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P21217 (FUT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galactoside 3(4)-L-fucosyltransferase

EC=2.4.1.65
Alternative name(s):
Blood group Lewis alpha-4-fucosyltransferase
Short name=Lewis FT
Fucosyltransferase 3
Fucosyltransferase III
Short name=FucT-III
Gene names
Name:FUT3
Synonyms:FT3B, LE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May catalyze alpha-1,3 and alpha-1,4 glycosidic linkages involved in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. May be involved in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. Also acts on the corresponding 1,4-galactosyl derivative, forming 1,3-L-fucosyl links.

Catalytic activity

GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->4))-N-acetyl-beta-D-glucosaminyl-R.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Note: Membrane-bound form in trans cisternae of Golgi.

Tissue specificity

Highly expressed in stomach, colon, small intestine, lung and kidney and to a lesser extent in salivary gland, bladder, uterus and liver.

Sequence similarities

Belongs to the glycosyltransferase 10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Galactoside 3(4)-L-fucosyltransferase
PRO_0000221096

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3419Helical; Signal-anchor for type II membrane protein; Potential
Topological domain35 – 361327Lumenal Potential

Amino acid modifications

Glycosylation1541N-linked (GlcNAc...) Probable
Glycosylation1851N-linked (GlcNAc...) Probable

Natural variations

Natural variant51G → S. Ref.5
Corresponds to variant rs28362458 [ dbSNP | Ensembl ].
VAR_022200
Natural variant201L → R in Le(-). Ref.5 Ref.9 Ref.10 Ref.11 Ref.13
Corresponds to variant rs28362459 [ dbSNP | Ensembl ].
VAR_003426
Natural variant681W → R in Le(-). Ref.4 Ref.5 Ref.6 Ref.13 Ref.14
Corresponds to variant rs812936 [ dbSNP | Ensembl ].
VAR_007959
Natural variant1021Q → K in Le(+). Ref.15
Corresponds to variant rs59796499 [ dbSNP | Ensembl ].
VAR_007960
Natural variant1051T → M in Le(-). Ref.4 Ref.5 Ref.6 Ref.8 Ref.13 Ref.14
Corresponds to variant rs778986 [ dbSNP | Ensembl ].
VAR_003427
Natural variant1241S → A in Le(+). Ref.15
VAR_007961
Natural variant1601R → C. Ref.5
Corresponds to variant rs28362462 [ dbSNP | Ensembl ].
VAR_022201
Natural variant1621D → N in Le(-). Ref.5 Ref.15
Corresponds to variant rs28362463 [ dbSNP | Ensembl ].
VAR_007962
Natural variant1701G → S in Le(-); completely inactive. Ref.5 Ref.9 Ref.10
Corresponds to variant rs28362464 [ dbSNP | Ensembl ].
VAR_003428
Natural variant2231G → R in Le(-). Ref.5 Ref.15
Corresponds to variant rs28362466 [ dbSNP | Ensembl ].
VAR_007963
Natural variant2701V → M in Le(-). Ref.5 Ref.15
Corresponds to variant rs28381968 [ dbSNP | Ensembl ].
VAR_007964
Natural variant3251T → M. Ref.5
Corresponds to variant rs28381969 [ dbSNP | Ensembl ].
VAR_022202
Natural variant3271R → Q. Ref.5
Corresponds to variant rs28381970 [ dbSNP | Ensembl ].
VAR_022203
Natural variant3361D → A in Le(-). Ref.9
VAR_003429
Natural variant3561I → K in Le(-); less than 10% reduction in activity. Ref.11 Ref.12 Ref.13
Corresponds to variant rs3894326 [ dbSNP | Ensembl ].
VAR_003430

Sequences

Sequence LengthMass (Da)Tools
P21217 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: BF4398044F19C284

FASTA36142,117
        10         20         30         40         50         60 
MDPLGAAKPQ WPWRRCLAAL LFQLLVAVCF FSYLRVSRDD ATGSPRAPSG SSRQDTTPTR 

        70         80         90        100        110        120 
PTLLILLWTW PFHIPVALSR CSEMVPGTAD CHITADRKVY PQADTVIVHH WDIMSNPKSR 

       130        140        150        160        170        180 
LPPSPRPQGQ RWIWFNLEPP PNCQHLEALD RYFNLTMSYR SDSDIFTPYG WLEPWSGQPA 

       190        200        210        220        230        240 
HPPLNLSAKT ELVAWAVSNW KPDSARVRYY QSLQAHLKVD VYGRSHKPLP KGTMMETLSR 

       250        260        270        280        290        300 
YKFYLAFENS LHPDYITEKL WRNALEAWAV PVVLGPSRSN YERFLPPDAF IHVDDFQSPK 

       310        320        330        340        350        360 
DLARYLQELD KDHARYLSYF RWRETLRPRS FSWALDFCKA CWKLQQESRY QTVRSIAAWF 


T 

« Hide

References

« Hide 'large scale' references
[1]"A cloned human cDNA determines expression of a mouse stage-specific embryonic antigen and the Lewis blood group alpha(1,3/1,4)fucosyltransferase."
Kukowska-Latallo J.F., Larsen R.D., Nair R.P., Lowe J.B.
Genes Dev. 4:1288-1303(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms."
Cameron H.S., Szczepaniak D., Weston B.W.
J. Biol. Chem. 270:20112-20122(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Isolation and expression of human alpha (1,3/1,4) fucosyltransferase."
Rahim I., Schmidt L.R., Wahl D., Drayson E., Maslanik W., Stranahan P.L., Pettijohn D.E.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Squamous cell carcinoma.
[4]"Allele frequencies of fucosyltransferases 1, 2, and 3 of Styrian blood donors."
Matzhold E.M.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-68 AND MET-105.
Tissue: Blood.
[5]SeattleSNPs variation discovery resource
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-5; ARG-20; ARG-68; MET-105; CYS-160; ASN-162; SER-170; ARG-223; MET-270; MET-325 AND GLN-327.
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ARG-68 AND MET-105.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon and Lung.
[8]"Genotypic heterogeneity among Lewis negative individuals."
Elmgren A., Rydberg L., Larson G.
Biochem. Biophys. Res. Commun. 196:515-520(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LE(-) MET-105.
[9]"Alpha (1,3/1,4)fucosyltransferase (FucT-III) gene is inactivated by a single amino acid substitution in Lewis histo-blood type negative individuals."
Nishihara S., Yazawa S., Iwasaki H., Nakazato M., Kudo T., Ando T., Narimatsu H.
Biochem. Biophys. Res. Commun. 196:624-631(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LE(-) ARG-20; SER-170 AND ALA-336.
[10]"Analysis of Lewis fucosyltransferase genes from the human gastric mucosa of Lewis-positive and -negative individuals."
Koda Y., Kimura H., Mekada E.
Blood 82:2915-2919(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LE(-) ARG-20 AND SER-170.
[11]"Molecular basis for Lewis alpha(1,3/1,4)-fucosyltransferase gene deficiency (FUT3) found in Lewis-negative Indonesian pedigrees."
Mollicone R., Reguigne I., Kelly R.J., Fletcher A., Watt J., Chatfield S., Aziz A., Cameron H.S., Weston B.W., Lowe J.B., Oriol R.
J. Biol. Chem. 269:20987-20994(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LE(-) ARG-20 AND LYS-356.
[12]"Molecular genetic analysis of the human Lewis histo-blood group system."
Nishihara S., Narimatsu H., Iwasaki H., Yazawa S., Akamatsu S., Ando T., Seno T., Narimatsu I.
J. Biol. Chem. 269:29271-29278(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LE(-) LYS-356.
[13]"DNA sequencing and screening for point mutations in the human Lewis 'FUT3' gene enables molecular genotyping of the human Lewis blood group system."
Elmgren A., Boerjeson C., Svensson L., Rydberg L., Larson G.
Vox Sang. 70:97-103(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LE(-) ARG-20; ARG-68; MET-105 AND LYS-356.
[14]"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."
Elmgren A., Mollicone R., Costache M., Boerjeson C., Oriol R., Harrington J., Larson G.
J. Biol. Chem. 272:21994-21998(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LE(-) ARG-68 AND MET-105.
[15]"Five novel missense mutations of the Lewis gene 'FUT3' in African 'Xhosa' and Caucasian populations in South Africa."
Pang H., Liu Y., Koda Y., Soejima M., Jia J., Schlaphoff T., du Toit E.D., Kimura H.
Hum. Genet. 102:675-680(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LE(+) LYS-102 AND ALA-124, VARIANTS LE(-) ASN-162; ARG-223 AND MET-270.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

GGDB

GlycoGene database

SeattleSNPs
Functional Glycomics Gateway - GTase

Fucosyltransferase 3

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53578 mRNA. Translation: CAA37641.1.
U27326 mRNA. Translation: AAC50185.1.
U27327 mRNA. Translation: AAC50186.1.
U27328 mRNA. Translation: AAC50187.1.
D89324 Genomic DNA. Translation: BAA13941.1.
D89325 Genomic DNA. Translation: BAA13942.1.
AF131913 mRNA. Translation: AAD33514.1.
FM210024 Genomic DNA. Translation: CAR64692.1.
FM210025 Genomic DNA. Translation: CAR64693.1.
AY870341 Genomic DNA. Translation: AAW34365.1.
AC024592 Genomic DNA. No translation available.
BC074836 mRNA. Translation: AAH74836.1.
BC074837 mRNA. Translation: AAH74837.1.
BC108675 mRNA. Translation: AAI08676.1.
PIRA36669.
RefSeqNP_000140.1. NM_000149.3.
NP_001091108.1. NM_001097639.1.
NP_001091109.1. NM_001097640.1.
NP_001091110.1. NM_001097641.1.
UniGeneHs.169238.

3D structure databases

ProteinModelPortalP21217.
SMRP21217. Positions 187-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000305603.

Chemistry

ChEMBLCHEMBL3269.

Protein family/group databases

CAZyGT10. Glycosyltransferase Family 10.

PTM databases

PhosphoSiteP21217.

Polymorphism databases

DMDM121137.

Proteomic databases

PaxDbP21217.
PRIDEP21217.

Protocols and materials databases

DNASU2525.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303225; ENSP00000305603; ENSG00000171124.
ENST00000458379; ENSP00000416443; ENSG00000171124.
ENST00000589620; ENSP00000465804; ENSG00000171124.
ENST00000589918; ENSP00000468123; ENSG00000171124.
GeneID2525.
KEGGhsa:2525.
UCSCuc002mdj.2. human.

Organism-specific databases

CTD2525.
GeneCardsGC19M005843.
HGNCHGNC:4014. FUT3.
HPAHPA046966.
MIM111100. gene+phenotype.
neXtProtNX_P21217.
PharmGKBPA28430.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG283180.
HOGENOMHOG000045583.
HOVERGENHBG000274.
InParanoidP21217.
KOK00716.
OrthoDBEOG7RJPS6.
PhylomeDBP21217.
TreeFamTF316348.

Enzyme and pathway databases

BRENDA2.4.1.65. 2681.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressP21217.
BgeeP21217.
CleanExHS_FUT3.
GenevestigatorP21217.

Family and domain databases

InterProIPR001503. Glyco_trans_10.
[Graphical view]
PANTHERPTHR11929. PTHR11929. 1 hit.
PfamPF00852. Glyco_transf_10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFucosyltransferase_3.
GenomeRNAi2525.
NextBio9943.
PROP21217.
SOURCESearch...

Entry information

Entry nameFUT3_HUMAN
AccessionPrimary (citable) accession number: P21217
Secondary accession number(s): B5U7U9 expand/collapse secondary AC list , B5U7V0, Q32NE7, Q99448, Q99449
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries