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Q9W589

- OFUT2_DROME

UniProt

Q9W589 - OFUT2_DROME

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Protein
GDP-fucose protein O-fucosyltransferase 2
Gene
O-fut2, CG14789
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Does not require divalent metal ions for optimal activity.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei443 – 4431Essential for catalytic activity By similarity

GO - Molecular functioni

  1. peptide-O-fucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. O-glycan processing Source: UniProtKB
  2. embryo development Source: UniProtKB
  3. fucose metabolic process Source: UniProtKB-KW
  4. protein O-linked fucosylation Source: GOC
  5. regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism

Enzyme and pathway databases

ReactomeiREACT_218181. O-glycosylation of TSR domain-containing proteins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT68. Glycosyltransferase Family 68.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:O-fut2
ORF Names:CG14789
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0027791. O-fut2.

Subcellular locationi

Endoplasmic reticulum. Golgi apparatus
Note: Mainly located in the endoplasmic reticulum.1 Publication

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi442 – 4421E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-443. 1 Publication
Mutagenesisi443 – 4431E → A: Abolishes enzyme activity but no effect on protein folding nor secretion; when associated with A-442. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed prediction
Add
BLAST
Chaini26 – 490465GDP-fucose protein O-fucosyltransferase 2
PRO_0000236806Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...) Reviewed prediction
Glycosylationi79 – 791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi368 – 3681N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9W589.
PRIDEiQ9W589.

Expressioni

Gene expression databases

BgeeiQ9W589.

Interactioni

Protein-protein interaction databases

BioGridi57655. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9W589.
SMRiQ9W589. Positions 73-476.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG77810.
GeneTreeiENSGT00390000007989.
InParanoidiQ9W589.
KOiK03691.
OMAiICAHARF.
OrthoDBiEOG76T9S1.
PhylomeDBiQ9W589.

Family and domain databases

InterProiIPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view]
PfamiPF10250. O-FucT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9W589-1 [UniParc]FASTAAdd to Basket

« Hide

MRGSWPRLGF PALLLLLHLL TGSDAAVRNG TAKREIGDSR GSSGTCVKGF    50
LQEILPLPAT CPPEVLGMRG AVYILYDVNI SEGFNLRRDV YIRMAVFVRR 100
LQRRRRFRHV RLVLPPWPRL YHWHSQGLQQ SGLPWSHFFD LASLRRYAPV 150
LDYEEFLAEQ RLFGNPGAPL VHVGHAFRLQ HYEVMLEQGI FRDKFERVTD 200
KPCSEGSLSG GPLLQQAELR VGRFHCVRFQ GSAGLLEKLL REAIDEDTAG 250
PEDVDDMRTY ALLSAETVLH DHWGDEHFWQ ARRSMRFARR LEQVAADFRR 300
QALDTTDASA GVQRPAMWEL ERPKRNAKGG DYLCAHLRRG DFVRSRDATT 350
PTLKAAAQQV KQLLRGFNMT TVFLATDATP YELMELKELF YRFRLVHFAP 400
ESNVQRRELK DGGVAVVDQL VCAYARYFVG TYESTFTYRI YEEREILGFT 450
QASTFNTFCK ALGGSCSRNA VWPIVWADGD SDSEEDSDPY 490
Length:490
Mass (Da):56,021
Last modified:May 1, 2000 - v1
Checksum:i54038E7CDD020768
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_569916.1. NM_130560.3.
UniGeneiDm.4643.

Genome annotation databases

EnsemblMetazoaiFBtr0070296; FBpp0070283; FBgn0027791.
GeneIDi31098.
KEGGidme:Dmel_CG14789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
RefSeqi NP_569916.1. NM_130560.3.
UniGenei Dm.4643.

3D structure databases

ProteinModelPortali Q9W589.
SMRi Q9W589. Positions 73-476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 57655. 1 interaction.

Protein family/group databases

CAZyi GT68. Glycosyltransferase Family 68.

Proteomic databases

PaxDbi Q9W589.
PRIDEi Q9W589.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0070296 ; FBpp0070283 ; FBgn0027791 .
GeneIDi 31098.
KEGGi dme:Dmel_CG14789.

Organism-specific databases

CTDi 31098.
FlyBasei FBgn0027791. O-fut2.

Phylogenomic databases

eggNOGi NOG77810.
GeneTreei ENSGT00390000007989.
InParanoidi Q9W589.
KOi K03691.
OMAi ICAHARF.
OrthoDBi EOG76T9S1.
PhylomeDBi Q9W589.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_218181. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GenomeRNAii 31098.
NextBioi 771923.
PROi Q9W589.

Gene expression databases

Bgeei Q9W589.

Family and domain databases

InterProi IPR019378. GDP-Fuc_O-FucTrfase.
[Graphical view ]
Pfami PF10250. O-FucT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  4. 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.

Entry informationi

Entry nameiOFUT2_DROME
AccessioniPrimary (citable) accession number: Q9W589
Secondary accession number(s): Q7K729, Q9U985
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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