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P83337 (OFUT1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) (Cricetulus barabensis griseus) [Complete proteome]
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
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 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. Ref.3 Ref.4 Ref.5

Catalytic activity

Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the serine hydroxy group of a protein acceptor. Ref.3 Ref.4 Ref.5

Enzyme regulation

Activated by manganese and, to a lesser extent, by other divalent metals such as cobalt and calcium. Inhibited by copper, ferric and zinc ions. Ref.3

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity.

Post-translational modification

N-glycosylated. Contains high mannose-type carbohydrates. Ref.5

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Biophysicochemical properties

Kinetic parameters:

KM=11 µM for His(6)-F7-EGF-1 Ref.5

KM=15 µM for F7-EGF-1

Vmax=2.5 µmol/min/mg enzyme

Vmax=2.4 µmol/min/mg enzyme

pH dependence:

Optimum pH is 5.5-8.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392GDP-fucose protein O-fucosyltransferase 1
PRO_0000220935

Regions

Region48 – 503Substrate binding By similarity
Region242 – 2443Substrate binding By similarity
Region360 – 3612Substrate binding By similarity
Motif389 – 3924Prevents secretion from ER Potential

Sites

Binding site3391Substrate By similarity

Amino acid modifications

Glycosylation661N-linked (GlcNAc...) Potential
Glycosylation1641N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 44 By similarity
Disulfide bond130 ↔ 144 By similarity
Disulfide bond253 ↔ 287 By similarity
Disulfide bond271 ↔ 358 By similarity

Experimental info

Sequence conflict661N → V AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P83337 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: 45E1421CBA0880C4

FASTA39244,669
        10         20         30         40         50         60 
MGAAAWAPPH LLLRVSLLLL LLLPLRGRLA GSWDLAGYLL YCPCMGRFGN QADHFLGSLA 

        70         80         90        100        110        120 
FAKLLNRTLA VPPWIEYQHH KPPFTNLHVS YQKYFKLEPL QAYHRVISLE EFMEKLAPIH 

       130        140        150        160        170        180 
WPPEKRVAYC FEVAAQRSPD KKTCPMKEGN PFGPFWDQFH VSFNKSELFT GISFSASYKE 

       190        200        210        220        230        240 
QWIQRFPPEE HPVLALPGAP AQFPVLEEHR ALQKYMVWSD EMVKTGEAQI STHLIRPYVG 

       250        260        270        280        290        300 
IHLRIGSDWK NACAMLKDGT AGSHFMASPQ CVGYSRSTAT PLTMTMCLPD LNEIQRAVKL 

       310        320        330        340        350        360 
WVRALNARSI YIATDSESYV PEIQQLFKEK VKVVSLKPEV AQVDLYILGQ ADHFIGNCVS 

       370        380        390 
SFTAFVKRER DLHGRQSSFF GMDRPSQPRD EF 

« Hide

References

« Hide 'large scale' references
[1]"The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line."
Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W., Fan H.C., Wang J., Gui Y., Lee K.H. expand/collapse author list , Betenbaugh M.J., Quake S.R., Famili I., Palsson B.O., Wang J.
Nat. Biotechnol. 29:735-741(2011) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
JH000311 Genomic DNA. Translation: EGW00282.1.
RefSeqXP_003502364.1. XM_003502316.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100753417.
KEGGcge:100753417.

Phylogenomic databases

KOK03691.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

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

Entry information

Entry nameOFUT1_CRIGR
AccessionPrimary (citable) accession number: P83337
Secondary accession number(s): G3HE95
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: January 9, 2013
Last modified: July 9, 2014
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways