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Q9VYV5

- FUT8_DROME

UniProt

Q9VYV5 - FUT8_DROME

Protein

Alpha-(1,6)-fucosyltransferase

Gene

FucT6

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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: FlyBase
    2. glycoprotein 6-alpha-L-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. fucosylation Source: GOC
    2. GDP-L-fucose metabolic process Source: UniProtKB
    3. N-glycan fucosylation Source: GOC
    4. protein glycosylation in Golgi Source: InterPro
    5. protein N-linked glycosylation via asparagine Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_180687. 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):
    GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
    GDP-fucose--glycoprotein fucosyltransferase
    Glycoprotein 6-alpha-L-fucosyltransferase
    Gene namesi
    Name:FucT6
    ORF Names:CG2448
    OrganismiDrosophila melanogaster (Fruit fly)Imported
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0030327. FucT6.

    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 – 619619Alpha-(1,6)-fucosyltransferasePRO_0000080530Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi253 ↔ 315By similarity
    Disulfide bondi261 ↔ 279By similarity
    Disulfide bondi267 ↔ 271By similarity
    Disulfide bondi511 ↔ 518By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9VYV5.
    PRIDEiQ9VYV5.

    Expressioni

    Gene expression databases

    BgeeiQ9VYV5.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CG3916Q9VGB81EBI-172309,EBI-147840
    Ipk2Q9VPR61EBI-172309,EBI-83394

    Protein-protein interaction databases

    BioGridi58529. 3 interactions.
    DIPiDIP-21409N.
    IntActiQ9VYV5. 2 interactions.
    MINTiMINT-900962.
    STRINGi7227.FBpp0073457.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VYV5.
    SMRiQ9VYV5. Positions 155-616.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini39 – 619581LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei18 – 3821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini255 – 539285GT23PROSITE-ProRule annotationAdd
    BLAST
    Domaini548 – 60962SH3By similarityAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni411 – 4122Important for donor substrate bindingPROSITE-ProRule annotation

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi345 – 3517SH3-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, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG251249.
    GeneTreeiENSGT00530000063737.
    InParanoidiQ9VYV5.
    KOiK00717.
    OMAiDPIVWWV.
    OrthoDBiEOG7N37C3.
    PhylomeDBiQ9VYV5.

    Family and domain databases

    InterProiIPR015827. Alpha1_6FUT_euk.
    IPR027350. GT23_dom.
    IPR001452. SH3_domain.
    [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.

    Q9VYV5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLVRQLFGA SANSWARALI IFVLAWIGLV YVFVVKLTNT QGQQAAGESE    50
    LNARRISQAL QMLEHTRQRN EELKQLIDEL MSDQLDKQSA MKLVQRLEND 100
    ALNPKLAPEV AGPEPESMFE SAPADLRGWN NVAEGAPNDL EAGVPDHGEF 150
    EPSLEYEFTR RRIQTNIGEI WNFFSSELGK VRKAVAAGHA SADLEESINQ 200
    VLLQGAEHKR SLLSDMERMR QSDGYEAWRH KEARDLSDLV QRRLHHLQNP 250
    SDCQNARKLV CKLNKGCGYG CQLHHVVYCF IVAYATERTL ILKSRGWRYH 300
    KGGWEEVFQP VSNSCHDAGT ANTYNWPGKP NTQVLVLPII DSLMPRPPYL 350
    PLAVPEDLAP RLKRLHGDPI VWWVGQFLKY LLRPQPTTRD FLTSGMRNLG 400
    WERPIVGVHV RRTDKVGTEA ACHSVEEYMT YVEDYYRTLE VNGSTVARRI 450
    FLASDDAQVI EEARRKYPQY QIIGDPEVAR MASVSTRYTD TALNGIILDI 500
    HLLSMSDHLV CTFSSQVCRV AYEIMQTMYP DAAHRFKSLD DIYYYGGQNA 550
    HNRRVVIAHK PRTHEDLQLR VGDLVSVAGN HWDGNSKGKN TRTNQGGLFP 600
    SFKVEEKVDT AKLPLYAGI 619
    Length:619
    Mass (Da):70,206
    Last modified:May 1, 2000 - v1
    Checksum:i691BFD9B5C6557DE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF441264 mRNA. Translation: AAN63649.1.
    AE014298 Genomic DNA. Translation: AAF48079.1.
    AY051451 mRNA. Translation: AAK92875.1.
    RefSeqiNP_572740.1. NM_132512.4.
    UniGeneiDm.4605.

    Genome annotation databases

    EnsemblMetazoaiFBtr0073620; FBpp0073457; FBgn0030327.
    GeneIDi32122.
    KEGGidme:Dmel_CG2448.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF441264 mRNA. Translation: AAN63649.1 .
    AE014298 Genomic DNA. Translation: AAF48079.1 .
    AY051451 mRNA. Translation: AAK92875.1 .
    RefSeqi NP_572740.1. NM_132512.4.
    UniGenei Dm.4605.

    3D structure databases

    ProteinModelPortali Q9VYV5.
    SMRi Q9VYV5. Positions 155-616.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 58529. 3 interactions.
    DIPi DIP-21409N.
    IntActi Q9VYV5. 2 interactions.
    MINTi MINT-900962.
    STRINGi 7227.FBpp0073457.

    Protein family/group databases

    CAZyi GT23. Glycosyltransferase Family 23.

    Proteomic databases

    PaxDbi Q9VYV5.
    PRIDEi Q9VYV5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0073620 ; FBpp0073457 ; FBgn0030327 .
    GeneIDi 32122.
    KEGGi dme:Dmel_CG2448.

    Organism-specific databases

    CTDi 32122.
    FlyBasei FBgn0030327. FucT6.

    Phylogenomic databases

    eggNOGi NOG251249.
    GeneTreei ENSGT00530000063737.
    InParanoidi Q9VYV5.
    KOi K00717.
    OMAi DPIVWWV.
    OrthoDBi EOG7N37C3.
    PhylomeDBi Q9VYV5.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_180687. Reactions specific to the complex N-glycan synthesis pathway.

    Miscellaneous databases

    ChiTaRSi FucT6. drosophila.
    GenomeRNAii 32122.
    NextBioi 776952.
    PROi Q9VYV5.

    Gene expression databases

    Bgeei Q9VYV5.

    Family and domain databases

    InterProi IPR015827. Alpha1_6FUT_euk.
    IPR027350. GT23_dom.
    IPR001452. SH3_domain.
    [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. "Core a3- and a6-fucosyltransferases in Drosophila: characterization and origin of diversity."
      Petit D., Picaud F., Dupuy F., Germot A., Julien R., Maftah A.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Testis.
    5. "Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism."
      Roos C., Kolmer M., Mattila P., Renkonen R.
      J. Biol. Chem. 277:3168-3175(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOLOGY.

    Entry informationi

    Entry nameiFUT8_DROME
    AccessioniPrimary (citable) accession number: Q9VYV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3