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

Q6EV56 (OFUT2_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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 2

EC=2.4.1.221
Alternative name(s):
Peptide-O-fucosyltransferase 2
Short name=O-FucT-2
Gene names
Name:POFUT2
Synonyms:FUT13
OrganismPan troglodytes (Chimpanzee) [Reference proteome]
Taxonomic identifier9598 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePan

Protein attributes

Sequence length429 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 in the consensus sequence C1-X(2,3)-S/T-C2-X(2)-G of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombosporin (TSP) and spondin families. Required for the proper secretion of ADAMTS family members such as ADAMSL1 and ADAMST13. O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm By similarity.

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum By similarity. Golgi apparatus By similarity. Note: Mainly located in the endoplasmic reticulum By similarity.

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 429408GDP-fucose protein O-fucosyltransferase 2
PRO_0000012156

Regions

Region53 – 564Substrate binding By similarity
Region388 – 3892Substrate binding By similarity

Sites

Active site541Proton donor/acceptor By similarity
Binding site2941Substrate By similarity
Site3961Essential for catalytic activity By similarity

Amino acid modifications

Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Disulfide bond161 ↔ 192 By similarity
Disulfide bond412 ↔ 419 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6EV56 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 77A3635BD4698983

FASTA42949,847
        10         20         30         40         50         60 
MATLSFVFLL LGAVSWPPAS ASGQEFWPGQ SAADILSGAA SRRRYLLYDV NPPEGFNLRR 

        70         80         90        100        110        120 
DVYIRIASLL KTLLKTEEWV LVLPPWGRLY HWQSPDIHQV RIPWSEFFDL PSLNKNIPVI 

       130        140        150        160        170        180 
EYEQFIAESG GPFIDQVYVL QSYAEGWKEG TWEEKVDERP CIDQLLYSQD KHEYYRGWFW 

       190        200        210        220        230        240 
GYEETRGLNV SCLSVQGSAS IVAPLLLRNT SARSVMLDRA ENLLHDHYGG KEYWDTRRSM 

       250        260        270        280        290        300 
VFARHLREVG DEFRSRHLNS TDDADGIPFQ EDWTKMKVKL GSALGGPYLG VHLRRKDFIW 

       310        320        330        340        350        360 
GHRQDVPSLE GAVRKIRSLM KTHRLDKVFV ATDAVRKEYE ELKKLLPEMV RFEPTWEELE 

       370        380        390        400        410        420 
LYKDGGVAII DQWICAHARF FIGTSVSTFS FRIHEEREIL GLDPKTTYNR FCGDQEKACE 


QPTHWKITY 

« 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
AJ781756 mRNA. Translation: CAH03731.1.
RefSeqNP_001008983.1. NM_001008983.1.
UniGenePtr.6191.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9598.ENSPTRP00000024102.

Protein family/group databases

CAZyGT68. Glycosyltransferase Family 68.

Proteomic databases

PRIDEQ6EV56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPTRT00000026129; ENSPTRP00000024102; ENSPTRG00000014001.
GeneID449505.
KEGGptr:449505.

Organism-specific databases

CTD23275.

Phylogenomic databases

eggNOGNOG77810.
GeneTreeENSGT00390000007989.
HOGENOMHOG000015874.
HOVERGENHBG053367.
InParanoidQ6EV56.
KOK03691.
OMAICAHARF.
OrthoDBEOG76T9S1.
TreeFamTF314337.

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

NextBio20832633.

Entry information

Entry nameOFUT2_PANTR
AccessionPrimary (citable) accession number: Q6EV56
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 63 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