FUT2_RAT
ID FUT2_RAT Reviewed; 354 AA.
AC Q10984; O35087; Q9JK44; Q9R275;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 2 {ECO:0000305};
DE AltName: Full=Alpha 1,2-fucosyltransferase;
DE AltName: Full=Alpha 1,2-fucosyltransferase B;
DE AltName: Full=Alpha 1-2 fucosyltransferase;
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 blood group alpha-2-fucosyltransferase;
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000305};
DE EC=2.4.1.69 {ECO:0000269|PubMed:11179967, ECO:0000269|PubMed:11341836};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000305};
DE EC=2.4.1.344 {ECO:0000269|PubMed:11179967, ECO:0000269|PubMed:11341836};
GN Name=Fut2 {ECO:0000312|RGD:2639}; Synonyms=Ftb, Sec1;
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 [MRNA] (ISOFORM 2), FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Fischer;
RX PubMed=11341836; DOI=10.1021/bi0102104;
RA Sherwood A.L., Stroud M.R., Levery S.B., Holmes E.H.;
RT "An amino acid region at the N-terminus of rat hepatoma alpha1-->2
RT fucosyltransferase modulates enzyme activity and interaction with lipids:
RT strong preference for glycosphingolipids containing terminal
RT Galbeta1-->3GalNAc-structures.";
RL Biochemistry 40:5708-5719(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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] (ISOFORM 1).
RC TISSUE=Colon cancer;
RA Soejima M., Wang B., Koda Y., Kimura H.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 222-354 (ISOFORM 2).
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 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:11341836, PubMed:11179967).
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 (By similarity). Creates a
CC soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the
CC H antigen which is an essential substrate for the final step in the
CC soluble ABO blood group antigen synthesis pathway (PubMed:11179967).
CC {ECO:0000250|UniProtKB:Q9JL27, ECO:0000269|PubMed:11179967,
CC ECO:0000269|PubMed:11341836}.
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:11179967, ECO:0000269|PubMed:11341836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665;
CC Evidence={ECO:0000305|PubMed:11341836};
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:11179967, ECO:0000269|PubMed:11341836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669;
CC Evidence={ECO:0000305|PubMed:11341836};
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:0000269|PubMed:11341836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42041;
CC Evidence={ECO:0000305|PubMed:11341836};
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:0000269|PubMed:11341836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42045;
CC Evidence={ECO:0000305|PubMed:11341836};
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=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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33 mM for phenyl-beta-galactose {ECO:0000269|PubMed:11179967};
CC KM=20 mM for N-acetyllactosamine {ECO:0000269|PubMed:11179967};
CC KM=8.3 mM for lacto-N-biose {ECO:0000269|PubMed:11179967};
CC KM=3.8 mM for galacto-N-biose {ECO:0000269|PubMed:11179967};
CC KM=24 uM for GDP-fucose {ECO:0000269|PubMed:11179967};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11179967, ECO:0000269|PubMed:11341836}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q10984-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q10984-2; Sequence=VSP_016526;
CC -!- TISSUE SPECIFICITY: Specifically expressed in gut.
CC {ECO:0000269|PubMed:11179967}.
CC -!- MISCELLANEOUS: In rat, there are three genes (Fut1/Fta, Fut2/Ftb and
CC Ftc) which encode galactoside 2-L-fucosyltransferase. They are
CC expressed in a tissue-specific manner and Ftc may have no enzymatic
CC activity.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF264005; AAF72200.1; -; mRNA.
DR EMBL; AF131238; AAD24469.1; -; Genomic_DNA.
DR EMBL; AB006138; BAA21742.1; -; mRNA.
DR EMBL; L26010; AAB41515.1; -; mRNA.
DR PIR; S46494; S46494.
DR RefSeq; NP_113823.1; NM_031635.1.
DR RefSeq; XP_006229197.1; XM_006229135.3.
DR AlphaFoldDB; Q10984; -.
DR STRING; 10116.ENSRNOP00000028519; -.
DR SwissLipids; SLP:000000796; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; Q10984; 1 site.
DR PaxDb; Q10984; -.
DR PRIDE; Q10984; -.
DR GeneID; 58924; -.
DR KEGG; rno:58924; -.
DR UCSC; RGD:2639; rat. [Q10984-1]
DR CTD; 2524; -.
DR RGD; 2639; Fut2.
DR eggNOG; ENOG502S316; Eukaryota.
DR InParanoid; Q10984; -.
DR OrthoDB; 1006406at2759; -.
DR PhylomeDB; Q10984; -.
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 Reactome; R-RNO-9037629; Lewis blood group biosynthesis.
DR SABIO-RK; Q10984; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q10984; -.
DR Proteomes; UP000002494; 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:0008417; F:fucosyltransferase activity; ISO:RGD.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IDA:RGD.
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; ISO:RGD.
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 Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 2"
FT /id="PRO_0000149114"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 354
FT /note="H -> ALTPACPRSHFHLKAKGVTCYVAGRAF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11341836,
FT ECO:0000303|PubMed:8010942"
FT /id="VSP_016526"
FT CONFLICT 26
FT /note="T -> I (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="V -> G (in Ref. 4; AAB41515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39983 MW; 123E8C8379E8559E CRC64;
MASAQVPFSF PLAHFLIFVF VTSTITHLQQ RIVKLQPLSE KELPMTTQMS SGNTESPEMR
RDSEQHGNGE LRGMFTINSI GRLGNQMGEY ATLFALARMN GRLAFIPASM HNALAPIFRI
SLPVLHSDTA KKIPWQNYHL NDWMEERYRH IPGHFVRFTG YPCSWTFYHH LRPEILKEFT
LHDHVREEAQ AFLRGLRVNG SQPSTFVGVH VRRGDYVHVM PNVWKGVVAD RGYLEKALDM
FRARYSSPVF VVTSNGMAWC RENINASRGD VVFAGNGIEG SPAKDFALLT QCNHTIMTIG
TFGIWAAYLA GGDTIYLANY TLPDSPFLKV FKPEAAFLPE WVGIPADLSP LLKH
