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Q9V6X7

- OFUT1_DROME

UniProt

Q9V6X7 - OFUT1_DROME

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Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

O-fut1

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 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.3 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei344 – 3441SubstrateBy similarity

GO - Molecular functioni

  1. fucosyltransferase activity Source: UniProtKB
  2. Notch binding Source: FlyBase
  3. peptide-O-fucosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. embryo development Source: UniProtKB
  2. endocytosis Source: FlyBase
  3. fucose metabolic process Source: UniProtKB-KW
  4. fucosylation Source: GOC
  5. lateral inhibition Source: FlyBase
  6. negative regulation of Notch signaling pathway Source: FlyBase
  7. Notch signaling pathway Source: UniProtKB
  8. O-glycan processing Source: UniProtKB
  9. protein catabolic process Source: FlyBase
  10. protein O-linked fucosylation Source: GOC
  11. protein O-linked glycosylation Source: UniProtKB
  12. regulation of Notch signaling pathway Source: FlyBase
  13. regulation of transcription, DNA-templated Source: UniProtKB
  14. single organismal cell-cell adhesion Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Enzyme and pathway databases

ReactomeiREACT_180761. Pre-NOTCH Processing in the Endoplasmic Reticulum.
SignaLinkiQ9V6X7.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT65. Glycosyltransferase Family 65.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:O-fut1
Synonyms:nti
ORF Names:CG12366
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033901. O-fut1.

Subcellular locationi

Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic vesicle Source: FlyBase
  3. endoplasmic reticulum Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 402379GDP-fucose protein O-fucosyltransferase 1PRO_0000012153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 38By similarity
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi122 ↔ 141By similarity
Disulfide bondi254 ↔ 284By similarity
Disulfide bondi269 ↔ 363By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9V6X7.
PRIDEiQ9V6X7.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.1 Publication

Gene expression databases

BgeeiQ9V6X7.
ExpressionAtlasiQ9V6X7. differential.

Interactioni

Subunit structurei

Interacts with N (via its EGF domains); the interaction is required for the endocyctic transport of N.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CG9784Q9VXE71EBI-97485,EBI-165741
SyndQ9VDI11EBI-97485,EBI-106353

Protein-protein interaction databases

BioGridi62315. 4 interactions.
DIPiDIP-20580N.
IntActiQ9V6X7. 3 interactions.
MINTiMINT-304675.
STRINGi7227.FBpp0086649.

Structurei

3D structure databases

ProteinModelPortaliQ9V6X7.
SMRiQ9V6X7. Positions 28-386.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 443Substrate bindingBy similarity
Regioni243 – 2453Substrate bindingBy similarity
Regioni365 – 3662Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG250895.
GeneTreeiENSGT00390000015634.
InParanoidiQ9V6X7.
KOiK03691.
OMAiSEHPVLA.
OrthoDBiEOG7ZD1VC.
PhylomeDBiQ9V6X7.

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.

Q9V6X7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQWLKMKLRF VNLILLLISS TCAQLGGDPN GYLTYCPCMG RFGNQADHFL
60 70 80 90 100
GSLAFAKALN RTLILPPWVE YRRGELRSRQ VPFNTYFEVE PLKEYHRVIT
110 120 130 140 150
MADFMWHLAD DIWPESERVS FCYKERYSLQ QEKNDPDKPN CHAKDGNPFG
160 170 180 190 200
PFWDTFHIDF VRSEFYAPLH FDVHHSNEAA KWQTKYPAES YPVLAFTGAP
210 220 230 240 250
ASFPVQLENC KLQRYLQWSQ RYREASKDFI REQLPRGAFL GIHLRNGIDW
260 270 280 290 300
VRACEHVKDS QHLFASPQCL GYKNERGALY PELCMPSKEA IIRQLKRTIK
310 320 330 340 350
NVRQTQPDNE IKSVFVASDS NHMIGELNTA LSRMGISVHK LPEDDPYLDL
360 370 380 390 400
AILGQSNHFI GNCISSYSAF EKRERDVHGF PSYFWGFPKE KDRKHTNVHE

EL
Length:402
Mass (Da):46,834
Last modified:May 1, 2000 - v1
Checksum:iE52FF4F86509C2E6
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti371 – 3711E → V in AAM50020. (PubMed:12537569)Curated
Sequence conflicti389 – 3891K → E in BAC55010. (PubMed:12917292)Curated
Sequence conflicti389 – 3891K → E in AAX33443. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093572 mRNA. Translation: BAC55010.1.
AE013599 Genomic DNA. Translation: AAF58290.1.
BT021295 mRNA. Translation: AAX33443.1.
AY118651 mRNA. Translation: AAM50020.1. Different initiation.
RefSeqiNP_001286406.1. NM_001299477.1.
NP_610931.1. NM_137087.3.
UniGeneiDm.30916.

Genome annotation databases

EnsemblMetazoaiFBtr0087520; FBpp0086649; FBgn0033901.
GeneIDi36564.
KEGGidme:Dmel_CG12366.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB093572 mRNA. Translation: BAC55010.1 .
AE013599 Genomic DNA. Translation: AAF58290.1 .
BT021295 mRNA. Translation: AAX33443.1 .
AY118651 mRNA. Translation: AAM50020.1 . Different initiation.
RefSeqi NP_001286406.1. NM_001299477.1.
NP_610931.1. NM_137087.3.
UniGenei Dm.30916.

3D structure databases

ProteinModelPortali Q9V6X7.
SMRi Q9V6X7. Positions 28-386.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62315. 4 interactions.
DIPi DIP-20580N.
IntActi Q9V6X7. 3 interactions.
MINTi MINT-304675.
STRINGi 7227.FBpp0086649.

Protein family/group databases

CAZyi GT65. Glycosyltransferase Family 65.

Proteomic databases

PaxDbi Q9V6X7.
PRIDEi Q9V6X7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0087520 ; FBpp0086649 ; FBgn0033901 .
GeneIDi 36564.
KEGGi dme:Dmel_CG12366.

Organism-specific databases

CTDi 36564.
FlyBasei FBgn0033901. O-fut1.

Phylogenomic databases

eggNOGi NOG250895.
GeneTreei ENSGT00390000015634.
InParanoidi Q9V6X7.
KOi K03691.
OMAi SEHPVLA.
OrthoDBi EOG7ZD1VC.
PhylomeDBi Q9V6X7.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_180761. Pre-NOTCH Processing in the Endoplasmic Reticulum.
SignaLinki Q9V6X7.

Miscellaneous databases

GenomeRNAii 36564.
NextBioi 799227.
PROi Q9V6X7.

Gene expression databases

Bgeei Q9V6X7.
ExpressionAtlasi Q9V6X7. differential.

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. "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.
    , 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. 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. 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.

Entry informationi

Entry nameiOFUT1_DROME
AccessioniPrimary (citable) accession number: Q9V6X7
Secondary accession number(s): Q5BIC9, Q86SA7, Q8MSR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 103 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