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Q18014

- OFUT1_CAEEL

UniProt

Q18014 - OFUT1_CAEEL

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

C15C7.7

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 5 (01 Feb 2005)
      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 in EGF domains.1 Publication

    Catalytic activityi

    Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei334 – 3341Substrate

    GO - Molecular functioni

    1. fucosyltransferase activity Source: UniProtKB
    2. peptide-O-fucosyltransferase activity Source: WormBase

    GO - Biological processi

    1. fucose metabolic process Source: UniProtKB-KW
    2. Notch signaling pathway Source: UniProtKB-KW
    3. protein O-linked fucosylation Source: WormBase
    4. protein O-linked glycosylation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    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):
    Peptide-O-fucosyltransferase 1
    Short name:
    O-FucT-1
    Gene namesi
    ORF Names:C15C7.7
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome X

    Organism-specific databases

    WormBaseiC15C7.7; CE36786; WBGene00015793.

    Subcellular locationi

    Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: WormBase

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431N → A: Reduces enzyme activity by over 90%. 1 Publication
    Mutagenesisi240 – 2401R → A or K: Abolishes enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 389368GDP-fucose protein O-fucosyltransferase 1PRO_0000012152Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Curated
    Disulfide bondi35 ↔ 371 Publication
    Disulfide bondi119 ↔ 1351 Publication
    Disulfide bondi249 ↔ 2811 Publication
    Disulfide bondi266 ↔ 3531 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ18014.
    PRIDEiQ18014.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    389
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 344
    Beta strandi38 – 403
    Helixi41 – 5818
    Beta strandi61 – 633
    Beta strandi67 – 693
    Beta strandi71 – 744
    Beta strandi76 – 783
    Helixi80 – 834
    Helixi86 – 894
    Turni90 – 923
    Helixi98 – 1047
    Helixi106 – 1094
    Helixi112 – 1143
    Beta strandi116 – 1216
    Helixi143 – 1497
    Beta strandi156 – 1594
    Turni164 – 1674
    Beta strandi170 – 1723
    Helixi178 – 1814
    Turni184 – 1863
    Beta strandi188 – 1947
    Helixi203 – 2119
    Helixi216 – 22914
    Beta strandi232 – 2398
    Helixi243 – 2508
    Turni254 – 2563
    Turni261 – 2633
    Helixi264 – 2674
    Helixi269 – 2713
    Helixi278 – 2814
    Helixi285 – 29915
    Beta strandi302 – 3109
    Helixi314 – 3218
    Helixi322 – 3243
    Helixi336 – 34510
    Beta strandi346 – 3516
    Helixi356 – 36712
    Beta strandi368 – 3714
    Beta strandi375 – 3773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZY2X-ray1.54A26-383[»]
    3ZY3X-ray1.86A/B26-383[»]
    3ZY4X-ray1.74A26-383[»]
    3ZY5X-ray1.96A26-383[»]
    3ZY6X-ray1.91A26-383[»]
    ProteinModelPortaliQ18014.
    SMRiQ18014. Positions 26-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ18014.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 433Substrate binding
    Regioni238 – 2403Substrate binding
    Regioni355 – 3562Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250895.
    GeneTreeiENSGT00390000015634.
    HOGENOMiHOG000231651.
    InParanoidiQ18014.
    KOiK03691.
    OMAiSEHPVLA.
    OrthoDBiEOG7ZD1VC.
    PhylomeDBiQ18014.

    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.

    Q18014-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRVSKVLTLA SFISVCSYSE AKSNETDPNG YIVFCPCMGR FGNQVDQFLG    50
    VLAFAKALDR TLVLPNFIEF KHPETKMIPF EFLFQVGTVA KYTRVVTMQE 100
    FTKKIMPTVW PPEKRKAFCW TPRQAIYDKS AEPGCHSKEG NPFGPYWDQI 150
    DVSFVGDEYF GDIPGGFDLN QMGSRKKWLE KFPSEEYPVL AFSSAPAPFP 200
    SKGKVWSIQK YLRWSSRITE QAKKFISANL AKPFVAVHLR NDADWVRVCE 250
    HIDTTTNRPL FASEQCLGEG HHLGTLTKEI CSPSKQQILE QIVEKVGSIG 300
    AKSVFVASDK DHMIDEINEA LKPYEIEAHR QEPDDMYTSL AIMGRADLFV 350
    GNCVSTFSHI VKRERDHAGQ SPRPSAFFGI RAVKRHIDL 389
    Length:389
    Mass (Da):44,051
    Last modified:February 1, 2005 - v5
    Checksum:i0C84F202AA184554
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FO080550 Genomic DNA. Translation: CCD64591.1.
    RefSeqiNP_741744.2. NM_171649.6.
    UniGeneiCel.30602.

    Genome annotation databases

    EnsemblMetazoaiC15C7.7; C15C7.7; WBGene00015793.
    GeneIDi180607.
    KEGGicel:CELE_C15C7.7.
    UCSCiC15C7.7. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FO080550 Genomic DNA. Translation: CCD64591.1 .
    RefSeqi NP_741744.2. NM_171649.6.
    UniGenei Cel.30602.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZY2 X-ray 1.54 A 26-383 [» ]
    3ZY3 X-ray 1.86 A/B 26-383 [» ]
    3ZY4 X-ray 1.74 A 26-383 [» ]
    3ZY5 X-ray 1.96 A 26-383 [» ]
    3ZY6 X-ray 1.91 A 26-383 [» ]
    ProteinModelPortali Q18014.
    SMRi Q18014. Positions 26-381.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT65. Glycosyltransferase Family 65.

    Proteomic databases

    PaxDbi Q18014.
    PRIDEi Q18014.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai C15C7.7 ; C15C7.7 ; WBGene00015793 .
    GeneIDi 180607.
    KEGGi cel:CELE_C15C7.7.
    UCSCi C15C7.7. c. elegans.

    Organism-specific databases

    CTDi 180607.
    WormBasei C15C7.7 ; CE36786 ; WBGene00015793 .

    Phylogenomic databases

    eggNOGi NOG250895.
    GeneTreei ENSGT00390000015634.
    HOGENOMi HOG000231651.
    InParanoidi Q18014.
    KOi K03691.
    OMAi SEHPVLA.
    OrthoDBi EOG7ZD1VC.
    PhylomeDBi Q18014.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    EvolutionaryTracei Q18014.
    NextBioi 910082.
    PROi Q18014.

    Family and domain databases

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

    Publicationsi

    1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    2. "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.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 26-383 IN COMPLEX WITH GDP-FUCOSE AND MANGANESE, ABSENCE OF COFACTOR REQUIREMENT, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF ASN-43 AND ARG-240.

    Entry informationi

    Entry nameiOFUT1_CAEEL
    AccessioniPrimary (citable) accession number: Q18014
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 91 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Miscellaneous

    Manganese is bound to the substrate GDP-fucose, but is not required for enzyme activity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3