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Q9V6X7

- OFUT1_DROME

UniProt

Q9V6X7 - OFUT1_DROME

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

O-fut1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines. Specifically uses GDP-fucose as donor substrate and proper disulfide pairing of the substrate EGF domains is required for fucose transfer. Plays a crucial role in Notch signaling. Initial fucosylation of Notch/N by POFUT1 generates a substrate for Fringe/Fng, an acetylglucosaminyltransferase that can then extend the fucosylation on the Notch EGF repeats. This extended fucosylation is required for optimal ligand binding and canonical NOTCH signaling induced by Delta/Dl or Serrate/Ser. Also required for the transport of Notch/N to the early endosome.3 Publications

    Catalytic activityi

    Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei344 – 3441SubstrateBy similarity

    GO - Molecular functioni

    1. fucosyltransferase activity Source: UniProtKB
    2. Notch binding Source: FlyBase
    3. peptide-O-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. embryo development Source: UniProtKB
    2. endocytosis Source: FlyBase
    3. fucose metabolic process Source: UniProtKB-KW
    4. fucosylation Source: GOC
    5. lateral inhibition Source: FlyBase
    6. negative regulation of Notch signaling pathway Source: FlyBase
    7. Notch signaling pathway Source: UniProtKB
    8. O-glycan processing Source: UniProtKB
    9. protein catabolic process Source: FlyBase
    10. protein O-linked fucosylation Source: GOC
    11. protein O-linked glycosylation Source: UniProtKB
    12. regulation of Notch signaling pathway Source: FlyBase
    13. regulation of transcription, DNA-templated Source: UniProtKB
    14. single organismal cell-cell adhesion Source: FlyBase

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

    Enzyme and pathway databases

    ReactomeiREACT_180761. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    SignaLinkiQ9V6X7.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT65. Glycosyltransferase Family 65.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-fucose protein O-fucosyltransferase 1 (EC:2.4.1.221)
    Alternative name(s):
    Neurotic protein
    Peptide-O-fucosyltransferase 1
    Short name:
    O-FucT-1
    Gene namesi
    Name:O-fut1
    Synonyms:nti
    ORF Names:CG12366
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0033901. O-fut1.

    Subcellular locationi

    Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: FlyBase
    3. endoplasmic reticulum Source: FlyBase

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 402379GDP-fucose protein O-fucosyltransferase 1PRO_0000012153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 38By similarity
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi122 ↔ 141By similarity
    Disulfide bondi254 ↔ 284By similarity
    Disulfide bondi269 ↔ 363By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9V6X7.
    PRIDEiQ9V6X7.

    Expressioni

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiQ9V6X7.

    Interactioni

    Subunit structurei

    Interacts with N (via its EGF domains); the interaction is required for the endocyctic transport of N.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CG9784Q9VXE71EBI-97485,EBI-165741
    SyndQ9VDI11EBI-97485,EBI-106353

    Protein-protein interaction databases

    BioGridi62315. 4 interactions.
    DIPiDIP-20580N.
    IntActiQ9V6X7. 3 interactions.
    MINTiMINT-304675.
    STRINGi7227.FBpp0086649.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9V6X7.
    SMRiQ9V6X7. Positions 28-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni42 – 443Substrate bindingBy similarity
    Regioni243 – 2453Substrate bindingBy similarity
    Regioni365 – 3662Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250895.
    GeneTreeiENSGT00390000015634.
    InParanoidiQ9V6X7.
    KOiK03691.
    OMAiSEHPVLA.
    OrthoDBiEOG7ZD1VC.
    PhylomeDBiQ9V6X7.

    Family and domain databases

    InterProiIPR019378. GDP-Fuc_O-FucTrfase.
    [Graphical view]
    PfamiPF10250. O-FucT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9V6X7-1 [UniParc]FASTAAdd to Basket

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    MQWLKMKLRF VNLILLLISS TCAQLGGDPN GYLTYCPCMG RFGNQADHFL    50
    GSLAFAKALN RTLILPPWVE YRRGELRSRQ VPFNTYFEVE PLKEYHRVIT 100
    MADFMWHLAD DIWPESERVS FCYKERYSLQ QEKNDPDKPN CHAKDGNPFG 150
    PFWDTFHIDF VRSEFYAPLH FDVHHSNEAA KWQTKYPAES YPVLAFTGAP 200
    ASFPVQLENC KLQRYLQWSQ RYREASKDFI REQLPRGAFL GIHLRNGIDW 250
    VRACEHVKDS QHLFASPQCL GYKNERGALY PELCMPSKEA IIRQLKRTIK 300
    NVRQTQPDNE IKSVFVASDS NHMIGELNTA LSRMGISVHK LPEDDPYLDL 350
    AILGQSNHFI GNCISSYSAF EKRERDVHGF PSYFWGFPKE KDRKHTNVHE 400
    EL 402
    Length:402
    Mass (Da):46,834
    Last modified:May 1, 2000 - v1
    Checksum:iE52FF4F86509C2E6
    GO

    Sequence cautioni

    The sequence AAM50020.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti371 – 3711E → V in AAM50020. (PubMed:12537569)Curated
    Sequence conflicti389 – 3891K → E in BAC55010. (PubMed:12917292)Curated
    Sequence conflicti389 – 3891K → E in AAX33443. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB093572 mRNA. Translation: BAC55010.1.
    AE013599 Genomic DNA. Translation: AAF58290.1.
    BT021295 mRNA. Translation: AAX33443.1.
    AY118651 mRNA. Translation: AAM50020.1. Different initiation.
    RefSeqiNP_610931.1. NM_137087.2.
    UniGeneiDm.30916.

    Genome annotation databases

    EnsemblMetazoaiFBtr0087520; FBpp0086649; FBgn0033901.
    GeneIDi36564.
    KEGGidme:Dmel_CG12366.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB093572 mRNA. Translation: BAC55010.1 .
    AE013599 Genomic DNA. Translation: AAF58290.1 .
    BT021295 mRNA. Translation: AAX33443.1 .
    AY118651 mRNA. Translation: AAM50020.1 . Different initiation.
    RefSeqi NP_610931.1. NM_137087.2.
    UniGenei Dm.30916.

    3D structure databases

    ProteinModelPortali Q9V6X7.
    SMRi Q9V6X7. Positions 28-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62315. 4 interactions.
    DIPi DIP-20580N.
    IntActi Q9V6X7. 3 interactions.
    MINTi MINT-304675.
    STRINGi 7227.FBpp0086649.

    Protein family/group databases

    CAZyi GT65. Glycosyltransferase Family 65.

    Proteomic databases

    PaxDbi Q9V6X7.
    PRIDEi Q9V6X7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087520 ; FBpp0086649 ; FBgn0033901 .
    GeneIDi 36564.
    KEGGi dme:Dmel_CG12366.

    Organism-specific databases

    CTDi 36564.
    FlyBasei FBgn0033901. O-fut1.

    Phylogenomic databases

    eggNOGi NOG250895.
    GeneTreei ENSGT00390000015634.
    InParanoidi Q9V6X7.
    KOi K03691.
    OMAi SEHPVLA.
    OrthoDBi EOG7ZD1VC.
    PhylomeDBi Q9V6X7.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_180761. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    SignaLinki Q9V6X7.

    Miscellaneous databases

    GenomeRNAii 36564.
    NextBioi 799227.
    PROi Q9V6X7.

    Gene expression databases

    Bgeei Q9V6X7.

    Family and domain databases

    InterProi IPR019378. GDP-Fuc_O-FucTrfase.
    [Graphical view ]
    Pfami PF10250. O-FucT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Neurotic, a novel maternal neurogenic gene, encodes an O-fucosyltransferase that is essential for Notch-Delta interactions."
      Sasamura T., Sasaki N., Miyashita F., Nakao S., Ishikawa H., Ito M., Kitagawa M., Harigaya K., Spana E., Bilder D., Perrmon N., Matsuno K.
      Development 130:4785-4795(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-402.
      Strain: Berkeley.
      Tissue: Embryo.
    6. "Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase."
      Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S.
      J. Biol. Chem. 276:40338-40345(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOLOGY.
    7. "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.
    8. "Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe."
      Okajima T., Xu A., Irvine K.D.
      J. Biol. Chem. 278:42340-42345(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila."
      Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S., Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.
      Development 134:1347-1356(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH N.

    Entry informationi

    Entry nameiOFUT1_DROME
    AccessioniPrimary (citable) accession number: Q9V6X7
    Secondary accession number(s): Q5BIC9, Q86SA7, Q8MSR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 101 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