Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9WTS2

- FUT8_MOUSE

UniProt

Q9WTS2 - FUT8_MOUSE

Protein

Alpha-(1,6)-fucosyltransferase

Gene

Fut8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    GO - Cellular componenti

    1. Golgi cisterna membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 99CytoplasmicSequence Analysis
    Topological domaini31 – 575545LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 123 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