FUT2_HUMAN
ID FUT2_HUMAN Reviewed; 343 AA.
AC Q10981; Q0VAG5; Q14338; Q5D0G2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 2 {ECO:0000305};
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=SE2;
DE AltName: Full=Secretor blood group alpha-2-fucosyltransferase {ECO:0000303|PubMed:7876235};
DE AltName: Full=Secretor factor;
DE Short=Se;
DE AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000305};
DE EC=2.4.1.69 {ECO:0000269|PubMed:7876235};
DE AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT2 {ECO:0000305};
DE EC=2.4.1.344 {ECO:0000269|PubMed:7876235};
GN Name=FUT2 {ECO:0000312|HGNC:HGNC:4013}; Synonyms=SEC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7876235; DOI=10.1074/jbc.270.9.4640;
RA Kelly R.J., Rouquier S., Giorgi D., Lennon G.G., Lowe J.B.;
RT "Sequence and expression of a candidate for the human Secretor blood group
RT alpha(1,2)fucosyltransferase gene (FUT2). Homozygosity for an enzyme-
RT inactivating nonsense mutation commonly correlates with the non-secretor
RT phenotype.";
RL J. Biol. Chem. 270:4640-4649(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-140.
RX PubMed=9219535; DOI=10.1111/j.1432-1033.1997.t01-1-00750.x;
RA Koda Y., Soejima M., Wang B., Kimura H.;
RT "Structure and expression of the gene encoding secretor-type galactoside 2-
RT alpha-L-fucosyltransferase (FUT2).";
RL Eur. J. Biochem. 246:750-755(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-25; CYS-138; ASN-172
RP AND SER-258.
RG SeattleSNPs variation discovery resource;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-140.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-343, AND VARIANT PHE-140.
RX PubMed=8621666; DOI=10.1074/jbc.271.16.9830;
RA Kudo T., Iwasaki H., Nishihara S., Shinya N., Ando T., Narimatsu I.,
RA Narimatsu H.;
RT "Molecular genetic analysis of the human Lewis histo-blood group system.
RT II. Secretor gene inactivation by a novel single missense mutation A385T in
RT Japanese nonsecretor individuals.";
RL J. Biol. Chem. 271:9830-9837(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-343.
RX PubMed=8755920;
RA Koda Y., Soejima M., Liu Y., Kimura H.;
RT "Molecular basis for secretor type alpha(1,2)-fucosyltransferase gene
RT deficiency in a Japanese population: a fusion gene generated by unequal
RT crossover responsible for the enzyme deficiency.";
RL Am. J. Hum. Genet. 59:343-350(1996).
RN [8]
RP FUNCTION.
RX PubMed=8018146; DOI=10.1126/science.8018146;
RA Boren T., Falk P., Roth K.A., Larson G., Normark S.;
RT "Attachment of Helicobacter pylori to human gastric epithelium mediated by
RT blood group antigens.";
RL Science 262:1892-1895(1993).
RN [9]
RP FUNCTION, AND INVOLVEMENT IN RESISTANCE TO NORWALK VIRUS.
RX PubMed=12692541; DOI=10.1038/nm860;
RA Lindesmith L., Moe C., Marionneau S., Ruvoen N., Jiang X., Lindblad L.,
RA Stewart P., LePendu J., Baric R.;
RT "Human susceptibility and resistance to Norwalk virus infection.";
RL Nat. Med. 9:548-553(2003).
RN [10]
RP FUNCTION.
RX PubMed=20506485; DOI=10.1002/jcb.22692;
RA Palumberi D., Aldi S., Ermini L., Ziche M., Finetti F., Donnini S.,
RA Rosati F.;
RT "RNA-mediated gene silencing of FUT1 and FUT2 influences expression and
RT activities of bovine and human fucosylated nucleolin and inhibits cell
RT adhesion and proliferation.";
RL J. Cell. Biochem. 111:229-238(2010).
RN [11]
RP FUNCTION.
RX PubMed=21625510; DOI=10.1371/journal.pone.0020113;
RA Wacklin P., Maekivuokko H., Alakulppi N., Nikkilae J., Tenkanen H.,
RA Raebinae J., Partanen J., Aranko K., Maettoe J.;
RT "Secretor genotype (FUT2 gene) is strongly associated with the composition
RT of Bifidobacteria in the human intestine.";
RL PLoS ONE 6:E20113-E20113(2011).
RN [12]
RP FUNCTION.
RX PubMed=22068912; DOI=10.1073/pnas.1106408108;
RA Rausch P., Rehman A., Kuenzel S., Haesler R., Ott S.J., Schreiber S.,
RA Rosenstiel P., Franke A., Baines J.F.;
RT "Colonic mucosa-associated microbiota is influenced by an interaction of
RT Crohn disease and FUT2 (Secretor) genotype.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:19030-19035(2011).
RN [13]
RP FUNCTION.
RX PubMed=24733310; DOI=10.1371/journal.pone.0094863;
RA Wacklin P., Tuimala J., Nikkilae J., Tims S., Maekivuokko H., Alakulppi N.,
RA Laine P., Rajilic-Stojanovic M., Paulin L., de Vos W.M., Maettoe J.;
RT "Faecal microbiota composition in adults is associated with the FUT2 gene
RT determining the secretor status.";
RL PLoS ONE 9:E94863-E94863(2014).
RN [14]
RP VARIANTS VAL-25; CYS-138 AND ASN-172.
RX PubMed=9760207; DOI=10.1007/s004390050808;
RA Liu Y., Koda Y., Soejima M., Pang H., Schlaphoff T., du Toit E.D.,
RA Kimura H.;
RT "Extensive polymorphism of the FUT2 gene in an African (Xhosa) population
RT of South Africa.";
RL Hum. Genet. 103:204-210(1998).
RN [15]
RP INVOLVEMENT IN B12QTL1.
RX PubMed=18776911; DOI=10.1038/ng.210;
RA Hazra A., Kraft P., Selhub J., Giovannucci E.L., Thomas G., Hoover R.N.,
RA Chanock S.J., Hunter D.J.;
RT "Common variants of FUT2 are associated with plasma vitamin B12 levels.";
RL Nat. Genet. 40:1160-1162(2008).
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:7876235, PubMed:8018146,
CC PubMed:12692541). Preferentially fucosylates gangliosides GA1 and GM1
CC in the antrum, cecum and colon and in the female reproductive organs
CC (By similarity). Fucosylated host glycoproteins or glycolipids mediate
CC interaction with intestinal microbiota influencing its composition
CC (PubMed:22068912, PubMed:21625510, PubMed:24733310). Creates a soluble
CC precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H
CC antigen which is an essential substrate for the final step in the
CC soluble ABO blood group antigen synthesis pathway (PubMed:7876235).
CC {ECO:0000250|UniProtKB:Q9JL27, ECO:0000269|PubMed:12692541,
CC ECO:0000269|PubMed:21625510, ECO:0000269|PubMed:22068912,
CC ECO:0000269|PubMed:24733310, ECO:0000269|PubMed:7876235,
CC ECO:0000269|PubMed:8018146}.
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:7876235};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50665;
CC Evidence={ECO:0000269|PubMed:7876235};
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:7876235};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50669;
CC Evidence={ECO:0000305|PubMed:7876235};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.5 mM for phenyl-beta-D-galactoside
CC {ECO:0000269|PubMed:7876235};
CC KM=3.6 mM for lacto-N-biose {ECO:0000269|PubMed:7876235};
CC KM=3.8 mM for N-acetyllactosamine {ECO:0000269|PubMed:7876235};
CC KM=197 uM for GDP-fucose {ECO:0000269|PubMed:7876235};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:7876235}.
CC -!- INTERACTION:
CC Q10981; P23560-2: BDNF; NbExp=3; IntAct=EBI-9090702, EBI-12275524;
CC Q10981; P27797: CALR; NbExp=3; IntAct=EBI-9090702, EBI-1049597;
CC Q10981; P36957: DLST; NbExp=3; IntAct=EBI-9090702, EBI-351007;
CC Q10981; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-9090702, EBI-1055945;
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: Small intestine, colon and lung.
CC -!- POLYMORPHISM: Three alleles have been identified in the Japanese
CC population: Se1, Se2, and Sej. {ECO:0000269|PubMed:8621666}.
CC -!- POLYMORPHISM: Common polymorphisms in FUT2 define the vitamin B12
CC plasma level quantitative trait locus 1 (B12QTL1) [MIM:612542]. Vitamin
CC B12 found in meat and milk products is necessary for the formation of
CC red blood cells, DNA synthesis during cell division, and maintenance of
CC the myelin nerve sheath, among other functions. Deficiency in vitamin
CC B12, clinically associated with pernicious anemia, cardiovascular
CC disease, cancer, and neurodegenerative disorders, is often related to
CC poor intestinal B12 absorption rather than direct dietary deficiency.
CC {ECO:0000269|PubMed:18776911}.
CC -!- POLYMORPHISM: Genetic variation in FUT2 results in the non-secretor
CC phenotype which gives rise to non-functional FUT2, resulting in a lack
CC of the H type-1 oligosaccharide ligand in secretions, and this prevents
CC Norwalk virus binding contributing to resistance to Norwalk virus
CC infection. {ECO:0000269|PubMed:12692541}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=hh";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/fut2/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Fucosyltransferase 2;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_599";
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DR EMBL; U17894; AAC24453.1; -; Genomic_DNA.
DR EMBL; D87942; BAA21684.1; -; mRNA.
DR EMBL; AY937240; AAX14047.1; -; Genomic_DNA.
DR EMBL; AC008888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC121066; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; D89327; BAA13944.1; -; Genomic_DNA.
DR EMBL; D82933; BAA11638.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS33069.1; -.
DR PIR; A56098; A56098.
DR RefSeq; NP_000502.4; NM_000511.5.
DR RefSeq; NP_001091107.1; NM_001097638.2.
DR AlphaFoldDB; Q10981; -.
DR SMR; Q10981; -.
DR BioGRID; 108800; 1.
DR IntAct; Q10981; 5.
DR STRING; 9606.ENSP00000387498; -.
DR ChEMBL; CHEMBL4105777; -.
DR CAZy; GT11; Glycosyltransferase Family 11.
DR GlyGen; Q10981; 3 sites.
DR iPTMnet; Q10981; -.
DR PhosphoSitePlus; Q10981; -.
DR BioMuta; FUT2; -.
DR DMDM; 1730125; -.
DR MassIVE; Q10981; -.
DR PaxDb; Q10981; -.
DR PeptideAtlas; Q10981; -.
DR PRIDE; Q10981; -.
DR Antibodypedia; 2644; 153 antibodies from 30 providers.
DR DNASU; 2524; -.
DR Ensembl; ENST00000391876.5; ENSP00000375748.4; ENSG00000176920.13.
DR Ensembl; ENST00000425340.3; ENSP00000387498.2; ENSG00000176920.13.
DR Ensembl; ENST00000522966.2; ENSP00000430227.2; ENSG00000176920.13.
DR GeneID; 2524; -.
DR KEGG; hsa:2524; -.
DR MANE-Select; ENST00000425340.3; ENSP00000387498.2; NM_000511.6; NP_000502.4.
DR UCSC; uc010emc.4; human.
DR CTD; 2524; -.
DR DisGeNET; 2524; -.
DR GeneCards; FUT2; -.
DR HGNC; HGNC:4013; FUT2.
DR HPA; ENSG00000176920; Tissue enhanced (intestine, salivary gland, stomach).
DR MalaCards; FUT2; -.
DR MIM; 182100; gene+phenotype.
DR MIM; 612542; phenotype.
DR neXtProt; NX_Q10981; -.
DR OpenTargets; ENSG00000176920; -.
DR PharmGKB; PA28429; -.
DR VEuPathDB; HostDB:ENSG00000176920; -.
DR eggNOG; ENOG502S316; Eukaryota.
DR GeneTree; ENSGT00390000001450; -.
DR HOGENOM; CLU_043399_0_1_1; -.
DR InParanoid; Q10981; -.
DR OMA; KGMWTIN; -.
DR PhylomeDB; Q10981; -.
DR TreeFam; TF315810; -.
DR BioCyc; MetaCyc:HS11104-MON; -.
DR BRENDA; 2.4.1.344; 2681.
DR BRENDA; 2.4.1.69; 2681.
DR PathwayCommons; Q10981; -.
DR Reactome; R-HSA-9033807; ABO blood group biosynthesis.
DR Reactome; R-HSA-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q10981; -.
DR SIGNOR; Q10981; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 2524; 25 hits in 1065 CRISPR screens.
DR ChiTaRS; FUT2; human.
DR GeneWiki; FUT2; -.
DR GenomeRNAi; 2524; -.
DR Pharos; Q10981; Tbio.
DR PRO; PR:Q10981; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q10981; protein.
DR Bgee; ENSG00000176920; Expressed in olfactory segment of nasal mucosa and 132 other tissues.
DR ExpressionAtlas; Q10981; baseline and differential.
DR Genevisible; Q10981; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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:0008417; F:fucosyltransferase activity; TAS:ProtInc.
DR GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0036065; P:fucosylation; ISS:UniProtKB.
DR GO; GO:0006664; P:glycolipid metabolic process; ISS:UniProtKB.
DR GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
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 Blood group antigen; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Galactoside alpha-(1,2)-fucosyltransferase 2"
FT /id="PRO_0000012140"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 25
FT /note="I -> V (in dbSNP:rs1800021)"
FT /evidence="ECO:0000269|PubMed:9760207, ECO:0000269|Ref.3"
FT /id="VAR_003422"
FT VARIANT 138
FT /note="R -> C (in dbSNP:rs1800022)"
FT /evidence="ECO:0000269|PubMed:9760207, ECO:0000269|Ref.3"
FT /id="VAR_003423"
FT VARIANT 140
FT /note="I -> F (in allele Sej; non-secretor phenotype;
FT dbSNP:rs1047781)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8621666, ECO:0000269|PubMed:9219535"
FT /id="VAR_003424"
FT VARIANT 172
FT /note="D -> N (in dbSNP:rs1800025)"
FT /evidence="ECO:0000269|PubMed:9760207, ECO:0000269|Ref.3"
FT /id="VAR_003425"
FT VARIANT 258
FT /note="G -> S (in dbSNP:rs602662)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022187"
SQ SEQUENCE 343 AA; 39017 MW; 12066D9CF175E13A CRC64;
MLVVQMPFSF PMAHFILFVF TVSTIFHVQQ RLAKIQAMWE LPVQIPVLAS TSKALGPSQL
RGMWTINAIG RLGNQMGEYA TLYALAKMNG RPAFIPAQMH STLAPIFRIT LPVLHSATAS
RIPWQNYHLN DWMEEEYRHI PGEYVRFTGY PCSWTFYHHL RQEILQEFTL HDHVREEAQK
FLRGLQVNGS RPGTFVGVHV RRGDYVHVMP KVWKGVVADR RYLQQALDWF RARYSSLIFV
VTSNGMAWCR ENIDTSHGDV VFAGDGIEGS PAKDFALLTQ CNHTIMTIGT FGIWAAYLTG
GDTIYLANYT LPDSPFLKIF KPEAAFLPEW TGIAADLSPL LKH
