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Protein

Alpha-(1,6)-fucosyltransferase

Gene

Fut8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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.

Pathwayi

GO - Molecular functioni

  1. alpha-(1->6)-fucosyltransferase activity Source: MGI
  2. glycoprotein 6-alpha-L-fucosyltransferase activity Source: UniProtKB
  3. transferase activity, transferring glycosyl groups Source: MGI

GO - Biological processi

  1. cell migration Source: MGI
  2. GDP-L-fucose metabolic process Source: UniProtKB
  3. integrin-mediated signaling pathway Source: MGI
  4. N-glycan fucosylation Source: MGI
  5. protein glycosylation in Golgi Source: InterPro
  6. protein N-linked glycosylation via asparagine Source: UniProtKB
  7. receptor metabolic process Source: MGI
  8. respiratory gaseous exchange Source: MGI
  9. transforming growth factor beta receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_198568. Reactions specific to the complex N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT23. Glycosyltransferase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-(1,6)-fucosyltransferase (EC:2.4.1.68)
Short name:
Alpha1-6FucT
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 namesi
Name:Fut8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1858901. Fut8.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini31 – 575545LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. Golgi cisterna membrane Source: UniProtKB-SubCell
  4. integral component of membrane Source: UniProtKB-KW
  5. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 575575Alpha-(1,6)-fucosyltransferasePRO_0000080527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi204 ↔ 266By similarity
Disulfide bondi212 ↔ 230By similarity
Disulfide bondi218 ↔ 222By similarity
Disulfide bondi465 ↔ 472By similarity

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9WTS2.
PaxDbiQ9WTS2.
PRIDEiQ9WTS2.

PTM databases

PhosphoSiteiQ9WTS2.

Expressioni

Gene expression databases

BgeeiQ9WTS2.
CleanExiMM_FUT8.
ExpressionAtlasiQ9WTS2. baseline and differential.
GenevestigatoriQ9WTS2.

Structurei

3D structure databases

ProteinModelPortaliQ9WTS2.
SMRiQ9WTS2. Positions 108-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 493288GT23PROSITE-ProRule annotationAdd
BLAST
Domaini502 – 56362SH3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni365 – 3662Important for donor substrate binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi299 – 3057SH3-bindingSequence Analysis

Sequence similaritiesi

Belongs to the glycosyltransferase 23 family.PROSITE-ProRule annotation
Contains 1 GT23 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain, SH3-binding, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG251249.
GeneTreeiENSGT00530000063737.
HOGENOMiHOG000007175.
HOVERGENiHBG028260.
InParanoidiQ9WTS2.
KOiK00717.
OMAiNDKDVQV.
OrthoDBiEOG7N37C3.
TreeFamiTF106108.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51659. GT23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WTS2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL
60 70 80 90 100
ERLKQQNEDL RRMAESLRIP EGPIDQGTAT GRVRVLEEQL VKAKEQIENY
110 120 130 140 150
KKQARNGLGK DHEILRRRIE NGAKELWFFL QSELKKLKHL EGNELQRHAD
160 170 180 190 200
EILLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN
210 220 230 240 250
PKDCSKARKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY
260 270 280 290 300
ATGGWETVFR PVSETCTDRS GLSTGHWSGE VNDKNIQVVE LPIVDSLHPR
310 320 330 340 350
PPYLPLAVPE DLADRLLRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT
360 370 380 390 400
KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD
410 420 430 440 450
KKRVYLATDD PTLLKEAKTK YSNYEFISDN SISWSAGLHN RYTENSLRGV
460 470 480 490 500
ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG
510 520 530 540 550
GQNAHNQIAV YPHKPRTEEE IPMEPGDIIG VAGNHWDGYS KGINRKLGKT
560 570
GLYPSYKVRE KIETVKYPTY PEAEK
Length:575
Mass (Da):66,557
Last modified:July 27, 2011 - v2
Checksum:i226092A8959B3EB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401S → T in BAA76392 (PubMed:10902914).Curated
Sequence conflicti388 – 3881E → Q in BAA76392 (PubMed:10902914).Curated
Sequence conflicti418 – 4181K → N in BAA76392 (PubMed:10902914).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25999.1.
RefSeqiNP_001239543.1. NM_001252614.1.
NP_001239544.1. NM_001252615.1.
NP_001239545.1. NM_001252616.1.
NP_058589.2. NM_016893.5.
UniGeneiMm.35628.
Mm.489686.

Genome annotation databases

EnsembliENSMUST00000062804; ENSMUSP00000054530; ENSMUSG00000021065.
ENSMUST00000171770; ENSMUSP00000130845; ENSMUSG00000021065.
ENSMUST00000177595; ENSMUSP00000136327; ENSMUSG00000021065.
GeneIDi53618.
KEGGimmu:53618.
UCSCiuc007nyy.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Fucosyltransferase 8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25999.1.
RefSeqiNP_001239543.1. NM_001252614.1.
NP_001239544.1. NM_001252615.1.
NP_001239545.1. NM_001252616.1.
NP_058589.2. NM_016893.5.
UniGeneiMm.35628.
Mm.489686.

3D structure databases

ProteinModelPortaliQ9WTS2.
SMRiQ9WTS2. Positions 108-572.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT23. Glycosyltransferase Family 23.

PTM databases

PhosphoSiteiQ9WTS2.

Proteomic databases

MaxQBiQ9WTS2.
PaxDbiQ9WTS2.
PRIDEiQ9WTS2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062804; ENSMUSP00000054530; ENSMUSG00000021065.
ENSMUST00000171770; ENSMUSP00000130845; ENSMUSG00000021065.
ENSMUST00000177595; ENSMUSP00000136327; ENSMUSG00000021065.
GeneIDi53618.
KEGGimmu:53618.
UCSCiuc007nyy.2. mouse.

Organism-specific databases

CTDi2530.
MGIiMGI:1858901. Fut8.

Phylogenomic databases

eggNOGiNOG251249.
GeneTreeiENSGT00530000063737.
HOGENOMiHOG000007175.
HOVERGENiHBG028260.
InParanoidiQ9WTS2.
KOiK00717.
OMAiNDKDVQV.
OrthoDBiEOG7N37C3.
TreeFamiTF106108.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_198568. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

NextBioi310339.
PROiQ9WTS2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTS2.
CleanExiMM_FUT8.
ExpressionAtlasiQ9WTS2. baseline and differential.
GenevestigatoriQ9WTS2.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51659. GT23. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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].

Entry informationi

Entry nameiFUT8_MOUSE
AccessioniPrimary (citable) accession number: Q9WTS2
Secondary accession number(s): Q543F5, Q921U1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.