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Q8WR51 (OFUT2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Patterning defective protein 2
Peptide-O-fucosyltransferase 2
Short name=O-FucT-2
Gene names
Name:pad-2
ORF Names:K10G9.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length424 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 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 By similarity. Ref.1

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. Note: Mainly located in the endoplasmic reticulum. Ref.1

Tissue specificity

Expressed in the anterior part of embryos, in the hypodermal and neuronal cells of the head. Expressed at different levels in a variety of cell types after hatching, including neuronal, hypodermal, muscle, intestinal, and somatic gonadal cells. Expressed in the nerve ring around the pharynx, in dorsal and ventral nerve cords, intestine, and a variety of hypodermal cells of L1-L3 larvae. Expressed in gonadal sheath cells, spermatheca, and tissues surrounding the vulva of adult hermaphrodites, and in the body wall muscle and hypodermal cells of adults of both sexes. Ref.1

Developmental stage

Expressed starts at morphogenetic embryonic stages and continues throughout development. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 424404GDP-fucose protein O-fucosyltransferase 2
PRO_0000012157

Regions

Region51 – 544Substrate binding By similarity
Region383 – 3842Substrate binding By similarity

Sites

Active site521Proton donor/acceptor By similarity
Binding site2901Substrate By similarity
Site3911Essential for catalytic activity By similarity

Amino acid modifications

Glycosylation2051N-linked (GlcNAc...) Ref.3
Disulfide bond154 ↔ 187 By similarity
Disulfide bond407 ↔ 414 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8WR51 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 2A35F5FC04EF70B3

FASTA42450,106
        10         20         30         40         50         60 
MHFFPIQLLV LFFAEKIAFA ENSDQTVSRV DSNRYSVAAE KKFLLYDVNF GEGFNLRRDV 

        70         80         90        100        110        120 
YMRVANTVRS LRDSGENYIL VLPPWGRLHH WKRMEVALSW RLFFDLESLN RFIPVIEFED 

       130        140        150        160        170        180 
FLDENRPIDQ VIYLQHYAEG WGTEYVRKFE KRSCLPPAES HYKQVEEFKW KGWFYSYEDV 

       190        200        210        220        230        240 
YSRNFQCVSI QGDSGTLKDL LKHSNFSEST SIMVDRAETI LHEHYGEVDY WKARRSMRYS 

       250        260        270        280        290        300 
NDLVDVADAF RKKYLDSDDK RDKTKLVDDW TKEKPRRTAI GGPYLGIHWR RRDFLYARRA 

       310        320        330        340        350        360 
QLPTIPGTAK ILQDLCKKLD LQKIYLATDA PDQEVDELKA LLNGELEVYR FTDTQKLNDG 

       370        380        390        400        410        420 
QIAIIDQYLC AHAAYFIGSY ESTFTFRIQE DREIIGFPIS TTFNRLCPDT EPTCEQPAKW 


KIVY 

« Hide

References

« Hide 'large scale' references
[1]"The Caenorhabditis elegans ortholog of C21orf80, a potential new protein O-fucosyltransferase, is required for normal development."
Menzel O., Vellai T., Takacs-Vellai K., Reymond A., Mueller F., Antonarakis S.E., Guipponi M.
Genomics 84:320-330(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]"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.
[3]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-205, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF455271 mRNA. Translation: AAL65193.1.
Z36282 Genomic DNA. Translation: CAD45602.1.
RefSeqNP_001255070.1. NM_001268141.1.
UniGeneCel.9168.

3D structure databases

ProteinModelPortalQ8WR51.
SMRQ8WR51. Positions 39-424.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.K10G9.3.

Protein family/group databases

CAZyGT68. Glycosyltransferase Family 68.

Proteomic databases

PaxDbQ8WR51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaK10G9.3a; K10G9.3a; WBGene00010757.
GeneID259529.
KEGGcel:CELE_K10G9.3.
UCSCK10G9.3. c. elegans.

Organism-specific databases

CTD259529.
WormBaseK10G9.3a; CE31715; WBGene00010757; pad-2.

Phylogenomic databases

eggNOGNOG77810.
GeneTreeENSGT00390000007989.
HOGENOMHOG000015874.
InParanoidQ8WR51.
KOK03691.
PhylomeDBQ8WR51.

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

NextBio952052.
PROQ8WR51.

Entry information

Entry nameOFUT2_CAEEL
AccessionPrimary (citable) accession number: Q8WR51
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

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