Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q18014 (OFUT1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
ORF Names:C15C7.7
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length389 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Ref.3 UniProtKB Q9H488

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subunit structure

Monomer. Ref.3

Subcellular location

Endoplasmic reticulum By similarity.

Miscellaneous

Manganese is bound to the substrate GDP-fucose, but is not required for enzyme activity.

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 389368GDP-fucose protein O-fucosyltransferase 1
PRO_0000012152

Regions

Region41 – 433Substrate binding
Region238 – 2403Substrate binding
Region355 – 3562Substrate binding

Sites

Binding site3341Substrate

Amino acid modifications

Glycosylation241N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 37 Ref.3
Disulfide bond119 ↔ 135 Ref.3
Disulfide bond249 ↔ 281 Ref.3
Disulfide bond266 ↔ 353 Ref.3

Experimental info

Mutagenesis431N → A: Reduces enzyme activity by over 90%. Ref.3
Mutagenesis2401R → A or K: Abolishes enzyme activity. Ref.3

Secondary structure

......................................................................... 389
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q18014 [UniParc].

Last modified February 1, 2005. Version 5.
Checksum: 0C84F202AA184554

FASTA38944,051
        10         20         30         40         50         60 
MRVSKVLTLA SFISVCSYSE AKSNETDPNG YIVFCPCMGR FGNQVDQFLG VLAFAKALDR 

        70         80         90        100        110        120 
TLVLPNFIEF KHPETKMIPF EFLFQVGTVA KYTRVVTMQE FTKKIMPTVW PPEKRKAFCW 

       130        140        150        160        170        180 
TPRQAIYDKS AEPGCHSKEG NPFGPYWDQI DVSFVGDEYF GDIPGGFDLN QMGSRKKWLE 

       190        200        210        220        230        240 
KFPSEEYPVL AFSSAPAPFP SKGKVWSIQK YLRWSSRITE QAKKFISANL AKPFVAVHLR 

       250        260        270        280        290        300 
NDADWVRVCE HIDTTTNRPL FASEQCLGEG HHLGTLTKEI CSPSKQQILE QIVEKVGSIG 

       310        320        330        340        350        360 
AKSVFVASDK DHMIDEINEA LKPYEIEAHR QEPDDMYTSL AIMGRADLFV GNCVSTFSHI 

       370        380 
VKRERDHAGQ SPRPSAFFGI RAVKRHIDL 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[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: HOMOLOGY.
[3]"Structural insights into the mechanism of protein O-fucosylation."
Lira-Navarrete E., Valero-Gonzalez J., Villanueva R., Martinez-Julvez M., Tejero T., Merino P., Panjikar S., Hurtado-Guerrero R.
PLoS ONE 6:E25365-E25365(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 26-383 IN COMPLEX WITH GDP-FUCOSE AND MANGANESE, ABSENCE OF COFACTOR REQUIREMENT, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF ASN-43 AND ARG-240.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080550 Genomic DNA. Translation: CCD64591.1.
RefSeqNP_741744.2. NM_171649.6.
UniGeneCel.30602.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZY2X-ray1.54A26-383[»]
3ZY3X-ray1.86A/B26-383[»]
3ZY4X-ray1.74A26-383[»]
3ZY5X-ray1.96A26-383[»]
3ZY6X-ray1.91A26-383[»]
ProteinModelPortalQ18014.
SMRQ18014. Positions 26-381.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

Proteomic databases

PaxDbQ18014.
PRIDEQ18014.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC15C7.7; C15C7.7; C15C7.7.
GeneID180607.
KEGGcel:CELE_C15C7.7.
UCSCC15C7.7. c. elegans.

Organism-specific databases

CTD180607.
WormBaseC15C7.7; CE36786; WBGene00015793.

Phylogenomic databases

eggNOGNOG250895.
GeneTreeENSGT00390000015634.
HOGENOMHOG000231651.
InParanoidQ18014.
KOK03691.
OMAPHFMASP.
OrthoDBEOG7ZD1VC.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

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

Other

EvolutionaryTraceQ18014.
NextBio910082.
PROQ18014.

Entry information

Entry nameOFUT1_CAEEL
AccessionPrimary (citable) accession number: Q18014
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: February 1, 2005
Last modified: November 13, 2013
This is version 87 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase