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Q10984 (FUT2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galactoside 2-alpha-L-fucosyltransferase 2

EC=2.4.1.69
Alternative name(s):
Alpha 1,2-fucosyltransferase
Alpha 1,2-fucosyltransferase B
Alpha 1-2 fucosyltransferase
Alpha(1,2)FT 2
Fucosyltransferase 2
GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2
Secretor blood group alpha-2-fucosyltransferase
Gene names
Name:Fut2
Synonyms:Ftb, Sec1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Creates a membrane-associated precursor oligosaccharide Fuc-alpha((1,2)Gal-beta-) called the H antigen which is an essential substrate for the final step in the membrane-associated A and B antigen synthesis pathway. Ref.2

Catalytic activity

GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.

Pathway

Protein modification; protein glycosylation.

Subcellular location

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

Tissue specificity

Specifically expressed in gut. Ref.2

Miscellaneous

In rat, there are three genes (Fut1/Fta, Fut2/Ftb and Ftc) which encode galactoside 2-L-fucosyltransferase. They are expressed in a tissue-specific manner and Ftc may have no enzymatic activity.

Sequence similarities

Belongs to the glycosyltransferase 11 family.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiongalactoside 2-alpha-L-fucosyltransferase activity

Inferred from direct assay Ref.2. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q10984-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q10984-2)

The sequence of this isoform differs from the canonical sequence as follows:
     354-354: H → ALTPACPRSHFHLKAKGVTCYVAGRAF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Galactoside 2-alpha-L-fucosyltransferase 2
PRO_0000149114

Regions

Topological domain1 – 55Cytoplasmic Potential
Transmembrane6 – 2621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 354328Lumenal Potential

Amino acid modifications

Glycosylation1991N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence3541H → ALTPACPRSHFHLKAKGVTC YVAGRAF in isoform 2.
VSP_016526

Experimental info

Sequence conflict261T → I Ref.1
Sequence conflict261T → I Ref.3
Sequence conflict2711V → G in AAB41515. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 123E8C8379E8559E

FASTA35439,983
        10         20         30         40         50         60 
MASAQVPFSF PLAHFLIFVF VTSTITHLQQ RIVKLQPLSE KELPMTTQMS SGNTESPEMR 

        70         80         90        100        110        120 
RDSEQHGNGE LRGMFTINSI GRLGNQMGEY ATLFALARMN GRLAFIPASM HNALAPIFRI 

       130        140        150        160        170        180 
SLPVLHSDTA KKIPWQNYHL NDWMEERYRH IPGHFVRFTG YPCSWTFYHH LRPEILKEFT 

       190        200        210        220        230        240 
LHDHVREEAQ AFLRGLRVNG SQPSTFVGVH VRRGDYVHVM PNVWKGVVAD RGYLEKALDM 

       250        260        270        280        290        300 
FRARYSSPVF VVTSNGMAWC RENINASRGD VVFAGNGIEG SPAKDFALLT QCNHTIMTIG 

       310        320        330        340        350 
TFGIWAAYLA GGDTIYLANY TLPDSPFLKV FKPEAAFLPE WVGIPADLSP LLKH 

« Hide

Isoform 2 [UniParc].

Checksum: 8183786AE8212EBE
Show »

FASTA38042,730

References

[1]"An amino acid region at the N-terminus of rat hepatoma alpha1-->2 fucosyltransferase modulates enzyme activity and interaction with lipids: strong preference for glycosphingolipids containing terminal Galbeta1-->3GalNAc-structures."
Sherwood A.L., Stroud M.R., Levery S.B., Holmes E.H.
Biochemistry 40:5708-5719(2001) [PubMed: 11341836] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: Fischer.
[2]"Comparison of the three rat GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferases FTA, FTB and FTC."
Bureau V., Marionneau S., Cailleau-Thomas A., Le Moullac-Vaidye B., Liehr T., Le Pendu J.
Eur. J. Biochem. 268:1006-1019(2001) [PubMed: 11179967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
Strain: BDIX.
[3]Soejima M., Wang B., Koda Y., Kimura H.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon cancer.
[4]"Evidence for two distinct alpha(1,2)-fucosyltransferase genes differentially expressed throughout the rat colon."
Piau J.-P., Labarriere N., Dabouis G., Denis M.G.
Biochem. J. 300:623-626(1994) [PubMed: 8010942] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 222-354 (ISOFORM 2).
Strain: BDIX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF264005 mRNA. Translation: AAF72200.1.
AF131238 Genomic DNA. Translation: AAD24469.1.
AB006138 mRNA. Translation: BAA21742.1.
L26010 mRNA. Translation: AAB41515.1.
IPIIPI00202052.
IPI00559563.
PIRS46494.
RefSeqNP_113823.1. NM_031635.1.
UniGeneRn.10678.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ10984.

Protein family/group databases

CAZyGT11. Glycosyltransferase Family 11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000028519; ENSRNOP00000028519; ENSRNOG00000021011.
GeneID58924.
KEGGrno:58924.
UCSCNM_031635. rat.

Organism-specific databases

CTD2524.
RGD2639. Fut2.

Phylogenomic databases

eggNOGmaNOG09331.
GeneTreeENSGT00390000001450.
HOVERGENHBG004338.
InParanoidQ10984.
OrthoDBEOG4BK545.

Gene expression databases

ArrayExpressQ10984.
GenevestigatorQ10984.
GermOnlineENSRNOG00000021011. Rattus norvegicus.

Family and domain databases

InterProIPR002516. Glyco_trans_11.
[Graphical view]
KOK00718.
PANTHERPTHR11927. Glyco_trans_11. 1 hit.
PfamPF01531. Glyco_transf_11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio611490.

Entry information

Entry nameFUT2_RAT
AccessionPrimary (citable) accession number: Q10984
Secondary accession number(s): O35087, Q9JK44, Q9R275
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: November 16, 2011
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families