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P83337

- OFUT1_CRIGR

UniProt

P83337 - OFUT1_CRIGR

Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

POFUT1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 44 (01 Oct 2014)
      Sequence version 2 (09 Jan 2013)
      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 DELTA1 or JAGGED1 By similarity. 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.3 Publications

    Enzyme regulationi

    Activated by manganese and, to a lesser extent, by other divalent metals such as cobalt and calcium. Inhibited by copper, ferric and zinc ions.1 Publication

    Kineticsi

    1. KM=11 µM for His(6)-F7-EGF-11 Publication
    2. KM=15 µM for F7-EGF-11 Publication

    Vmax=2.5 µmol/min/mg enzyme1 Publication

    Vmax=2.4 µmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 5.5-8.0.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei339 – 3391SubstrateBy similarity

    GO - Molecular functioni

    1. peptide-O-fucosyltransferase activity Source: UniProtKB
    2. transferase activity Source: UniProtKB
    3. transferase activity, transferring glycosyl groups Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    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
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus
    ProteomesiUP000001075: Unassembled WGS sequence

    Subcellular locationi

    Endoplasmic reticulum By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 392392GDP-fucose protein O-fucosyltransferase 1PRO_0000220935Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 44By similarity
    Glycosylationi66 – 661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi130 ↔ 144By similarity
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi253 ↔ 287By similarity
    Disulfide bondi271 ↔ 358By similarity

    Post-translational modificationi

    N-glycosylated. Contains high mannose-type carbohydrates.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni48 – 503Substrate bindingBy similarity
    Regioni242 – 2443Substrate bindingBy similarity
    Regioni360 – 3612Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi389 – 3924Prevents secretion from ERSequence Analysis

    Sequence similaritiesi

    Belongs to the glycosyltransferase 68 family.Curated

    Phylogenomic databases

    KOiK03691.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P83337-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAAAWAPPH LLLRVSLLLL LLLPLRGRLA GSWDLAGYLL YCPCMGRFGN    50
    QADHFLGSLA FAKLLNRTLA VPPWIEYQHH KPPFTNLHVS YQKYFKLEPL 100
    QAYHRVISLE EFMEKLAPIH WPPEKRVAYC FEVAAQRSPD KKTCPMKEGN 150
    PFGPFWDQFH VSFNKSELFT GISFSASYKE QWIQRFPPEE HPVLALPGAP 200
    AQFPVLEEHR ALQKYMVWSD EMVKTGEAQI STHLIRPYVG IHLRIGSDWK 250
    NACAMLKDGT AGSHFMASPQ CVGYSRSTAT PLTMTMCLPD LNEIQRAVKL 300
    WVRALNARSI YIATDSESYV PEIQQLFKEK VKVVSLKPEV AQVDLYILGQ 350
    ADHFIGNCVS SFTAFVKRER DLHGRQSSFF GMDRPSQPRD EF 392
    Length:392
    Mass (Da):44,669
    Last modified:January 9, 2013 - v2
    Checksum:i45E1421CBA0880C4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661N → V AA sequence (PubMed:11524432)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JH000311 Genomic DNA. Translation: EGW00282.1.
    RefSeqiXP_003502364.1. XM_003502316.2.

    Genome annotation databases

    GeneIDi100753417.
    KEGGicge:100753417.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JH000311 Genomic DNA. Translation: EGW00282.1 .
    RefSeqi XP_003502364.1. XM_003502316.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100753417.
    KEGGi cge:100753417.

    Organism-specific databases

    CTDi 23509.

    Phylogenomic databases

    KOi K03691.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Family and domain databases

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

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: PROTEIN SEQUENCE OF 28-88.
    3. "O-linked fucose and other post-translational modifications unique to EGF modules."
      Harris R.J., Spellman M.W.
      Glycobiology 3:219-224(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY.
    4. "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: FUNCTION.
    5. "Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells."
      Wang Y., Spellman M.W.
      J. Biol. Chem. 273:8112-8118(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES.

    Entry informationi

    Entry nameiOFUT1_CRIGR
    AccessioniPrimary (citable) accession number: P83337
    Secondary accession number(s): G3HE95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2004
    Last sequence update: January 9, 2013
    Last modified: October 1, 2014
    This is version 44 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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