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)

Q9W589

- OFUT2_DROME

UniProt

Q9W589 - OFUT2_DROME

Protein

GDP-fucose protein O-fucosyltransferase 2

Gene

O-fut2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of a number of protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Does not require divalent metal ions for optimal activity.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei443 – 4431Essential for catalytic activityBy similarity

    GO - Molecular functioni

    1. peptide-O-fucosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. embryo development Source: UniProtKB
    2. fucose metabolic process Source: UniProtKB-KW
    3. O-glycan processing Source: UniProtKB
    4. protein O-linked fucosylation Source: GOC
    5. regulation of transcription, DNA-templated Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism

    Enzyme and pathway databases

    ReactomeiREACT_218181. O-glycosylation of TSR domain-containing proteins.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT68. Glycosyltransferase Family 68.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-fucose protein O-fucosyltransferase 2 (EC:2.4.1.221)
    Alternative name(s):
    Peptide-O-fucosyltransferase 2
    Short name:
    O-FucT-2
    Gene namesi
    Name:O-fut2
    ORF Names:CG14789
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome X

    Organism-specific databases

    FlyBaseiFBgn0027791. O-fut2.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication. Golgi apparatus 1 Publication
    Note: Mainly located in the endoplasmic reticulum.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. Golgi apparatus Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Golgi apparatus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi442 – 4421E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-443. 1 Publication
    Mutagenesisi443 – 4431E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-442. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 490465GDP-fucose protein O-fucosyltransferase 2PRO_0000236806Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9W589.
    PRIDEiQ9W589.

    Expressioni

    Gene expression databases

    BgeeiQ9W589.

    Interactioni

    Protein-protein interaction databases

    BioGridi57655. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9W589.
    SMRiQ9W589. Positions 73-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77810.
    GeneTreeiENSGT00390000007989.
    InParanoidiQ9W589.
    KOiK03691.
    OMAiICAHARF.
    OrthoDBiEOG76T9S1.
    PhylomeDBiQ9W589.

    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.

    Q9W589-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGSWPRLGF PALLLLLHLL TGSDAAVRNG TAKREIGDSR GSSGTCVKGF    50
    LQEILPLPAT CPPEVLGMRG AVYILYDVNI SEGFNLRRDV YIRMAVFVRR 100
    LQRRRRFRHV RLVLPPWPRL YHWHSQGLQQ SGLPWSHFFD LASLRRYAPV 150
    LDYEEFLAEQ RLFGNPGAPL VHVGHAFRLQ HYEVMLEQGI FRDKFERVTD 200
    KPCSEGSLSG GPLLQQAELR VGRFHCVRFQ GSAGLLEKLL REAIDEDTAG 250
    PEDVDDMRTY ALLSAETVLH DHWGDEHFWQ ARRSMRFARR LEQVAADFRR 300
    QALDTTDASA GVQRPAMWEL ERPKRNAKGG DYLCAHLRRG DFVRSRDATT 350
    PTLKAAAQQV KQLLRGFNMT TVFLATDATP YELMELKELF YRFRLVHFAP 400
    ESNVQRRELK DGGVAVVDQL VCAYARYFVG TYESTFTYRI YEEREILGFT 450
    QASTFNTFCK ALGGSCSRNA VWPIVWADGD SDSEEDSDPY 490
    Length:490
    Mass (Da):56,021
    Last modified:May 1, 2000 - v1
    Checksum:i54038E7CDD020768
    GO

    Sequence cautioni

    The sequence CAB53644.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF45629.1.
    AL031027 Genomic DNA. No translation available.
    AL035632 Genomic DNA. Translation: CAB53644.1. Sequence problems.
    AY047568 mRNA. Translation: AAK77300.1.
    RefSeqiNP_569916.1. NM_130560.3.
    UniGeneiDm.4643.

    Genome annotation databases

    EnsemblMetazoaiFBtr0070296; FBpp0070283; FBgn0027791.
    GeneIDi31098.
    KEGGidme:Dmel_CG14789.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014298 Genomic DNA. Translation: AAF45629.1 .
    AL031027 Genomic DNA. No translation available.
    AL035632 Genomic DNA. Translation: CAB53644.1 . Sequence problems.
    AY047568 mRNA. Translation: AAK77300.1 .
    RefSeqi NP_569916.1. NM_130560.3.
    UniGenei Dm.4643.

    3D structure databases

    ProteinModelPortali Q9W589.
    SMRi Q9W589. Positions 73-476.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 57655. 1 interaction.

    Protein family/group databases

    CAZyi GT68. Glycosyltransferase Family 68.

    Proteomic databases

    PaxDbi Q9W589.
    PRIDEi Q9W589.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0070296 ; FBpp0070283 ; FBgn0027791 .
    GeneIDi 31098.
    KEGGi dme:Dmel_CG14789.

    Organism-specific databases

    CTDi 31098.
    FlyBasei FBgn0027791. O-fut2.

    Phylogenomic databases

    eggNOGi NOG77810.
    GeneTreei ENSGT00390000007989.
    InParanoidi Q9W589.
    KOi K03691.
    OMAi ICAHARF.
    OrthoDBi EOG76T9S1.
    PhylomeDBi Q9W589.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_218181. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    GenomeRNAii 31098.
    NextBioi 771923.
    PROi Q9W589.

    Gene expression databases

    Bgeei Q9W589.

    Family and domain databases

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

    Publicationsi

    1. "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.
    2. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Oregon-R.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    5. "Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats."
      Luo Y., Koles K., Vorndam W., Haltiwanger R.S., Panin V.M.
      J. Biol. Chem. 281:9393-9399(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442 AND GLU-443.

    Entry informationi

    Entry nameiOFUT2_DROME
    AccessioniPrimary (citable) accession number: Q9W589
    Secondary accession number(s): Q7K729, Q9U985
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 92 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