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

Q6EV69 (OFUT1_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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
Synonyms:FUT12
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 DLL1 or JAGGED1. Fucosylates AGRN and determines its ability to cluster acetylcholine receptors (AChRs) By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 388362GDP-fucose protein O-fucosyltransferase 1
PRO_0000012150

Regions

Region44 – 463Substrate binding By similarity
Region238 – 2403Substrate binding By similarity
Region356 – 3572Substrate binding By similarity
Motif385 – 3884Prevents secretion from ER Potential

Sites

Binding site3351Substrate By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation1601N-linked (GlcNAc...) Potential
Disulfide bond38 ↔ 40 By similarity
Disulfide bond126 ↔ 140 By similarity
Disulfide bond249 ↔ 283 By similarity
Disulfide bond267 ↔ 354 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6EV69 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 3FACCCA434D02415

FASTA38843,956
        10         20         30         40         50         60 
MGAAAWARPL SVSFLLLLLP LPGMPAGSWD PAGYLLYCPC MGRFGNQADH FLGSLAFAKL 

        70         80         90        100        110        120 
LNRTLAVPPW IEYQHHKPPF TNLHVSYQKY FKLEPLQAYH RVISLEDFME KLAPTHWPPE 

       130        140        150        160        170        180 
KRVAYCFEVA AQRSPDKKTC PMKEGNPFGP FWDQFHVSFN KSELFTGISF SASYREQWSQ 

       190        200        210        220        230        240 
RFSPKEHPVL ALPGAPAQFP VLEEHRPLQK YMVWSDEMVK TGEAQIHAHL VRPYVGIHLR 

       250        260        270        280        290        300 
IGSDWKNACA MLKDGTAGSH FMASPQCVGY SRSTAAPLTM TMCLPDLKEI QRAVKLWVRS 

       310        320        330        340        350        360 
LDAQSVYVAT DSESYVPELQ QLFKGKVKVV SLKPEVAQVD LYILGQADHF IGNCVSSFTA 

       370        380 
FVKRERDLQG RPSSFFGMDR PPKLRDEF 

« Hide

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ781500 mRNA. Translation: CAH03712.1.
RefSeqNP_001008982.1. NM_001008982.1.
UniGenePtr.6249.

3D structure databases

ProteinModelPortalQ6EV69.
SMRQ6EV69. Positions 30-378.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000022931.

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

Proteomic databases

PRIDEQ6EV69.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000024842; ENSPTRP00000022931; ENSPTRG00000013375.
GeneID449504.
KEGGptr:449504.

Organism-specific databases

CTD23509.

Phylogenomic databases

eggNOGNOG250895.
GeneTreeENSGT00390000015634.
HOGENOMHOG000231651.
HOVERGENHBG059976.
InParanoidQ6EV69.
KOK03691.
OMASEHPVLA.
OrthoDBEOG7ZD1VC.
TreeFamTF314805.

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

NextBio20832632.

Entry information

Entry nameOFUT1_PANTR
AccessionPrimary (citable) accession number: Q6EV69
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: August 16, 2004
Last modified: May 14, 2014
This is version 64 of the entry and version 1 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