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Q9V6X7 (OFUT1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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·Interactions·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):
Neurotic protein
Peptide-O-fucosyltransferase 1
Short name=O-FucT-1
Gene names
Name:O-fut1
Synonyms:nti
ORF Names:CG12366
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length402 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 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/N by POFUT1 generates a substrate for Fringe/Fng, 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 Delta/Dl or Serrate/Ser. Also required for the transport of Notch/N to the early endosome. Ref.1 Ref.8 Ref.9

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.

Subunit structure

Interacts with N (via its EGF domains); the interaction is required for the endocyctic transport of N. Ref.9

Subcellular location

Endoplasmic reticulum By similarity.

Developmental stage

Expressed both maternally and zygotically. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Sequence caution

The sequence AAM50020.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Fucose metabolism
Notch signaling pathway
   Cellular componentEndoplasmic reticulum
   DomainSignal
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Non-traceable author statement Ref.7. Source: UniProtKB

O-glycan processing

Traceable author statement Ref.7. Source: UniProtKB

embryo development

Non-traceable author statement Ref.7. Source: UniProtKB

endocytosis

Inferred from mutant phenotype Ref.9. Source: FlyBase

fucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

fucosylation

Inferred from direct assay PubMed 12526814. Source: GOC

lateral inhibition

Inferred from mutant phenotype PubMed 19363474. Source: FlyBase

negative regulation of Notch signaling pathway

Inferred from mutant phenotype Ref.9. Source: FlyBase

protein O-linked fucosylation

Traceable author statement Ref.7. Source: GOC

protein O-linked glycosylation

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

protein catabolic process

Inferred from mutant phenotype Ref.9. Source: FlyBase

regulation of Notch signaling pathway

Inferred from mutant phenotype Ref.1. Source: FlyBase

regulation of transcription, DNA-templated

Non-traceable author statement Ref.7. Source: UniProtKB

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 15611340. Source: FlyBase

   Cellular_componentcytoplasm

Inferred by curator Ref.7. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay Ref.9. Source: FlyBase

endoplasmic reticulum

Inferred from direct assay PubMed 15692013. Source: FlyBase

   Molecular_functionNotch binding

Inferred from direct assay Ref.9. Source: FlyBase

fucosyltransferase activity

Inferred from sequence or structural similarity Ref.6. Source: UniProtKB

peptide-O-fucosyltransferase activity

Traceable author statement Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG9784Q9VXE71EBI-97485,EBI-165741
SyndQ9VDI11EBI-97485,EBI-106353

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 402379GDP-fucose protein O-fucosyltransferase 1
PRO_0000012153

Regions

Region42 – 443Substrate binding By similarity
Region243 – 2453Substrate binding By similarity
Region365 – 3662Substrate binding By similarity

Sites

Binding site3441Substrate By similarity

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 38 By similarity
Disulfide bond122 ↔ 141 By similarity
Disulfide bond254 ↔ 284 By similarity
Disulfide bond269 ↔ 363 By similarity

Experimental info

Sequence conflict3711E → V in AAM50020. Ref.5
Sequence conflict3891K → E in BAC55010. Ref.1
Sequence conflict3891K → E in AAX33443. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9V6X7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E52FF4F86509C2E6

FASTA40246,834
        10         20         30         40         50         60 
MQWLKMKLRF VNLILLLISS TCAQLGGDPN GYLTYCPCMG RFGNQADHFL GSLAFAKALN 

        70         80         90        100        110        120 
RTLILPPWVE YRRGELRSRQ VPFNTYFEVE PLKEYHRVIT MADFMWHLAD DIWPESERVS 

       130        140        150        160        170        180 
FCYKERYSLQ QEKNDPDKPN CHAKDGNPFG PFWDTFHIDF VRSEFYAPLH FDVHHSNEAA 

       190        200        210        220        230        240 
KWQTKYPAES YPVLAFTGAP ASFPVQLENC KLQRYLQWSQ RYREASKDFI REQLPRGAFL 

       250        260        270        280        290        300 
GIHLRNGIDW VRACEHVKDS QHLFASPQCL GYKNERGALY PELCMPSKEA IIRQLKRTIK 

       310        320        330        340        350        360 
NVRQTQPDNE IKSVFVASDS NHMIGELNTA LSRMGISVHK LPEDDPYLDL AILGQSNHFI 

       370        380        390        400 
GNCISSYSAF EKRERDVHGF PSYFWGFPKE KDRKHTNVHE EL 

« Hide

References

« Hide 'large scale' references
[1]"Neurotic, a novel maternal neurogenic gene, encodes an O-fucosyltransferase that is essential for Notch-Delta interactions."
Sasamura T., Sasaki N., Miyashita F., Nakao S., Ishikawa H., Ito M., Kitagawa M., Harigaya K., Spana E., Bilder D., Perrmon N., Matsuno K.
Development 130:4785-4795(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
[2]"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.
[3]"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.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"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] OF 11-402.
Strain: Berkeley.
Tissue: Embryo.
[6]"Modification of epidermal growth factor-like repeats with O-fucose: molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase."
Wang Y., Shao L., Shi S., Harris R.J., Spellman M.W., Stanley P., Haltiwanger R.S.
J. Biol. Chem. 276:40338-40345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOLOGY.
[7]"Composition of Drosophila melanogaster proteome involved in fucosylated glycan metabolism."
Roos C., Kolmer M., Mattila P., Renkonen R.
J. Biol. Chem. 277:3168-3175(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOLOGY.
[8]"Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe."
Okajima T., Xu A., Irvine K.D.
J. Biol. Chem. 278:42340-42345(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila."
Sasamura T., Ishikawa H.O., Sasaki N., Higashi S., Kanai M., Nakao S., Ayukawa T., Aigaki T., Noda K., Miyoshi E., Taniguchi N., Matsuno K.
Development 134:1347-1356(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH N.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB093572 mRNA. Translation: BAC55010.1.
AE013599 Genomic DNA. Translation: AAF58290.1.
BT021295 mRNA. Translation: AAX33443.1.
AY118651 mRNA. Translation: AAM50020.1. Different initiation.
RefSeqNP_610931.1. NM_137087.2.
UniGeneDm.30916.

3D structure databases

ProteinModelPortalQ9V6X7.
SMRQ9V6X7. Positions 28-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62315. 4 interactions.
DIPDIP-20580N.
IntActQ9V6X7. 3 interactions.
MINTMINT-304675.
STRING7227.FBpp0086649.

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

Proteomic databases

PaxDbQ9V6X7.
PRIDEQ9V6X7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0087520; FBpp0086649; FBgn0033901.
GeneID36564.
KEGGdme:Dmel_CG12366.

Organism-specific databases

CTD36564.
FlyBaseFBgn0033901. O-fut1.

Phylogenomic databases

eggNOGNOG250895.
GeneTreeENSGT00390000015634.
InParanoidQ9V6X7.
KOK03691.
OMASEHPVLA.
OrthoDBEOG7ZD1VC.
PhylomeDBQ9V6X7.

Enzyme and pathway databases

SignaLinkQ9V6X7.
UniPathwayUPA00378.

Gene expression databases

BgeeQ9V6X7.

Family and domain databases

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

Other

GenomeRNAi36564.
NextBio799227.
PROQ9V6X7.

Entry information

Entry nameOFUT1_DROME
AccessionPrimary (citable) accession number: Q9V6X7
Secondary accession number(s): Q5BIC9, Q86SA7, Q8MSR1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 99 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