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Q9W589 (OFUT2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. 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):
Peptide-O-fucosyltransferase 2
Short name=O-FucT-2
Gene names
Name:O-fut2
ORF Names:CG14789
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length490 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 1 repeats where C1 and C2 are the first and second cysteines, respectively. O-fucosylates members of a number of protein families including the ADAMTS family, the thrombosporin (TSP) and spondin families. Ref.5

Catalytic activity

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

Enzyme regulation

Does not require divalent metal ions for optimal activity. Ref.5

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum. Golgi apparatus. Note: Mainly located in the endoplasmic reticulum. Ref.5

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence caution

The sequence CAB53644.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 490465GDP-fucose protein O-fucosyltransferase 2
PRO_0000236806

Sites

Site4431Essential for catalytic activity By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation3681N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis4421E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-443. Ref.5
Mutagenesis4431E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-442. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9W589 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 54038E7CDD020768

FASTA49056,021
        10         20         30         40         50         60 
MRGSWPRLGF PALLLLLHLL TGSDAAVRNG TAKREIGDSR GSSGTCVKGF LQEILPLPAT 

        70         80         90        100        110        120 
CPPEVLGMRG AVYILYDVNI SEGFNLRRDV YIRMAVFVRR LQRRRRFRHV RLVLPPWPRL 

       130        140        150        160        170        180 
YHWHSQGLQQ SGLPWSHFFD LASLRRYAPV LDYEEFLAEQ RLFGNPGAPL VHVGHAFRLQ 

       190        200        210        220        230        240 
HYEVMLEQGI FRDKFERVTD KPCSEGSLSG GPLLQQAELR VGRFHCVRFQ GSAGLLEKLL 

       250        260        270        280        290        300 
REAIDEDTAG PEDVDDMRTY ALLSAETVLH DHWGDEHFWQ ARRSMRFARR LEQVAADFRR 

       310        320        330        340        350        360 
QALDTTDASA GVQRPAMWEL ERPKRNAKGG DYLCAHLRRG DFVRSRDATT PTLKAAAQQV 

       370        380        390        400        410        420 
KQLLRGFNMT TVFLATDATP YELMELKELF YRFRLVHFAP ESNVQRRELK DGGVAVVDQL 

       430        440        450        460        470        480 
VCAYARYFVG TYESTFTYRI YEEREILGFT QASTFNTFCK ALGGSCSRNA VWPIVWADGD 

       490 
SDSEEDSDPY 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"From sequence to chromosome: the tip of the X chromosome of D. melanogaster."
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D., Minana B. expand/collapse author list , Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S., McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C., Glover D.M.
Science 287:2220-2222(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Oregon-R.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]"Protein O-fucosyltransferase 2 adds O-fucose to thrombospondin type 1 repeats."
Luo Y., Koles K., Vorndam W., Haltiwanger R.S., Panin V.M.
J. Biol. Chem. 281:9393-9399(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-442 AND GLU-443.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014298 Genomic DNA. Translation: AAF45629.1.
AL031027 Genomic DNA. No translation available.
AL035632 Genomic DNA. Translation: CAB53644.1. Sequence problems.
AY047568 mRNA. Translation: AAK77300.1.
RefSeqNP_569916.1. NM_130560.3.
UniGeneDm.4643.

3D structure databases

ProteinModelPortalQ9W589.
SMRQ9W589. Positions 73-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid57655. 1 interaction.

Protein family/group databases

CAZyGT68. Glycosyltransferase Family 68.

Proteomic databases

PaxDbQ9W589.
PRIDEQ9W589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0070296; FBpp0070283; FBgn0027791.
GeneID31098.
KEGGdme:Dmel_CG14789.

Organism-specific databases

CTD31098.
FlyBaseFBgn0027791. O-fut2.

Phylogenomic databases

eggNOGNOG77810.
GeneTreeENSGT00390000007989.
InParanoidQ9W589.
KOK03691.
OMAICAHARF.
OrthoDBEOG76T9S1.
PhylomeDBQ9W589.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ9W589.

Family and domain databases

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

Other

GenomeRNAi31098.
NextBio771923.
PROQ9W589.

Entry information

Entry nameOFUT2_DROME
AccessionPrimary (citable) accession number: Q9W589
Secondary accession number(s): Q7K729, Q9U985
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase