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Q6EV70

- OFUT1_RAT

UniProt

Q6EV70 - OFUT1_RAT

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

Pofut1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      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. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) By similarity. Plays a crucial role in NOTCH signaling. Initial fucosylation of NOTCH by POFUT1 generates a substrate for FRINGE/RFNG, 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 DLL1 or JAGGED1.By similarity1 Publication

    Catalytic activityi

    Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor.By similarity1 Publication

    Enzyme regulationi

    Activated by manganese and, to a lesser extent, by calcium.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei342 – 3421SubstrateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. fucose metabolic process Source: UniProtKB-KW
    3. heart development Source: Ensembl
    4. nervous system development Source: Ensembl
    5. Notch signaling pathway Source: UniProtKB-KW
    6. protein O-linked glycosylation Source: UniProtKB
    7. somitogenesis Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

    Keywords - Ligandi

    Manganese

    Enzyme and pathway databases

    ReactomeiREACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.
    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
    Name:Pofut1Imported
    Synonyms:Fut12
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi1303001. Pofut1.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: RGD
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 395363GDP-fucose protein O-fucosyltransferase 1Sequence AnalysisPRO_0000012151Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi45 ↔ 47By similarity
    Glycosylationi69 – 691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi133 ↔ 147By similarity
    Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi256 ↔ 290By similarity
    Disulfide bondi274 ↔ 361By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ6EV70.
    PRIDEiQ6EV70.

    Expressioni

    Gene expression databases

    GenevestigatoriQ6EV70.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000013730.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 533Substrate bindingBy similarity
    Regioni245 – 2473Substrate bindingBy similarity
    Regioni363 – 3642Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi392 – 3954Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Sequence Analysis

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250895.
    GeneTreeiENSGT00390000015634.
    HOGENOMiHOG000231651.
    HOVERGENiHBG059976.
    InParanoidiQ6EV70.
    KOiK03691.
    OMAiSEHPVLA.
    OrthoDBiEOG7ZD1VC.
    PhylomeDBiQ6EV70.
    TreeFamiTF314805.

    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.

    Q6EV70-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAAAWAPSH LLLRASFLLL LLLLPLPLRG RAGGSWDLAG YLLYCPCMGR    50
    FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL 100
    EPLQAYHRVI SLEDFMEKLA PFHWPPEKRV AYCFEVAAQR SPDKKTCPMK 150
    EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YKEQWIQRFP PKEHPVLALP 200
    GAPAQFPVLE EHRELQKYMV WSDEMVRTGE AQISTHLVRP YVGIHLRIGS 250
    DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TATPLTTTMC LPDLKEIQRA 300
    VKLWVRALDA RSVYIATDSE SYVSEIQQLF KEKVKVVSLK PEVAQIDLYI 350
    LGQADHFIGN CVSSFTAFVK RERDLHGRPS SFFGMDRPSQ LRDEF 395
    Length:395
    Mass (Da):44,983
    Last modified:August 16, 2004 - v1
    Checksum:i2A85521E22F38920
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ781499 mRNA. Translation: CAH03711.1.
    RefSeqiNP_001002278.1. NM_001002278.1.
    XP_006235352.1. XM_006235290.1.
    UniGeneiRn.214685.

    Genome annotation databases

    EnsembliENSRNOT00000013730; ENSRNOP00000013730; ENSRNOG00000010104.
    GeneIDi311551.
    KEGGirno:311551.
    UCSCiRGD:1303001. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ781499 mRNA. Translation: CAH03711.1 .
    RefSeqi NP_001002278.1. NM_001002278.1.
    XP_006235352.1. XM_006235290.1.
    UniGenei Rn.214685.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000013730.

    Protein family/group databases

    CAZyi GT65. Glycosyltransferase Family 65.

    Proteomic databases

    PaxDbi Q6EV70.
    PRIDEi Q6EV70.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000013730 ; ENSRNOP00000013730 ; ENSRNOG00000010104 .
    GeneIDi 311551.
    KEGGi rno:311551.
    UCSCi RGD:1303001. rat.

    Organism-specific databases

    CTDi 23509.
    RGDi 1303001. Pofut1.

    Phylogenomic databases

    eggNOGi NOG250895.
    GeneTreei ENSGT00390000015634.
    HOGENOMi HOG000231651.
    HOVERGENi HBG059976.
    InParanoidi Q6EV70.
    KOi K03691.
    OMAi SEHPVLA.
    OrthoDBi EOG7ZD1VC.
    PhylomeDBi Q6EV70.
    TreeFami TF314805.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_198791. Pre-NOTCH Processing in the Endoplasmic Reticulum.

    Miscellaneous databases

    NextBioi 663802.
    PROi Q6EV70.

    Gene expression databases

    Genevestigatori Q6EV70.

    Family and domain databases

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

    Publicationsi

    1. "A new superfamily of protein-O-fucosyltransferases, alpha2-fucosyltransferases, and alpha6-fucosyltransferases: phylogeny and identification of conserved peptide motifs."
      Martinez-Duncker I., Mollicone R., Candelier J.-J., Breton C., Oriol R.
      Glycobiology 13:1C-5C(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: WistarImported.
    2. "Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains."
      Wang Y., Lee G.F., Kelley R.F., Spellman M.W.
      Glycobiology 6:837-842(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, ENZYME REGULATION, SUBSTRATE SPECIFICITY.
    3. "O-fucosylation of notch occurs in the endoplasmic reticulum."
      Luo Y., Haltiwanger R.S.
      J. Biol. Chem. 280:11289-11294(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiOFUT1_RAT
    AccessioniPrimary (citable) accession number: Q6EV70
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3