR PaxDb; Q10982; -.
DR PRIDE; Q10982; -.
DR Ensembl; ENSSSCT00000003489; ENSSSCP00000003406; ENSSSCG00000003145.
DR Ensembl; ENSSSCT00015038280; ENSSSCP00015015187; ENSSSCG00015028901.
DR Ensembl; ENSSSCT00015038335; ENSSSCP00015015215; ENSSSCG00015028901.
DR Ensembl; ENSSSCT00030072738; ENSSSCP00030033192; ENSSSCG00030052217.
DR Ensembl; ENSSSCT00035062272; ENSSSCP00035025143; ENSSSCG00035046820.
DR Ensembl; ENSSSCT00040007308; ENSSSCP00040002891; ENSSSCG00040005533.
DR Ensembl; ENSSSCT00045027680; ENSSSCP00045019150; ENSSSCG00045016268.
DR Ensembl; ENSSSCT00055057143; ENSSSCP00055045711; ENSSSCG00055028807.
DR Ensembl; ENSSSCT00065061497; ENSSSCP00065026650; ENSSSCG00065044954.
DR Ensembl; ENSSSCT00070055875; ENSSSCP00070047466; ENSSSCG00070027851.
DR GeneID; 397139; -.
DR KEGG; ssc:397139; -.
DR CTD; 2524; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR GeneTree; ENSGT00390000001450; -.
DR HOGENOM; CLU_043399_0_1_1; -.
DR InParanoid; Q10982; -.
DR OMA; KGMWTIN; -.
DR TreeFam; TF315810; -.
DR BRENDA; 2.4.1.344; 6170.
DR BRENDA; 2.4.1.69; 6170.
DR Reactome; R-SSC-9033807; ABO blood group biosynthesis.
DR Reactome; R-SSC-9037629; Lewis blood group biosynthesis.
DR SABIO-RK; Q10982; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Chromosome 6.
DR Bgee; ENSSSCG00000003145; Expressed in uterus and 32 other tissues.
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; ISS:UniProtKB.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0036065; P:fucosylation; ISS:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0001936; P:regulation of endothelial cell proliferation; ISS: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 Direct protein sequencing; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lipid metabolism; Membrane; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 2"
FT /id="PRO_0000149111"
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..340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 158
FT /note="R -> H (in Ref. 4; CAA67932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 38987 MW; 0629F1C04FC206AD CRC64;
MLSMQASFFF PTGPFILFVF TASTIFHLQQ RMVKIQPTWE LQMVTQVTTE SPSSPQLKGM
WTINAIGRLG NQMGEYATLY ALARMNGRPA FIPPEMHSTL APIFRITLPV LHASTARRIP
WQNYHLNDWM EERYRHIPGE YVRLTGYPCS WTFYHHLRTE ILREFTLHNH VREEAQDFLR
GLRVNGSRPS TYVGVHVRRG DYVHVMPNVW KGVVADRRYL EQALDWFRAR YRSPVFVVSS
NGMAWCRENI NASRGDVVFA GNGIEGSPAK DFALLTQCNH TVMTIGTFGI WAAYLAGGET
IYLANYTLPD SPFLKLFKPE AAFLPEWIGI EADLSPLLKH
