FUT1_RAT
ID FUT1_RAT Reviewed; 376 AA.
AC Q10980; Q549F8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1 {ECO:0000305};
DE AltName: Full=Alpha 1,2-fucosyltransferase A;
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:0000312|RGD:2638}; Synonyms=Fta;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Colon cancer;
RA Soejima M., Wang B., Koda Y., Kimura H.;
RT "Two distinct rat GDP-L-fucose:beta-D-galactoside 2-alpha-L-
RT fucosyltransferase genes.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=BDIX;
RX PubMed=11179967; DOI=10.1046/j.1432-1327.2001.01962.x;
RA Bureau V., Marionneau S., Cailleau-Thomas A., Le Moullac-Vaidye B.,
RA Liehr T., Le Pendu J.;
RT "Comparison of the three rat GDP-L-fucose:beta-D-galactoside 2-alpha-L-
RT fucosyltransferases FTA, FTB and FTC.";
RL Eur. J. Biochem. 268:1006-1019(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 169-310.
RC STRAIN=BDIX;
RX PubMed=8010942; DOI=10.1042/bj3000623;
RA Piau J.-P., Labarriere N., Dabouis G., Denis M.G.;
RT "Evidence for two distinct alpha(1,2)-fucosyltransferase genes
RT differentially expressed throughout the rat colon.";
RL Biochem. J. 300:623-626(1994).
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 with expression restricted to cells of mesodermal or
CC endodermal origin respectively.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; AB015637; BAA31130.1; -; Genomic_DNA.
DR EMBL; AB006137; BAA21741.1; -; mRNA.
DR EMBL; AF131237; AAD24468.1; -; Genomic_DNA.
DR EMBL; L26009; AAB41514.1; -; mRNA.
DR PIR; S51582; S51582.
DR RefSeq; NP_112515.1; NM_031236.1.
DR RefSeq; XP_008757642.1; XM_008759420.2.
DR AlphaFoldDB; Q10980; -.
DR STRING; 10116.ENSRNOP00000028494; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; Q10980; 3 sites.
DR iPTMnet; Q10980; -.
DR PhosphoSitePlus; Q10980; -.
DR PaxDb; Q10980; -.
DR Ensembl; ENSRNOT00000028494; ENSRNOP00000028494; ENSRNOG00000020995.
DR GeneID; 81919; -.
DR KEGG; rno:81919; -.
DR UCSC; RGD:2638; rat.
DR CTD; 2523; -.
DR RGD; 2638; Fut1.
DR eggNOG; ENOG502S316; Eukaryota.
DR GeneTree; ENSGT00390000001450; -.
DR HOGENOM; CLU_043399_0_1_1; -.
DR InParanoid; Q10980; -.
DR OMA; MWPPSHR; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; Q10980; -.
DR TreeFam; TF315810; -.
DR BRENDA; 2.4.1.344; 5301.
DR BRENDA; 2.4.1.69; 5301.
DR Reactome; R-RNO-9033807; ABO blood group biosynthesis.
DR SABIO-RK; Q10980; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q10980; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020995; Expressed in pancreas and 12 other tissues.
DR Genevisible; Q10980; RN.
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; ISO:RGD.
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..376
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 1"
FT /id="PRO_0000149102"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 376 AA; 42417 MW; C350C737C758B7F8 CRC64;
MWTPSRKQLC LAFLSVCVLS AGSFFFHLNG GNFFQNALTF SVLCPDYHLL KSPVAMVCLP
YPSNASSGSP SCPEQSLLSG TWTITPGGRF GNQMGQYATL LALAQLNGRR AFIQPEMHTT
LAPVFRISLP VLDPEVDSLT PWQHLVLHDW MSEEYSHLED PFLKLSGFPC SWTFFHHLRE
QIRREFTLHD HLREDAQRLL SGLRIGPAGI RPRTYVGVHV RRGDYLEVMP NRWKGVVGDR
AYLQKAMDWF RARHKDPIFV VTSNGMRWCL ENIDTSHGDV VFAGNGQEGT PGKDFALLTQ
CNHTIMTIGT FGFWAAYLAG GDTVYLANFT LPDSEFLKIF RPKAAFLPEW VGINADLSPL
QAQFDPWETD SLFRLA
