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Reviewed, UniProtKB/Swiss-Prot Q9V6X7 (OFUT1_DROME)

Last modified January 19, 2010. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    GDP-fucose protein O-fucosyltransferase 1
    EC=2.4.1.221
Alternative name(s):
    Peptide-O-fucosyltransferase 1
      Short name=O-FucT-1
    Neurotic protein
Gene names
Name: O-fut1
Synonyms: nti
ORF Names: CG12366
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

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 in EGF domains. Plays a crucial role in Notch signaling; essential for the interaction of Notch with its ligand Delta, and for the ability of Fringe to modulate this interaction. 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.

Developmental stage

Expressed both maternally and zygotically. Ref.1

Sequence similarities

Belongs to the glycosyltransferase 68 family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Amino acid modifications

Glycosylation601N-linked (GlcNAc...) Potential

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
Q9V6X7-1 [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: 12917292] [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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[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: 12537569] [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: 11524432] [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: 11698403] [Abstract]
Cited for: HOMOLOGY.
+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.
UniGeneDm.30916

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP-20580N.
IntActQ9V6X7. 4 interactions.
STRINGQ9V6X7.

Protein family/group databases

CAZyGT65. Glycosyltransferase Family 65.

Proteomic databases

PRIDEQ9V6X7.

Genome annotation databases

EnsemblFBtr0087520; FBpp0086649; FBgn0033901; Drosophila melanogaster. [Genome view]
GeneID36564.
KEGGdme:Dmel_CG12366.
NMPDRfig|7227.3.peg.5171.

Organism-specific databases

CTD36564.
FlyBaseFBgn0033901. O-fut1.

Phylogenomic databases

eggNOGinNOG07511.
InParanoidQ9V6X7.
OMAQSVYIAT.
OrthoDBEOG9B8JMK.
PhylomeDBQ9V6X7.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-004551-MONOMER.
BRENDA2.4.1.221. 48.

Gene expression databases

GermOnlineCG12366. Drosophila melanogaster.

Family and domain databases

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

Other Resources

NextBio799227.

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: January 19, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents