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Q9WTS2

- FUT8_MOUSE

UniProt

Q9WTS2 - FUT8_MOUSE

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Protein

Alpha-(1,6)-fucosyltransferase

Gene
Fut8
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. fucosylation Source: GOC
  3. GDP-L-fucose metabolic process Source: UniProtKB
  4. integrin-mediated signaling pathway Source: MGI
  5. N-glycan fucosylation Source: GOC
  6. protein glycosylation in Golgi Source: InterPro
  7. protein N-linked glycosylation via asparagine Source: UniProtKB
  8. receptor metabolic process Source: MGI
  9. respiratory gaseous exchange Source: MGI
  10. 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; 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 – 99Cytoplasmic Reviewed prediction
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini31 – 575545Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
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 ↔ 266 By similarity
Disulfide bondi212 ↔ 230 By similarity
Disulfide bondi218 ↔ 222 By similarity
Disulfide bondi465 ↔ 472 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9WTS2.
PRIDEiQ9WTS2.

PTM databases

PhosphoSiteiQ9WTS2.

Expressioni

Gene expression databases

ArrayExpressiQ9WTS2.
BgeeiQ9WTS2.
CleanExiMM_FUT8.
GenevestigatoriQ9WTS2.

Structurei

3D structure databases

ProteinModelPortaliQ9WTS2.
SMRiQ9WTS2. Positions 108-572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 493288GT23Add
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-binding Reviewed prediction

Sequence similaritiesi

Contains 1 GT23 domain.
Contains 1 SH3 domain.

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG251249.
GeneTreeiENSGT00530000063737.
HOGENOMiHOG000007175.
HOVERGENiHBG028260.
InParanoidiQ543F5.
KOiK00717.
OMAiRMHVDKK.
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

MRAWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL    50
ERLKQQNEDL RRMAESLRIP EGPIDQGTAT GRVRVLEEQL VKAKEQIENY 100
KKQARNGLGK DHEILRRRIE NGAKELWFFL QSELKKLKHL EGNELQRHAD 150
EILLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN 200
PKDCSKARKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY 250
ATGGWETVFR PVSETCTDRS GLSTGHWSGE VNDKNIQVVE LPIVDSLHPR 300
PPYLPLAVPE DLADRLLRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT 350
KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD 400
KKRVYLATDD PTLLKEAKTK YSNYEFISDN SISWSAGLHN RYTENSLRGV 450
ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG 500
GQNAHNQIAV YPHKPRTEEE IPMEPGDIIG VAGNHWDGYS KGINRKLGKT 550
GLYPSYKVRE KIETVKYPTY PEAEK 575
Length:575
Mass (Da):66,557
Last modified:July 27, 2011 - v2
Checksum:i226092A8959B3EB7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401S → T in BAA76392. 1 Publication
Sequence conflicti388 – 3881E → Q in BAA76392. 1 Publication
Sequence conflicti418 – 4181K → N in BAA76392. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25999.1.
RefSeqi NP_001239543.1. NM_001252614.1.
NP_001239544.1. NM_001252615.1.
NP_001239545.1. NM_001252616.1.
NP_058589.2. NM_016893.5.
UniGenei Mm.35628.
Mm.489686.

3D structure databases

ProteinModelPortali Q9WTS2.
SMRi Q9WTS2. Positions 108-572.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT23. Glycosyltransferase Family 23.

PTM databases

PhosphoSitei Q9WTS2.

Proteomic databases

PaxDbi Q9WTS2.
PRIDEi Q9WTS2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000062804 ; ENSMUSP00000054530 ; ENSMUSG00000021065 .
ENSMUST00000171770 ; ENSMUSP00000130845 ; ENSMUSG00000021065 .
ENSMUST00000177595 ; ENSMUSP00000136327 ; ENSMUSG00000021065 .
GeneIDi 53618.
KEGGi mmu:53618.
UCSCi uc007nyy.2. mouse.

Organism-specific databases

CTDi 2530.
MGIi MGI:1858901. Fut8.

Phylogenomic databases

eggNOGi NOG251249.
GeneTreei ENSGT00530000063737.
HOGENOMi HOG000007175.
HOVERGENi HBG028260.
InParanoidi Q543F5.
KOi K00717.
OMAi RMHVDKK.
OrthoDBi EOG7N37C3.
TreeFami TF106108.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198568. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

NextBioi 310339.
PROi Q9WTS2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9WTS2.
Bgeei Q9WTS2.
CleanExi MM_FUT8.
Genevestigatori Q9WTS2.

Family and domain databases

InterProi IPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF14604. SH3_9. 1 hit.
[Graphical view ]
PIRSFi PIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTi SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS51659. GT23. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 122 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

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