FUT1_BOVIN
ID FUT1_BOVIN Reviewed; 360 AA.
AC F6Q1T7; Q9TTY7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1 {ECO:0000250|UniProtKB:P19526};
DE AltName: Full=Alpha(1,2)FT 1;
DE AltName: Full=Blood group H alpha 2-fucosyltransferase;
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 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], CATALYTIC ACTIVITY, FUNCTION, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11606704; DOI=10.1093/oxfordjournals.molbev.a003749;
RA Saunier K., Barreaud J.P., Eggen A., Oriol R., Leveziel H., Julien R.,
RA Petit J.-M.;
RT "Organization of the bovine alpha 2-fucosyltransferase gene cluster
RT suggests that the Sec1 gene might have been shaped through a nonautonomous
RT L1-retrotransposition event within the same locus.";
RL Mol. Biol. Evol. 18:2083-2091(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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 (PubMed:10814703). H antigen is essential for
CC maturation of the glomerular layer of the main olfactory bulb, in cell
CC migration and early cell-cell contacts during tumor associated
CC angiogenesis (By similarity). Preferentially fucosylates soluble
CC lactose and to a lesser extent, fucosylates glycolipids gangliosides
CC GA1 and GM1a (PubMed:10814703). {ECO:0000250|UniProtKB:O09160,
CC ECO:0000269|PubMed:10814703}.
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 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=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=0.26 uM for Galacto-N-biose {ECO:0000269|PubMed:10814703};
CC KM=1.29 uM for ganglioside GM1a {ECO:0000269|PubMed:10814703};
CC Vmax=48.6 pmol/min/mg enzyme towards Galacto-N-biose
CC {ECO:0000269|PubMed:10814703};
CC Vmax=58.5 pmol/min/mg enzyme towards ganglioside GM1a
CC {ECO:0000269|PubMed:10814703};
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 -!- TISSUE SPECIFICITY: Expressed in brain, intestine and kidney.
CC {ECO:0000269|PubMed:10814703}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; AF186465; AAF07933.1; -; Genomic_DNA.
DR EMBL; AH011099; AAL06321.1; -; mRNA.
DR EMBL; DAAA02047467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6Q1T7; -.
DR SwissLipids; SLP:000001421; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR Ensembl; ENSBTAT00000023560; ENSBTAP00000023560; ENSBTAG00000023374.
DR VEuPathDB; HostDB:ENSBTAG00000023374; -.
DR VGNC; VGNC:49145; FUT1.
DR GeneTree; ENSGT00390000001450; -.
DR Reactome; R-BTA-9033807; ABO blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000023374; Expressed in urinary bladder and 90 other tissues.
DR ExpressionAtlas; F6Q1T7; baseline and differential.
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: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; IEA:UniProtKB-UniPathway.
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..360
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 1"
FT /id="PRO_0000449792"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..27
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..360
FT /note="Lumenal"
FT /evidence="ECO:0000305"
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 CONFLICT 7
FT /note="H -> R (in Ref. 1; AAF07933 and 2; AAL06321)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="L -> V (in Ref. 1; AAF07933 and 2; AAL06321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 40754 MW; 6DA4A4027609B904 CRC64;
MWAPGHHHLC LIFLLTCVFA CVFFLLIHQN LFHSGLDLFL PCPDRSRVRS PVAILCLSGT
LMNPNATFTC PRHSASVSGT WTIDPKGRFG NQMGQYATLL ALAQLNGRQA FIQPSMHAVL
APVFRITLPV LAPEVDRHAP WQELELHDWM SEEYAHLKEP WLKLTGFPCS WTFFHHLRDQ
IRSEFTLHEH LRQEAQRSLS GLRFPRTGGR PSTFVGVHVR RGDYLQVMPL HWKGVVGDRA
YLQQAMDWFR ARHKAPIFVV TSNGMKWCRE NIDTSRGDVI FAGDGQEGAP NKDFALLTQC
NHTIMTIGTF GFWAAYLAGG DTIYLANFTL PDSSFLKIFK PEAAFLPEWV GINADLSPLQ
