FUT1_PIG
ID FUT1_PIG Reviewed; 365 AA.
AC Q29043; O19101;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1 {ECO:0000250|UniProtKB:P19526};
DE AltName: Full=Alpha(1,2)FT 1;
DE AltName: Full=Fucosyltransferase 1;
DE AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1;
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000250|UniProtKB:O09160};
DE EC=2.4.1.69 {ECO:0000250|UniProtKB:O09160};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1 {ECO:0000250|UniProtKB:P19526};
DE EC=2.4.1.344 {ECO:0000250|UniProtKB:P19526};
GN Name=FUT1 {ECO:0000250|UniProtKB:P19526};
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=8613146; DOI=10.1007/bf02602660;
RA Cohney S., Mouhtouris E., McKenzie I.F., Sandrin M.S.;
RT "Molecular cloning of the gene coding for pig alpha1-->2
RT fucosyltransferase.";
RL Immunogenetics 44:76-79(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-103 AND GLU-286.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS THR-103 AND GLU-286.
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).
CC -!- FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine
CC diphosphate-beta-L-fucose, to the terminal galactose residue of
CC glycoconjugates through an alpha(1,2) linkage leading to H antigen
CC synthesis that is an intermediate substrate in the synthesis of ABO
CC blood group antigens. H antigen is essential for maturation of the
CC glomerular layer of the main olfactory bulb, in cell migration and
CC early cell-cell contacts during tumor associated angiogenesis (By
CC similarity). Preferentially fucosylates soluble lactose and to a lesser
CC extent fucosylates glycolipids gangliosides GA1 and GM1a (By
CC similarity). {ECO:0000250|UniProtKB:O09160,
CC ECO:0000250|UniProtKB:P19526}.
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:P19526};
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:O09160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48321;
CC Evidence={ECO:0000250|UniProtKB:O09160};
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:O09160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32176;
CC Evidence={ECO:0000250|UniProtKB:O09160};
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:O09160};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48305;
CC Evidence={ECO:0000250|UniProtKB:O09160};
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:F6Q1T7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48293;
CC Evidence={ECO:0000250|UniProtKB:F6Q1T7};
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:F6Q1T7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62965;
CC Evidence={ECO:0000250|UniProtKB:F6Q1T7};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:P19526}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:O09160}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:O09160}. Note=Membrane-bound form in trans
CC cisternae of Golgi. {ECO:0000250|UniProtKB:O09160}.
CC -!- MISCELLANEOUS: There are two genes (Fut1 and Fut2) which encode
CC galactoside 2-L-fucosyltransferase. They are expressed in a tissue-
CC specific manner.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; L50534; AAB02984.1; -; Genomic_DNA.
DR EMBL; U70883; AAB81884.1; -; Genomic_DNA.
DR EMBL; AF136896; AAF59833.1; -; mRNA.
DR RefSeq; NP_999233.1; NM_214068.2.
DR AlphaFoldDB; Q29043; -.
DR STRING; 9823.ENSSSCP00000003400; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR PaxDb; Q29043; -.
DR Ensembl; ENSSSCT00015035435; ENSSSCP00015014100; ENSSSCG00015026684.
DR Ensembl; ENSSSCT00015035542; ENSSSCP00015014142; ENSSSCG00015026684.
DR Ensembl; ENSSSCT00015035552; ENSSSCP00015014146; ENSSSCG00015026684.
DR Ensembl; ENSSSCT00015035584; ENSSSCP00015014160; ENSSSCG00015026684.
DR Ensembl; ENSSSCT00025024193; ENSSSCP00025010233; ENSSSCG00025017841.
DR Ensembl; ENSSSCT00025024203; ENSSSCP00025010241; ENSSSCG00025017841.
DR Ensembl; ENSSSCT00025024218; ENSSSCP00025010247; ENSSSCG00025017841.
DR Ensembl; ENSSSCT00025024242; ENSSSCP00025010254; ENSSSCG00025017841.
DR Ensembl; ENSSSCT00070055868; ENSSSCP00070047459; ENSSSCG00070027846.
DR GeneID; 397138; -.
DR KEGG; ssc:397138; -.
DR CTD; 2523; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR InParanoid; Q29043; -.
DR OrthoDB; 1006406at2759; -.
DR BRENDA; 2.4.1.69; 6170.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 6.
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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0021772; P:olfactory bulb development; ISS:UniProtKB.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1904906; P:positive regulation of endothelial cell-matrix adhesion via fibronectin; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
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 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="Galactoside alpha-(1,2)-fucosyltransferase 1"
FT /id="PRO_0000149100"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..365
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 103
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:11132149,
FT ECO:0000269|PubMed:9321466"
FT VARIANT 286
FT /note="R -> E"
FT /evidence="ECO:0000269|PubMed:11132149,
FT ECO:0000269|PubMed:9321466"
FT CONFLICT 77
FT /note="L -> F (in Ref. 1; AAB02984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 365 AA; 41106 MW; DAFCE77E89A29D75 CRC64;
MWVPSRRHLC LTFLLVCVLA AIFFLNVYQD LFYSGLDLLA LCPDHNVVSS PVAIFCLAGT
PVHPNASDSC PKHPASLSGT WTIYPDGRFG NQMGQYATLL ALAQLNGRQA FIQPAMHAVL
APVFRITLPV LAPEVDRHAP WRELELHDWM SEDYAHLKEP WLKLTGFPCS WTFFHHLREQ
IRSEFTLHDH LRQEAQGVLS QFRLPRTGDR PSTFVGVHVR RGDYLRVMPK RWKGVVGDGA
YLQQAMDWFR ARYEAPVFVV TSNGMEWCRK NIDTSRGDVI FAGDGREAAP ARDFALLVQC
NHTIMTIGTF GFWAAYLAGG DTIYLANFTL PTSSFLKIFK PEAAFLPEWV GINADLSPLQ
MLAGP
