Q9Y231 (FUT9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-(1,3)-fucosyltransferase
EC=2.4.1.-

Alternative name(s):
Fucosyltransferase 9
Fucosyltransferase IX
Short name=Fuc-TIX
Short name=FucT-IX
Galactoside 3-L-fucosyltransferase

Gene names

Name:

FUT9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Transfers a fucose to lacto-N-neotetraose but not to either alpha2,3-sialyl lacto-N-neotetraose or lacto-N-tetraose. Can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides. Ref.1
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.
Tissue specificity	Strongly expressed in forebrain and stomach, lower expression in spleen and peripheral blood leukocytes, and no expression in small intestine, colon, liver, lung, kidney, adrenal cortex or uterus. Ref.1
Sequence similarities	Belongs to the glycosyltransferase 10 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-fucose catabolic process Non-traceable author statement PubMed 11698403. Source: UniProtKB nervous system development Inferred from electronic annotation. Source: Compara protein glycosylation Traceable author statement PubMed 11698403. Source: UniProtKB
Cellular_component	Golgi apparatus Traceable author statement PubMed 11698403. Source: UniProtKB Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	alpha-(1->3)-fucosyltransferase activity Traceable author statement PubMed 11698403. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Alpha-(1,3)-fucosyltransferase		PRO_0000221118
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	33 – 359	327	Lumenal Potential
Amino acid modifications
	Glycosylation	62	1	N-linked (GlcNAc...) Potential
	Glycosylation	101	1	N-linked (GlcNAc...) Potential
	Glycosylation	153	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	237	1	T → A. Ref.1 Ref.2 Ref.4 Corresponds to variant rs3811069 [ dbSNP | Ensembl ].		VAR_024465
	Natural variant	358	1	W → G. Corresponds to variant rs9986564 [ dbSNP | Ensembl ].		VAR_030575

Sequences

	Sequence		Length	Mass (Da)
	Q9Y231 [UniParc]. Last modified November 2, 2010. Version 2. Checksum: D57CFCB039B644D9	FASTA	359	42,071
	10 20 30 40 50 60 MTSTSKGILR PFLIVCIILG CFMACLLIYI KPTNSWIFSP MESASSVLKM KNFFSTKTDY 70 80 90 100 110 120 FNETTILVWV WPFGQTFDLT SCQAMFNIQG CHLTTDRSLY NKSHAVLIHH RDISWDLTNL 130 140 150 160 170 180 PQQARPPFQK WIWMNLESPT HTPQKSGIEH LFNLTLTYRR DSDIQVPYGF LTVSTNPFVF 190 200 210 220 230 240 EVPSKEKLVC WVVSNWNPEH ARVKYYNELS KSIEIHTYGQ AFGEYVNDKN LIPTISTCKF 250 260 270 280 290 300 YLSFENSIHK DYITEKLYNA FLAGSVPVVL GPSRENYENY IPADSFIHVE DYNSPSELAK 310 320 330 340 350 YLKEVDKNNK LYLSYFNWRK DFTVNLPRFW ESHACLACDH VKRHQEYKSV GNLEKWFWN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alpha-1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX." Kaneko M., Kudo T., Iwasaki H., Ikehara Y., Nishihara S., Nakagawa S., Sasaki K., Shiina T., Inoko H., Saitou N., Narimatsu H. FEBS Lett. 452:237-242(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, VARIANT ALA-237. Tissue: Brain.
[2]	"FUT4 and FUT9 genes are expressed early in human embryogenesis." Cailleau-Thomas A., Coullin P., Candelier J.J., Balanzino L., Oriol R., Mollicone R., Mennesson B. Glycobiology 10:789-802(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-237.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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], VARIANT ALA-237. Tissue: Brain.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Fucosyltransferase 9

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB023021 mRNA. Translation: BAA81685.1. AJ238701 mRNA. Translation: CAB41890.1. AL512406 Genomic DNA. Translation: CAI14863.1. BC036101 mRNA. Translation: AAH36101.1.
IPI	IPI00008600.
RefSeq	NP_006572.2. NM_006581.3.
UniGene	Hs.49117.
3D structure databases
ProteinModelPortal	Q9Y231.
SMR	Q9Y231. Positions 183-313.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y231. 1 interaction.
STRING	9606.ENSP00000302599.
Protein family/group databases
CAZy	GT10. Glycosyltransferase Family 10.
PTM databases
PhosphoSite	Q9Y231.
Polymorphism databases
DMDM	311033382.
Proteomic databases
PaxDb	Q9Y231.
PRIDE	Q9Y231.
Protocols and materials databases
DNASU	10690.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000302103; ENSP00000302599; ENSG00000172461.
GeneID	10690.
KEGG	hsa:10690.
UCSC	uc003pop.4. human.
Organism-specific databases
CTD	10690.
GeneCards	GC06P096463.
H-InvDB	HIX0025005.
HGNC	HGNC:4020. FUT9.
MIM	606865. gene.
neXtProt	NX_Q9Y231.
PharmGKB	PA28436.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG19459.
HOGENOM	HOG000045583.
HOVERGEN	HBG000274.
InParanoid	Q9Y231.
KO	K03663.
OMA	LIWVWPF.
OrthoDB	EOG412M5N.
PhylomeDB	Q9Y231.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q9Y231.
CleanEx	HS_FUT9.
Genevestigator	Q9Y231.
GermOnline	ENSG00000172461. Homo sapiens.
Family and domain databases
InterPro	IPR001503. Glyco_trans_10. [Graphical view]
PANTHER	PTHR11929. PTHR11929. 1 hit.
Pfam	PF00852. Glyco_transf_10. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL4985.
ChiTaRS	FUT9. human.
GenomeRNAi	10690.
NextBio	40631.
SOURCE	Search...

Entry information

Entry name

FUT9_HUMAN

Accession

Primary (citable) accession number: Q9Y231
Secondary accession number(s): Q5T0W4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 9, 2004
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.