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Reviewed, UniProtKB/Swiss-Prot P83337 (OFUT1_CRIGR)

Last modified June 16, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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 names
Name: POFUT1
OrganismCricetulus griseus (Chinese hamster)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length61 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in EGF domains. Plays a crucial role in Notch signaling. Ref.2 Ref.3 Ref.4

Catalytic activity

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor. Ref.2 Ref.3 Ref.4

Cofactor

Manganese. Other divalent cations increase activity: calcium, cobalt, cadmium, magnesium and nickel. Ref.3 Ref.4

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity.

Post-translational modification

N-glycosylated. Ref.4

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›61›61GDP-fucose protein O-fucosyltransferase 1
PRO_0000220935

Experimental info

Non-terminal residue611

Sequences

Sequence LengthMass (Da)Tools
P83337-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E9507AE60018F23A

FASTA616,955
        10         20         30         40         50         60 
RLAGSWDLAG YLLYXPXMGR FGNQADHFLG SLAFAKLXVR TLAVPPWIEY QHHKPPFTNL 


H 

« Hide

References

[1]"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: 11524432] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"O-linked fucose and other post-translational modifications unique to EGF modules."
Harris R.J., Spellman M.W.
Glycobiology 3:219-224(1993) [PubMed: 8358148] [Abstract]
Cited for: FUNCTION.
[3]"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: 9023546] [Abstract]
Cited for: FUNCTION.
[4]"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: 9525914] [Abstract]
Cited for: FUNCTION, GLYCOSYLATION.
Tissue: Ovary.

Cross-references

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP83337.

Enzyme and pathway databases

BRENDA2.4.1.221. 18.

Family and domain databases

InterProIPR019378. GDP-Fuc_prot_O-FucTrfase.
[Graphical view]
PfamPF10250. O-FucT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOFUT1_CRIGR
AccessionPrimary (citable) accession number: P83337
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents