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Q9WTS2 (FUT8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Alpha-(1,6)-fucosyltransferase

Short name=Alpha1-6FucT
EC=2.4.1.68
Alternative name(s):
Fucosyltransferase 8
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
GDP-fucose--glycoprotein fucosyltransferase
Glycoprotein 6-alpha-L-fucosyltransferase
Gene names
Name:Fut8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans By similarity.

Catalytic activity

GDP-beta-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine.

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.

Sequence similarities

Belongs to the glycosyltransferase 23 family.

Contains 1 GT23 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSH3 domain
SH3-binding
Signal-anchor
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGDP-L-fucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

N-glycan fucosylation

Inferred from sequence or structural similarity. Source: GOC

cell migration

Inferred from mutant phenotype PubMed 17043354. Source: MGI

fucosylation

Inferred from mutant phenotype PubMed 16236725PubMed 17043354. Source: GOC

integrin-mediated signaling pathway

Inferred from mutant phenotype PubMed 17043354. Source: MGI

protein N-linked glycosylation via asparagine

Inferred from sequence or structural similarity. Source: UniProtKB

protein glycosylation in Golgi

Inferred from electronic annotation. Source: InterPro

receptor metabolic process

Inferred from mutant phenotype PubMed 16236725. Source: MGI

respiratory gaseous exchange

Inferred from mutant phenotype PubMed 16236725. Source: MGI

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 16236725. Source: MGI

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionalpha-(1->6)-fucosyltransferase activity

Inferred from mutant phenotype PubMed 16236725PubMed 17043354. Source: MGI

glycoprotein 6-alpha-L-fucosyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transferase activity, transferring glycosyl groups

Inferred from sequence alignment Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 575575Alpha-(1,6)-fucosyltransferase
PRO_0000080527

Regions

Topological domain1 – 99Cytoplasmic Potential
Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 575545Lumenal Potential
Domain206 – 493288GT23
Domain502 – 56362SH3
Region365 – 3662Important for donor substrate binding
Motif299 – 3057SH3-binding Potential

Amino acid modifications

Disulfide bond204 ↔ 266 By similarity
Disulfide bond212 ↔ 230 By similarity
Disulfide bond218 ↔ 222 By similarity
Disulfide bond465 ↔ 472 By similarity

Experimental info

Sequence conflict401S → T in BAA76392. Ref.1
Sequence conflict3881E → Q in BAA76392. Ref.1
Sequence conflict4181K → N in BAA76392. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9WTS2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 226092A8959B3EB7

FASTA57566,557
        10         20         30         40         50         60 
MRAWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL ERLKQQNEDL 

        70         80         90        100        110        120 
RRMAESLRIP EGPIDQGTAT GRVRVLEEQL VKAKEQIENY KKQARNGLGK DHEILRRRIE 

       130        140        150        160        170        180 
NGAKELWFFL QSELKKLKHL EGNELQRHAD EILLDLGHHE RSIMTDLYYL SQTDGAGDWR 

       190        200        210        220        230        240 
EKEAKDLTEL VQRRITYLQN PKDCSKARKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT 

       250        260        270        280        290        300 
LILESQNWRY ATGGWETVFR PVSETCTDRS GLSTGHWSGE VNDKNIQVVE LPIVDSLHPR 

       310        320        330        340        350        360 
PPYLPLAVPE DLADRLLRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT KKLGFKHPVI 

       370        380        390        400        410        420 
GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD KKRVYLATDD PTLLKEAKTK 

       430        440        450        460        470        480 
YSNYEFISDN SISWSAGLHN RYTENSLRGV ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ 

       490        500        510        520        530        540 
TLHPDASANF HSLDDIYYFG GQNAHNQIAV YPHKPRTEEE IPMEPGDIIG VAGNHWDGYS 

       550        560        570 
KGINRKLGKT GLYPSYKVRE KIETVKYPTY PEAEK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of mouse alpha-1,6-fucosyltransferase and expression of its mRNA in the developing cerebrum."
Hayashi H., Yoneda A., Asada M., Ikekita M., Imamura T.
DNA Seq. 11:91-96(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Eye and Head.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025198 mRNA. Translation: BAA76392.1.
AK048520 mRNA. Translation: BAC33357.1.
AK051811 mRNA. Translation: BAC34777.1.
CH466526 Genomic DNA. Translation: EDL36441.1.
CH466526 Genomic DNA. Translation: EDL36443.1.
BC010666 mRNA. Translation: AAH10666.1.
RefSeqNP_001239543.1. NM_001252614.1.
NP_001239544.1. NM_001252615.1.
NP_001239545.1. NM_001252616.1.
NP_058589.2. NM_016893.5.
UniGeneMm.35628.
Mm.489686.

3D structure databases

ProteinModelPortalQ9WTS2.
SMRQ9WTS2. Positions 108-572.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT23. Glycosyltransferase Family 23.

PTM databases

PhosphoSiteQ9WTS2.

Proteomic databases

PaxDbQ9WTS2.
PRIDEQ9WTS2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062804; ENSMUSP00000054530; ENSMUSG00000021065.
ENSMUST00000171770; ENSMUSP00000130845; ENSMUSG00000021065.
ENSMUST00000177595; ENSMUSP00000136327; ENSMUSG00000021065.
GeneID53618.
KEGGmmu:53618.
UCSCuc007nyy.2. mouse.

Organism-specific databases

CTD2530.
MGIMGI:1858901. Fut8.

Phylogenomic databases

eggNOGNOG251249.
GeneTreeENSGT00530000063737.
HOGENOMHOG000007175.
HOVERGENHBG028260.
InParanoidQ543F5.
KOK00717.
OMAHNQIAVY.
OrthoDBEOG7N37C3.
TreeFamTF106108.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9WTS2.
BgeeQ9WTS2.
CleanExMM_FUT8.
GenevestigatorQ9WTS2.

Family and domain databases

InterProIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PIRSFPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS51659. GT23. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio310339.
PROQ9WTS2.
SOURCESearch...

Entry information

Entry nameFUT8_MOUSE
AccessionPrimary (citable) accession number: Q9WTS2
Secondary accession number(s): Q543F5, Q921U1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot