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Q6EV69

- OFUT1_PANTR

UniProt

Q6EV69 - OFUT1_PANTR

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

POFUT1

Organism
Pan troglodytes (Chimpanzee)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 65 (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. 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. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Manganese.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei335 – 3351SubstrateBy 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

    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:POFUT1
    Synonyms:FUT12
    OrganismiPan troglodytes (Chimpanzee)
    Taxonomic identifieri9598 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan
    ProteomesiUP000002277: Chromosome 20

    Subcellular locationi

    Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 388362GDP-fucose protein O-fucosyltransferase 1PRO_0000012150Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi38 ↔ 40By similarity
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi126 ↔ 140By similarity
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi249 ↔ 283By similarity
    Disulfide bondi267 ↔ 354By similarity

    Post-translational modificationi

    N-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ6EV69.

    Interactioni

    Protein-protein interaction databases

    STRINGi9598.ENSPTRP00000022931.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6EV69.
    SMRiQ6EV69. Positions 30-378.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 463Substrate bindingBy similarity
    Regioni238 – 2403Substrate bindingBy similarity
    Regioni356 – 3572Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi385 – 3884Prevents secretion from ERSequence Analysis

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG250895.
    GeneTreeiENSGT00390000015634.
    HOGENOMiHOG000231651.
    HOVERGENiHBG059976.
    InParanoidiQ6EV69.
    KOiK03691.
    OMAiSEHPVLA.
    OrthoDBiEOG7ZD1VC.
    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.

    Q6EV69-1 [UniParc]FASTAAdd to Basket

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    MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH    50
    FLGSLAFAKL LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH 100
    RVISLEDFME KLAPTHWPPE KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP 150
    FWDQFHVSFN KSELFTGISF SASYREQWSQ RFSPKEHPVL ALPGAPAQFP 200
    VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR IGSDWKNACA 250
    MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS 300
    LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF 350
    IGNCVSSFTA FVKRERDLQG RPSSFFGMDR PPKLRDEF 388
    Length:388
    Mass (Da):43,956
    Last modified:August 16, 2004 - v1
    Checksum:i3FACCCA434D02415
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ781500 mRNA. Translation: CAH03712.1.
    RefSeqiNP_001008982.1. NM_001008982.1.
    UniGeneiPtr.6249.

    Genome annotation databases

    EnsembliENSPTRT00000024842; ENSPTRP00000022931; ENSPTRG00000013375.
    GeneIDi449504.
    KEGGiptr:449504.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ781500 mRNA. Translation: CAH03712.1 .
    RefSeqi NP_001008982.1. NM_001008982.1.
    UniGenei Ptr.6249.

    3D structure databases

    ProteinModelPortali Q6EV69.
    SMRi Q6EV69. Positions 30-378.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9598.ENSPTRP00000022931.

    Protein family/group databases

    CAZyi GT65. Glycosyltransferase Family 65.

    Proteomic databases

    PRIDEi Q6EV69.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSPTRT00000024842 ; ENSPTRP00000022931 ; ENSPTRG00000013375 .
    GeneIDi 449504.
    KEGGi ptr:449504.

    Organism-specific databases

    CTDi 23509.

    Phylogenomic databases

    eggNOGi NOG250895.
    GeneTreei ENSGT00390000015634.
    HOGENOMi HOG000231651.
    HOVERGENi HBG059976.
    InParanoidi Q6EV69.
    KOi K03691.
    OMAi SEHPVLA.
    OrthoDBi EOG7ZD1VC.
    TreeFami TF314805.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 20832632.

    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].

    Entry informationi

    Entry nameiOFUT1_PANTR
    AccessioniPrimary (citable) accession number: Q6EV69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 65 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