FUT2_RABIT
ID FUT2_RABIT Reviewed; 354 AA.
AC Q10983;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=Secretor blood group alpha-2-fucosyltransferase;
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000250|UniProtKB:Q10981};
DE EC=2.4.1.69 {ECO:0000250|UniProtKB:Q9JL27};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000250|UniProtKB:Q10981};
DE EC=2.4.1.344 {ECO:0000250|UniProtKB:Q9JL27};
GN Name=FUT2 {ECO:0000250|UniProtKB:Q10981}; Synonyms=RFT-II, SEC1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7721792; DOI=10.1074/jbc.270.15.8844;
RA Hitoshi S., Kusunoki S., Kanazawa I., Tsuji S.;
RT "Molecular cloning and expression of two types of rabbit beta-galactoside
RT alpha 1,2-fucosyltransferase.";
RL J. Biol. Chem. 270:8844-8850(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:7721792). Preferentially fucosylates
CC gangliosides GA1 and GM1 in the antrum, cecum and colon and in the
CC female reproductive organs. Fucosylated host glycoproteins or
CC glycolipids mediate interaction with intestinal microbiota influencing
CC its composition (By similarity). 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 (PubMed:7721792).
CC {ECO:0000250|UniProtKB:Q9JL27, ECO:0000269|PubMed:7721792}.
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:7721792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665;
CC Evidence={ECO:0000305|PubMed:7721792};
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:7721792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669;
CC Evidence={ECO:0000305|PubMed:7721792};
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:7721792}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-
CC pass type II membrane protein. Note=Membrane-bound form in trans
CC cisternae of Golgi.
CC -!- TISSUE SPECIFICITY: Salivary and lactating mammary glands.
CC {ECO:0000269|PubMed:7721792}.
CC -!- MISCELLANEOUS: There are three genes (Fut1, Fut2 and Fut3) which encode
CC galactoside 2-L-fucosyltransferase in rabbit. They are expressed in a
CC tissue-specific manner.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
CC {ECO:0000305}.
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DR EMBL; X80225; CAA56512.1; -; mRNA.
DR PIR; B56392; B56392.
DR RefSeq; NP_001075871.1; NM_001082402.1.
DR AlphaFoldDB; Q10983; -.
DR STRING; 9986.ENSOCUP00000018371; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GeneID; 100009290; -.
DR KEGG; ocu:100009290; -.
DR CTD; 100009290; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR InParanoid; Q10983; -.
DR OrthoDB; 1006406at2759; -.
DR BRENDA; 2.4.1.69; 1749.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001811; 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; ISS: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; ISS:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..354
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 2"
FT /id="PRO_0000149113"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 40035 MW; 1E2B831F9DA6CCB4 CRC64;
MRFAPDYVLC PPTATRRLRA THPSVSTIYF LFTIFVVSTV FHCHQRLALV PAPWAYSARV
VVVPGHLPRE GMWTINAMGR LGNQMGEYAT LYALAKENGR PAYIPAQMHS TLAPIFRISL
PVLHSSTASR VPWQNYHLND WMEERYRHIP VPYVRLTGYP CSWTFYHHLR HEILREFTLH
DHVREEAQAF LRGLRVNGSR PSTFVGVHVR RGDYVRVMPQ VWKGVVADRG YLEQALDWFR
APTAPPVFVV TSNGMAWCRE NIDASRGDVV FAGNGLEGSP AKDFALLTQC NHTVMTIGTF
GFWAAYLTGG DTVYLANYTA PDSPFHLVFK PEAAFLPEWV GITANMGRAL WSGL
