Reviewed, UniProtKB/Swiss-Prot Q10980 (FUT1_RAT)

Names and origin

Protein names

Recommended name:
    Galactoside 2-alpha-L-fucosyltransferase 1
    EC=2.4.1.69
Alternative name(s):
    GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1
    Alpha(1,2)FT 1
    Fucosyltransferase 1
    Alpha 1,2-fucosyltransferase A

Gene names

Name:	Fut1
Synonyms:	Fta

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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 apparatus › Golgi stack membrane; Single-pass type II membrane protein By similarity. Note: Membrane-bound form in trans cisternae of Golgi By similarity.
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.
Sequence similarities	Belongs to the glycosyltransferase 11 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	galactoside 2-alpha-L-fucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	Galactoside 2-alpha-L-fucosyltransferase 1		PRO_0000149102
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 29	17	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 376	347	Lumenal Potential
Amino acid modifications
	Glycosylation	64	1	N-linked (GlcNAc...) Potential
	Glycosylation	302	1	N-linked (GlcNAc...) Potential
	Glycosylation	328	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q10980-1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: C350C737C758B7F8	FASTA	376	42,417
	10 20 30 40 50 60 MWTPSRKQLC LAFLSVCVLS AGSFFFHLNG GNFFQNALTF SVLCPDYHLL KSPVAMVCLP 70 80 90 100 110 120 YPSNASSGSP SCPEQSLLSG TWTITPGGRF GNQMGQYATL LALAQLNGRR AFIQPEMHTT 130 140 150 160 170 180 LAPVFRISLP VLDPEVDSLT PWQHLVLHDW MSEEYSHLED PFLKLSGFPC SWTFFHHLRE 190 200 210 220 230 240 QIRREFTLHD HLREDAQRLL SGLRIGPAGI RPRTYVGVHV RRGDYLEVMP NRWKGVVGDR 250 260 270 280 290 300 AYLQKAMDWF RARHKDPIFV VTSNGMRWCL ENIDTSHGDV VFAGNGQEGT PGKDFALLTQ 310 320 330 340 350 360 CNHTIMTIGT FGFWAAYLAG GDTVYLANFT LPDSEFLKIF RPKAAFLPEW VGINADLSPL 370 QAQFDPWETD SLFRLA

References

[1]	"Two distinct rat GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase genes." Soejima M., Wang B., Koda Y., Kimura H. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Colon cancer.
[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. Strain: BDIX.
[3]	"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 169-310. Strain: BDIX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB015637 Genomic DNA. Translation: BAA31130.1. AB006137 mRNA. Translation: BAA21741.1. AF131237 Genomic DNA. Translation: AAD24468.1. L26009 mRNA. Translation: AAB41514.1.
IPI	IPI00213658.
PIR	S51582.
RefSeq	NP_112515.1.
UniGene	Rn.11382
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q10980.
Protein family/group databases
CAZy	GT11. Glycosyltransferase Family 11.
PTM databases
PhosphoSite	Q10980.
Genome annotation databases
Ensembl	ENSRNOT00000028494; ENSRNOP00000028494; ENSRNOG00000020995; Rattus norvegicus. [Genome view]
GeneID	81919.
KEGG	rno:81919.
UCSC	NM_031236. rat.
Organism-specific databases
CTD	81919.
RGD	2638. Fut1.
Phylogenomic databases
HOVERGEN	Q10980.
OMA	MDWFRAR.
Enzyme and pathway databases
BRENDA	2.4.1.69. 248.
Gene expression databases
ArrayExpress	Q10980.
Genevestigator	Q10980.
GermOnline	ENSRNOG00000020995. Rattus norvegicus.
Family and domain databases
InterPro	IPR002516. Glyco_trans_11. [Graphical view]
PANTHER	PTHR11927. Glyco_trans_11. 1 hit.
Pfam	PF01531. Glyco_transf_11. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	615805.

Entry information

Entry name

FUT1_RAT

Accession

Primary (citable) accession number: Q10980
Secondary accession number(s): Q549F8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 15, 1999
Last modified:	November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)