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Galactoside 2-alpha-L-fucosyltransferase 2 (EC 2.4.1.344) (EC 2.4.1.69) (Alpha(1,2)FT 2) (Fucosyltransferase 2) (GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2) (SE2) (Secretor blood group alpha-2-fucosyltransferase) (Secretor factor) (Se)

 FUT2_HUMAN              Reviewed;         343 AA.
Q10981; Q0VAG5; Q14338; Q5D0G2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-OCT-2018, entry version 168.
RecName: Full=Galactoside 2-alpha-L-fucosyltransferase 2;
EC=2.4.1.344 {ECO:0000269|PubMed:7876235};
EC=2.4.1.69 {ECO:0000269|PubMed:7876235};
AltName: Full=Alpha(1,2)FT 2;
AltName: Full=Fucosyltransferase 2;
AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2;
AltName: Full=SE2;
AltName: Full=Secretor blood group alpha-2-fucosyltransferase;
AltName: Full=Secretor factor;
Short=Se;
Name=FUT2; Synonyms=SEC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7876235; DOI=10.1074/jbc.270.9.4640;
Kelly R.J., Rouquier S., Giorgi D., Lennon G.G., Lowe J.B.;
"Sequence and expression of a candidate for the human Secretor blood
group alpha(1,2)fucosyltransferase gene (FUT2). Homozygosity for an
enzyme-inactivating nonsense mutation commonly correlates with the
non-secretor phenotype.";
J. Biol. Chem. 270:4640-4649(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-140.
PubMed=9219535; DOI=10.1111/j.1432-1033.1997.t01-1-00750.x;
Koda Y., Soejima M., Wang B., Kimura H.;
"Structure and expression of the gene encoding secretor-type
galactoside 2-alpha-L-fucosyltransferase (FUT2).";
Eur. J. Biochem. 246:750-755(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-25; CYS-138;
ASN-172 AND SER-258.
SeattleSNPs variation discovery resource;
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-140.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-343, AND VARIANT PHE-140.
PubMed=8621666; DOI=10.1074/jbc.271.16.9830;
Kudo T., Iwasaki H., Nishihara S., Shinya N., Ando T., Narimatsu I.,
Narimatsu H.;
"Molecular genetic analysis of the human Lewis histo-blood group
system. II. Secretor gene inactivation by a novel single missense
mutation A385T in Japanese nonsecretor individuals.";
J. Biol. Chem. 271:9830-9837(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 70-343.
PubMed=8755920;
Koda Y., Soejima M., Liu Y., Kimura H.;
"Molecular basis for secretor type alpha(1,2)-fucosyltransferase gene
deficiency in a Japanese population: a fusion gene generated by
unequal crossover responsible for the enzyme deficiency.";
Am. J. Hum. Genet. 59:343-350(1996).
[7]
FUNCTION.
PubMed=8018146; DOI=10.1126/science.8018146;
Boren T., Falk P., Roth K.A., Larson G., Normark S.;
"Attachment of Helicobacter pylori to human gastric epithelium
mediated by blood group antigens.";
Science 262:1892-1895(1993).
[8]
FUNCTION, AND INVOLVEMENT IN RESISTANCE TO NORWALK VIRUS.
PubMed=12692541; DOI=10.1038/nm860;
Lindesmith L., Moe C., Marionneau S., Ruvoen N., Jiang X.,
Lindblad L., Stewart P., LePendu J., Baric R.;
"Human susceptibility and resistance to Norwalk virus infection.";
Nat. Med. 9:548-553(2003).
[9]
FUNCTION.
PubMed=21625510; DOI=10.1371/journal.pone.0020113;
Wacklin P., Maekivuokko H., Alakulppi N., Nikkilae J., Tenkanen H.,
Raebinae J., Partanen J., Aranko K., Maettoe J.;
"Secretor genotype (FUT2 gene) is strongly associated with the
composition of Bifidobacteria in the human intestine.";
PLoS ONE 6:E20113-E20113(2011).
[10]
FUNCTION.
PubMed=22068912; DOI=10.1073/pnas.1106408108;
Rausch P., Rehman A., Kuenzel S., Haesler R., Ott S.J., Schreiber S.,
Rosenstiel P., Franke A., Baines J.F.;
"Colonic mucosa-associated microbiota is influenced by an interaction
of Crohn disease and FUT2 (Secretor) genotype.";
Proc. Natl. Acad. Sci. U.S.A. 108:19030-19035(2011).
[11]
FUNCTION.
PubMed=24733310; DOI=10.1371/journal.pone.0094863;
Wacklin P., Tuimala J., Nikkilae J., Tims S., Maekivuokko H.,
Alakulppi N., Laine P., Rajilic-Stojanovic M., Paulin L., de Vos W.M.,
Maettoe J.;
"Faecal microbiota composition in adults is associated with the FUT2
gene determining the secretor status.";
PLoS ONE 9:E94863-E94863(2014).
[12]
VARIANTS VAL-25; CYS-138 AND ASN-172.
PubMed=9760207; DOI=10.1007/s004390050808;
Liu Y., Koda Y., Soejima M., Pang H., Schlaphoff T., du Toit E.D.,
Kimura H.;
"Extensive polymorphism of the FUT2 gene in an African (Xhosa)
population of South Africa.";
Hum. Genet. 103:204-210(1998).
[13]
INVOLVEMENT IN B12QTL1.
PubMed=18776911; DOI=10.1038/ng.210;
Hazra A., Kraft P., Selhub J., Giovannucci E.L., Thomas G.,
Hoover R.N., Chanock S.J., Hunter D.J.;
"Common variants of FUT2 are associated with plasma vitamin B12
levels.";
Nat. Genet. 40:1160-1162(2008).
-!- FUNCTION: Mediates the transfer of fucose to the terminal
galactose on glycan chains of cell surface glycoproteins and
glycolipids (PubMed:7876235). The resulting epitope plays a role
in cell-cell interaction including host-microbe interaction
(PubMed:12692541, PubMed:8018146). Mediates interaction with
intestinal microbiota influencing its composition
(PubMed:21625510, PubMed:24733310, PubMed:22068912). Creates a
soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called
the H antigen which is an essential substrate for the final step
in the soluble ABO blood group antigen synthesis pathway
(PubMed:7876235). {ECO:0000269|PubMed:21625510,
ECO:0000269|PubMed:22068912, ECO:0000269|PubMed:24733310,
ECO:0000269|PubMed:7876235, ECO:0000269|PubMed:8018146}.
-!- CATALYTIC ACTIVITY: GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-
N-acetyl-beta-D-glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-
beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-R.
{ECO:0000269|PubMed:7876235}.
-!- CATALYTIC ACTIVITY: GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-
N-acetyl-beta-D-glucosaminyl-R = GDP + alpha-L-fucosyl-(1->2)-
beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-R.
{ECO:0000269|PubMed:7876235}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=11.5 mM for phenyl-beta-D-galactoside
{ECO:0000269|PubMed:7876235};
KM=3.6 mM for lacto-N-biose {ECO:0000269|PubMed:7876235};
KM=3.8 mM for N-acetyllactosamine {ECO:0000269|PubMed:7876235};
KM=197 uM for GDP-fucose {ECO:0000269|PubMed:7876235};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000269|PubMed:7876235}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
Single-pass type II membrane protein. Note=Membrane-bound form in
trans cisternae of Golgi.
-!- TISSUE SPECIFICITY: Small intestine, colon and lung.
-!- POLYMORPHISM: Three alleles have been identified in the Japanese
population: Se1, Se2, and Sej. {ECO:0000269|PubMed:8621666}.
-!- POLYMORPHISM: Common polymorphisms in FUT2 define the vitamin B12
plasma level quantitative trait locus 1 (B12QTL1) [MIM:612542].
Vitamin B12 found in meat and milk products is necessary for the
formation of red blood cells, DNA synthesis during cell division,
and maintenance of the myelin nerve sheath, among other functions.
Deficiency in vitamin B12, clinically associated with pernicious
anemia, cardiovascular disease, cancer, and neurodegenerative
disorders, is often related to poor intestinal B12 absorption
rather than direct dietary deficiency.
{ECO:0000269|PubMed:18776911}.
-!- POLYMORPHISM: Genetic variation in FUT2 results in the non-
secretor phenotype which gives rise to non-functional FUT2,
resulting in a lack of the H type-1 oligosaccharide ligand in
secretions, and this prevents Norwalk virus binding contributing
to resistance to Norwalk virus infection.
{ECO:0000269|PubMed:12692541}.
-!- MISCELLANEOUS: There are two genes (FUT1 and FUT2) which encode
galactoside 2-L-fucosyltransferase. They are expressed in a
tissue-specific manner with expression restricted to cells of
mesodermal or endodermal origin respectively.
-!- SIMILARITY: Belongs to the glycosyltransferase 11 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA11638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=hh";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/fut2/";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Fucosyltransferase 2;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_599";
-----------------------------------------------------------------------
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EMBL; U17894; AAC24453.1; -; Genomic_DNA.
EMBL; D87942; BAA21684.1; -; mRNA.
EMBL; AY937240; AAX14047.1; -; Genomic_DNA.
EMBL; BC121066; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; D89327; BAA13944.1; -; Genomic_DNA.
EMBL; D82933; BAA11638.1; ALT_INIT; Genomic_DNA.
CCDS; CCDS33069.1; -.
PIR; A56098; A56098.
UniGene; Hs.579928; -.
ProteinModelPortal; Q10981; -.
SMR; Q10981; -.
BioGrid; 108800; 1.
IntAct; Q10981; 1.
STRING; 9606.ENSP00000375748; -.
CAZy; GT11; Glycosyltransferase Family 11.
iPTMnet; Q10981; -.
PhosphoSitePlus; Q10981; -.
BioMuta; FUT2; -.
DMDM; 1730125; -.
PaxDb; Q10981; -.
PeptideAtlas; Q10981; -.
PRIDE; Q10981; -.
ProteomicsDB; 58869; -.
ProteomicsDB; 58870; -.
DNASU; 2524; -.
Ensembl; ENST00000391876; ENSP00000375748; ENSG00000176920.
Ensembl; ENST00000425340; ENSP00000387498; ENSG00000176920.
GeneID; 2524; -.
KEGG; hsa:2524; -.
UCSC; uc010emc.4; human.
CTD; 2524; -.
DisGeNET; 2524; -.
EuPathDB; HostDB:ENSG00000176920.11; -.
GeneCards; FUT2; -.
HGNC; HGNC:4013; FUT2.
HPA; HPA014402; -.
MalaCards; FUT2; -.
MIM; 182100; gene+phenotype.
MIM; 612542; phenotype.
neXtProt; NX_Q10981; -.
OpenTargets; ENSG00000176920; -.
PharmGKB; PA28429; -.
eggNOG; ENOG410IFKR; Eukaryota.
eggNOG; ENOG4111HG3; LUCA.
GeneTree; ENSGT00390000001450; -.
HOGENOM; HOG000261621; -.
HOVERGEN; HBG004338; -.
InParanoid; Q10981; -.
KO; K00718; -.
OMA; AFLPEWT; -.
OrthoDB; EOG091G0X2P; -.
PhylomeDB; Q10981; -.
TreeFam; TF315810; -.
BioCyc; MetaCyc:HS11104-MONOMER; -.
BRENDA; 2.4.1.69; 2681.
SIGNOR; Q10981; -.
UniPathway; UPA00378; -.
GeneWiki; FUT2; -.
GenomeRNAi; 2524; -.
PRO; PR:Q10981; -.
Proteomes; UP000005640; Unplaced.
Bgee; ENSG00000176920; Expressed in 137 organ(s), highest expression level in minor salivary gland.
CleanEx; HS_FUT2; -.
ExpressionAtlas; Q10981; baseline and differential.
Genevisible; Q10981; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008417; F:fucosyltransferase activity; TAS:ProtInc.
GO; GO:0008107; F:galactoside 2-alpha-L-fucosyltransferase activity; TAS:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
GO; GO:0042355; P:L-fucose catabolic process; NAS:UniProtKB.
GO; GO:0006486; P:protein glycosylation; TAS:UniProtKB.
InterPro; IPR002516; Glyco_trans_11.
PANTHER; PTHR11927; PTHR11927; 1.
Pfam; PF01531; Glyco_transf_11; 1.
1: Evidence at protein level;
Blood group antigen; Complete proteome; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Membrane; Polymorphism;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 343 Galactoside 2-alpha-L-fucosyltransferase
2.
/FTId=PRO_0000012140.
TOPO_DOM 1 14 Cytoplasmic. {ECO:0000255}.
TRANSMEM 15 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 343 Lumenal. {ECO:0000255}.
CARBOHYD 188 188 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 282 282 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 25 25 I -> V (polymorphism found in Xhosa
population; dbSNP:rs1800021).
{ECO:0000269|PubMed:9760207,
ECO:0000269|Ref.3}.
/FTId=VAR_003422.
VARIANT 138 138 R -> C (polymorphism found in Xhosa
population; dbSNP:rs1800022).
{ECO:0000269|PubMed:9760207,
ECO:0000269|Ref.3}.
/FTId=VAR_003423.
VARIANT 140 140 I -> F (in allele Sej; non-secretor
phenotype; dbSNP:rs1047781).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8621666,
ECO:0000269|PubMed:9219535}.
/FTId=VAR_003424.
VARIANT 172 172 D -> N (polymorphism found in Xhosa
population; dbSNP:rs1800025).
{ECO:0000269|PubMed:9760207,
ECO:0000269|Ref.3}.
/FTId=VAR_003425.
VARIANT 258 258 G -> S (in dbSNP:rs602662).
{ECO:0000269|Ref.3}.
/FTId=VAR_022187.
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


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