Fucosyltransferase 3: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS (v470))
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Galactoside 3(4)-L-fucosyltransferase''' is an [[enzyme]] that in humans is encoded by the ''FUT3'' [[gene]].<ref name="pmid1977660">{{cite journal | vauthors = Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB | title = A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase | journal = Genes & Development | volume = 4 | issue = 8 | pages = 1288–303 | date = Aug 1990 | pmid = 1977660 | pmc =  | doi = 10.1101/gad.4.8.1288 }}</ref><ref name="pmid1740457">{{cite journal | vauthors = Weston BW, Nair RP, Larsen RD, Lowe JB | title = Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities | journal = The Journal of Biological Chemistry | volume = 267 | issue = 6 | pages = 4152–60 | date = Feb 1992 | pmid = 1740457 | pmc = | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)
| HGNCid = 4014
| Symbol = FUT3
| AltSymbols =; CD174; LE; Les; MGC131739
| OMIM = 111100
| ECnumber = 
| Homologene = 55438
| MGIid = 
| GeneAtlas_image1 = PBB_GE_FUT3_214088_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FUT3_210398_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_FUT3_211882_x_at_tn.png
| Function = {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0017060 |text = 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006486 |text = protein amino acid glycosylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2525
    | Hs_Ensembl = ENSG00000171124
    | Hs_RefseqProtein = NP_000140
    | Hs_RefseqmRNA = NM_000149
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 5793902
    | Hs_GenLoc_end = 5802482
    | Hs_Uniprot = P21217
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)''', also known as '''FUT3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The [[Lewis blood-group system|Lewis histo-blood group system]] comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2525| accessdate = }}</ref>
}}


==See also==
== See also ==
* [[Cluster of differentiation]]
* [[Cluster of differentiation]]


==References==
== References ==
{{reflist|2}}
{{reflist|30em}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin|35em}}
{{PBB_Further_reading
* {{cite journal | vauthors = Cameron HS, Szczepaniak D, Weston BW | title = Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms | journal = The Journal of Biological Chemistry | volume = 270 | issue = 34 | pages = 20112–22 | date = Aug 1995 | pmid = 7650030 | doi = 10.1074/jbc.270.34.20112 }}
| citations =
* {{cite journal | vauthors = Reguigne-Arnould I, Couillin P, Mollicone R, Fauré S, Fletcher A, Kelly RJ, Lowe JB, Oriol R | title = Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19 | journal = Cytogenetics and Cell Genetics | volume = 71 | issue = 2 | pages = 158–62 | year = 1995 | pmid = 7656588 | doi = 10.1159/000134098 }}
*{{cite journal | author=Weston BW, Nair RP, Larsen RD, Lowe JB |title=Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. |journal=J. Biol. Chem. |volume=267 |issue= 6 |pages= 4152-60 |year= 1992 |pmid= 1740457 |doi= }}
* {{cite journal | vauthors = Nishihara S, Nakazato M, Kudo T, Kimura H, Ando T, Narimatsu H | title = Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19 | journal = Biochemical and Biophysical Research Communications | volume = 190 | issue = 1 | pages = 42–6 | date = Jan 1993 | pmid = 7916594 | doi = 10.1006/bbrc.1993.1008 }}
*{{cite journal | author=Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB |title=A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase. |journal=Genes Dev. |volume=4 |issue= 8 |pages= 1288-303 |year= 1990 |pmid= 1977660 |doi= }}
* {{cite journal | vauthors = Nishihara S, Narimatsu H, Iwasaki H, Yazawa S, Akamatsu S, Ando T, Seno T, Narimatsu I | title = Molecular genetic analysis of the human Lewis histo-blood group system | journal = The Journal of Biological Chemistry | volume = 269 | issue = 46 | pages = 29271–8 | date = Nov 1994 | pmid = 7961897 | doi =  }}
*{{cite journal | author=Cameron HS, Szczepaniak D, Weston BW |title=Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. |journal=J. Biol. Chem. |volume=270 |issue= 34 |pages= 20112-22 |year= 1995 |pmid= 7650030 |doi= }}
* {{cite journal | vauthors = Mollicone R, Reguigne I, Kelly RJ, Fletcher A, Watt J, Chatfield S, Aziz A, Cameron HS, Weston BW, Lowe JB | title = Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees | journal = The Journal of Biological Chemistry | volume = 269 | issue = 33 | pages = 20987–94 | date = Aug 1994 | pmid = 8063716 | doi = }}
*{{cite journal | author=Reguigne-Arnould I, Couillin P, Mollicone R, ''et al.'' |title=Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19. |journal=Cytogenet. Cell Genet. |volume=71 |issue= 2 |pages= 158-62 |year= 1995 |pmid= 7656588 |doi=  }}
* {{cite journal | vauthors = Koda Y, Kimura H, Mekada E | title = Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals | journal = Blood | volume = 82 | issue = 9 | pages = 2915–9 | date = Nov 1993 | pmid = 8219240 | doi =  }}
*{{cite journal | author=Nishihara S, Nakazato M, Kudo T, ''et al.'' |title=Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19. |journal=Biochem. Biophys. Res. Commun. |volume=190 |issue= 1 |pages= 42-6 |year= 1993 |pmid= 7916594 |doi= 10.1006/bbrc.1993.1008 }}
* {{cite journal | vauthors = Elmgren A, Rydberg L, Larson G | title = Genotypic heterogeneity among Lewis negative individuals | journal = Biochemical and Biophysical Research Communications | volume = 196 | issue = 2 | pages = 515–20 | date = Oct 1993 | pmid = 8240322 | doi = 10.1006/bbrc.1993.2280 }}
*{{cite journal | author=Nishihara S, Narimatsu H, Iwasaki H, ''et al.'' |title=Molecular genetic analysis of the human Lewis histo-blood group system. |journal=J. Biol. Chem. |volume=269 |issue= 46 |pages= 29271-8 |year= 1994 |pmid= 7961897 |doi=  }}
* {{cite journal | vauthors = Nishihara S, Yazawa S, Iwasaki H, Nakazato M, Kudo T, Ando T, Narimatsu H | title = Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals | journal = Biochemical and Biophysical Research Communications | volume = 196 | issue = 2 | pages = 624–31 | date = Oct 1993 | pmid = 8240337 | doi = 10.1006/bbrc.1993.2295 }}
*{{cite journal | author=Mollicone R, Reguigne I, Kelly RJ, ''et al.'' |title=Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees. |journal=J. Biol. Chem. |volume=269 |issue= 33 |pages= 20987-94 |year= 1994 |pmid= 8063716 |doi= }}
* {{cite journal | vauthors = Elmgren A, Börjeson C, Svensson L, Rydberg L, Larson G | title = DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system | journal = Vox Sanguinis | volume = 70 | issue = 2 | pages = 97–103 | year = 1996 | pmid = 8801770 | doi = 10.1111/j.1423-0410.1996.tb01300.x }}
*{{cite journal | author=Koda Y, Kimura H, Mekada E |title=Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals. |journal=Blood |volume=82 |issue= 9 |pages= 2915-9 |year= 1993 |pmid= 8219240 |doi= }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Elmgren A, Rydberg L, Larson G |title=Genotypic heterogeneity among Lewis negative individuals. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 515-20 |year= 1993 |pmid= 8240322 |doi= 10.1006/bbrc.1993.2280 }}
* {{cite journal | vauthors = Orntoft TF, Vestergaard EM, Holmes E, Jakobsen JS, Grunnet N, Mortensen M, Johnson P, Bross P, Gregersen N, Skorstengaard K, Jensen UB, Bolund L, Wolf H | title = Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels | journal = The Journal of Biological Chemistry | volume = 271 | issue = 50 | pages = 32260–8 | date = Dec 1996 | pmid = 8943285 | doi = 10.1074/jbc.271.50.32260 }}
*{{cite journal | author=Nishihara S, Yazawa S, Iwasaki H, ''et al.'' |title=Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 624-31 |year= 1993 |pmid= 8240337 |doi= 10.1006/bbrc.1993.2295 }}
* {{cite journal | vauthors = Elmgren A, Mollicone R, Costache M, Börjeson C, Oriol R, Harrington J, Larson G | title = Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII | journal = The Journal of Biological Chemistry | volume = 272 | issue = 35 | pages = 21994–8 | date = Aug 1997 | pmid = 9268337 | doi = 10.1074/jbc.272.35.21994 }}
*{{cite journal | author=Elmgren A, Börjeson C, Svensson L, ''et al.'' |title=DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system. |journal=Vox Sang. |volume=70 |issue= 2 |pages= 97-103 |year= 1996 |pmid= 8801770 |doi= }}
* {{cite journal | vauthors = Pang H, Liu Y, Koda Y, Soejima M, Jia J, Schlaphoff T, Du Toit ED, Kimura H | title = Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa | journal = Human Genetics | volume = 102 | issue = 6 | pages = 675–80 | date = Jun 1998 | pmid = 9703429 | doi = 10.1007/s004390050760 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Nishihara S, Hiraga T, Ikehara Y, Iwasaki H, Kudo T, Yazawa S, Morozumi K, Suda Y, Narimatsu H | title = Molecular behavior of mutant Lewis enzymes in vivo | journal = Glycobiology | volume = 9 | issue = 4 | pages = 373–82 | date = Apr 1999 | pmid = 10089211 | doi = 10.1093/glycob/9.4.373 }}
*{{cite journal | author=Orntoft TF, Vestergaard EM, Holmes E, ''et al.'' |title=Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 32260-8 |year= 1997 |pmid= 8943285 |doi= }}
* {{cite journal | vauthors = Yazawa S, Tanaka S, Nishimura T, Miyanaga K, Kochibe N | title = Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia | journal = Experimental and Clinical Immunogenetics | volume = 16 | issue = 3 | pages = 125–30 | year = 1999 | pmid = 10394050 | doi = 10.1159/000019104 }}
*{{cite journal | author=Elmgren A, Mollicone R, Costache M, ''et al.'' |title=Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII. |journal=J. Biol. Chem. |volume=272 |issue= 35 |pages= 21994-8 |year= 1997 |pmid= 9268337 |doi= }}
* {{cite journal | vauthors = Holmes EH, Yen TY, Thomas S, Joshi R, Nguyen A, Long T, Gallet F, Maftah A, Julien R, Macher BA | title = Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites | journal = The Journal of Biological Chemistry | volume = 275 | issue = 32 | pages = 24237–45 | date = Aug 2000 | pmid = 10816554 | doi = 10.1074/jbc.M000888200 }}
*{{cite journal | author=Pang H, Liu Y, Koda Y, ''et al.'' |title=Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa. |journal=Hum. Genet. |volume=102 |issue= 6 |pages= 675-80 |year= 1998 |pmid= 9703429 |doi= }}
* {{cite journal | vauthors = Grahn A, Elmgren A, Aberg L, Svensson L, Jansson PA, Lönnroth P, Larson G | title = Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples | journal = Human Mutation | volume = 18 | issue = 4 | pages = 358–9 | date = Oct 2001 | pmid = 11668626 | doi = 10.1002/humu.1204 }}
*{{cite journal | author=Nishihara S, Hiraga T, Ikehara Y, ''et al.'' |title=Molecular behavior of mutant Lewis enzymes in vivo. |journal=Glycobiology |volume=9 |issue= 4 |pages= 373-82 |year= 1999 |pmid= 10089211 |doi= }}
* {{cite journal | vauthors = Roos C, Kolmer M, Mattila P, Renkonen R | title = Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism | journal = The Journal of Biological Chemistry | volume = 277 | issue = 5 | pages = 3168–75 | date = Feb 2002 | pmid = 11698403 | doi = 10.1074/jbc.M107927200 }}
*{{cite journal | author=Yazawa S, Tanaka S, Nishimura T, ''et al.'' |title=Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia. |journal=Exp. Clin. Immunogenet. |volume=16 |issue= 3 |pages= 125-30 |year= 1999 |pmid= 10394050 |doi= }}
*{{cite journal | author=Holmes EH, Yen TY, Thomas S, ''et al.'' |title=Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24237-45 |year= 2000 |pmid= 10816554 |doi= 10.1074/jbc.M000888200 }}
*{{cite journal  | author=Grahn A, Elmgren A, Aberg L, ''et al.'' |title=Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples. |journal=Hum. Mutat. |volume=18 |issue= 4 |pages= 358-9 |year= 2002 |pmid= 11668626 |doi= 10.1002/humu.1204 }}
*{{cite journal | author=Roos C, Kolmer M, Mattila P, Renkonen R |title=Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism. |journal=J. Biol. Chem. |volume=277 |issue= 5 |pages= 3168-75 |year= 2002 |pmid= 11698403 |doi= 10.1074/jbc.M107927200 }}
}}
{{refend}}
{{refend}}


==External links==
== External links ==
* {{MeshName|CD174+Antigen}}
* {{MeshName|CD174+Antigen}}


{{membrane-protein-stub}}
{{Clusters of differentiation}}
{{Clusters of differentiation}}
{{Glycosyltransferases}}
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]

Latest revision as of 01:36, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Galactoside 3(4)-L-fucosyltransferase is an enzyme that in humans is encoded by the FUT3 gene.[1][2][3]

Function

The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.[3]

See also

References

  1. Kukowska-Latallo JF, Larsen RD, Nair RP, Lowe JB (Aug 1990). "A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase". Genes & Development. 4 (8): 1288–303. doi:10.1101/gad.4.8.1288. PMID 1977660.
  2. Weston BW, Nair RP, Larsen RD, Lowe JB (Feb 1992). "Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities". The Journal of Biological Chemistry. 267 (6): 4152–60. PMID 1740457.
  3. 3.0 3.1 "Entrez Gene: FUT3 fucosyltransferase 3 (galactoside 3(4)-L-fucosyltransferase, Lewis blood group)".

Further reading

  • Cameron HS, Szczepaniak D, Weston BW (Aug 1995). "Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms". The Journal of Biological Chemistry. 270 (34): 20112–22. doi:10.1074/jbc.270.34.20112. PMID 7650030.
  • Reguigne-Arnould I, Couillin P, Mollicone R, Fauré S, Fletcher A, Kelly RJ, Lowe JB, Oriol R (1995). "Relative positions of two clusters of human alpha-L-fucosyltransferases in 19q (FUT1-FUT2) and 19p (FUT6-FUT3-FUT5) within the microsatellite genetic map of chromosome 19". Cytogenetics and Cell Genetics. 71 (2): 158–62. doi:10.1159/000134098. PMID 7656588.
  • Nishihara S, Nakazato M, Kudo T, Kimura H, Ando T, Narimatsu H (Jan 1993). "Human alpha-1,3 fucosyltransferase (FucT-VI) gene is located at only 13 kb 3' to the Lewis type fucosyltransferase (FucT-III) gene on chromosome 19". Biochemical and Biophysical Research Communications. 190 (1): 42–6. doi:10.1006/bbrc.1993.1008. PMID 7916594.
  • Nishihara S, Narimatsu H, Iwasaki H, Yazawa S, Akamatsu S, Ando T, Seno T, Narimatsu I (Nov 1994). "Molecular genetic analysis of the human Lewis histo-blood group system". The Journal of Biological Chemistry. 269 (46): 29271–8. PMID 7961897.
  • Mollicone R, Reguigne I, Kelly RJ, Fletcher A, Watt J, Chatfield S, Aziz A, Cameron HS, Weston BW, Lowe JB (Aug 1994). "Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees". The Journal of Biological Chemistry. 269 (33): 20987–94. PMID 8063716.
  • Koda Y, Kimura H, Mekada E (Nov 1993). "Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals". Blood. 82 (9): 2915–9. PMID 8219240.
  • Elmgren A, Rydberg L, Larson G (Oct 1993). "Genotypic heterogeneity among Lewis negative individuals". Biochemical and Biophysical Research Communications. 196 (2): 515–20. doi:10.1006/bbrc.1993.2280. PMID 8240322.
  • Nishihara S, Yazawa S, Iwasaki H, Nakazato M, Kudo T, Ando T, Narimatsu H (Oct 1993). "Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals". Biochemical and Biophysical Research Communications. 196 (2): 624–31. doi:10.1006/bbrc.1993.2295. PMID 8240337.
  • Elmgren A, Börjeson C, Svensson L, Rydberg L, Larson G (1996). "DNA sequencing and screening for point mutations in the human Lewis (FUT3) gene enables molecular genotyping of the human Lewis blood group system". Vox Sanguinis. 70 (2): 97–103. doi:10.1111/j.1423-0410.1996.tb01300.x. PMID 8801770.
  • Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Orntoft TF, Vestergaard EM, Holmes E, Jakobsen JS, Grunnet N, Mortensen M, Johnson P, Bross P, Gregersen N, Skorstengaard K, Jensen UB, Bolund L, Wolf H (Dec 1996). "Influence of Lewis alpha1-3/4-L-fucosyltransferase (FUT3) gene mutations on enzyme activity, erythrocyte phenotyping, and circulating tumor marker sialyl-Lewis a levels". The Journal of Biological Chemistry. 271 (50): 32260–8. doi:10.1074/jbc.271.50.32260. PMID 8943285.
  • Elmgren A, Mollicone R, Costache M, Börjeson C, Oriol R, Harrington J, Larson G (Aug 1997). "Significance of individual point mutations, T202C and C314T, in the human Lewis (FUT3) gene for expression of Lewis antigens by the human alpha(1,3/1,4)-fucosyltransferase, Fuc-TIII". The Journal of Biological Chemistry. 272 (35): 21994–8. doi:10.1074/jbc.272.35.21994. PMID 9268337.
  • Pang H, Liu Y, Koda Y, Soejima M, Jia J, Schlaphoff T, Du Toit ED, Kimura H (Jun 1998). "Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa". Human Genetics. 102 (6): 675–80. doi:10.1007/s004390050760. PMID 9703429.
  • Nishihara S, Hiraga T, Ikehara Y, Iwasaki H, Kudo T, Yazawa S, Morozumi K, Suda Y, Narimatsu H (Apr 1999). "Molecular behavior of mutant Lewis enzymes in vivo". Glycobiology. 9 (4): 373–82. doi:10.1093/glycob/9.4.373. PMID 10089211.
  • Yazawa S, Tanaka S, Nishimura T, Miyanaga K, Kochibe N (1999). "Plasma alpha1,3-fucosyltransferase deficiency in schizophrenia". Experimental and Clinical Immunogenetics. 16 (3): 125–30. doi:10.1159/000019104. PMID 10394050.
  • Holmes EH, Yen TY, Thomas S, Joshi R, Nguyen A, Long T, Gallet F, Maftah A, Julien R, Macher BA (Aug 2000). "Human alpha 1,3/4 fucosyltransferases. Characterization of highly conserved cysteine residues and N-linked glycosylation sites". The Journal of Biological Chemistry. 275 (32): 24237–45. doi:10.1074/jbc.M000888200. PMID 10816554.
  • Grahn A, Elmgren A, Aberg L, Svensson L, Jansson PA, Lönnroth P, Larson G (Oct 2001). "Determination of Lewis FUT3 gene mutations by PCR using sequence-specific primers enables efficient genotyping of clinical samples". Human Mutation. 18 (4): 358–9. doi:10.1002/humu.1204. PMID 11668626.
  • Roos C, Kolmer M, Mattila P, Renkonen R (Feb 2002). "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism". The Journal of Biological Chemistry. 277 (5): 3168–75. doi:10.1074/jbc.M107927200. PMID 11698403.

External links