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Protein

GDP-fucose protein O-fucosyltransferase 1

Gene

O-fut1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei349SubstrateBy similarity1

GO - Molecular functioni

  • fucosyltransferase activity Source: FlyBase
  • Notch binding Source: FlyBase
  • peptide-O-fucosyltransferase activity Source: FlyBase

GO - Biological processi

  • embryo development Source: UniProtKB
  • endocytosis Source: FlyBase
  • fucose metabolic process Source: UniProtKB-KW
  • lateral inhibition Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • Notch signaling pathway Source: UniProtKB
  • O-glycan processing Source: UniProtKB
  • positive regulation of Notch signaling pathway Source: FlyBase
  • protein catabolic process Source: FlyBase
  • protein O-linked fucosylation Source: FlyBase
  • protein O-linked glycosylation Source: UniProtKB
  • regulation of Notch signaling pathway Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • single organismal cell-cell adhesion Source: FlyBase

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processCarbohydrate metabolism, Fucose metabolism, Notch signaling pathway

Enzyme and pathway databases

BRENDAi2.4.1.221. 1994.
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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0033901. O-fut1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000001215324 – 402GDP-fucose protein O-fucosyltransferase 1Add BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi36 ↔ 38By similarity
Glycosylationi60N-linked (GlcNAc...) asparagineSequence analysis1
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

BgeeiFBgn0033901.
ExpressionAtlasiQ9V6X7. differential.
GenevisibleiQ9V6X7. DM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • Notch binding Source: FlyBase

Protein-protein interaction databases

BioGridi62315. 6 interactors.
DIPiDIP-20580N.
IntActiQ9V6X7. 3 interactors.
MINTiMINT-304675.
STRINGi7227.FBpp0086649.

Structurei

3D structure databases

ProteinModelPortaliQ9V6X7.
SMRiQ9V6X7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 44Substrate bindingBy similarity3
Regioni243 – 245Substrate bindingBy similarity3
Regioni366 – 367Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the glycosyltransferase 68 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3849. Eukaryota.
ENOG410Y3JQ. LUCA.
GeneTreeiENSGT00390000015634.
InParanoidiQ9V6X7.
KOiK03691.
OMAiGQSNHFI.
OrthoDBiEOG091G048B.
PhylomeDBiQ9V6X7.

Family and domain databases

InterProiView protein in InterPro
IPR019378. GDP-Fuc_O-FucTrfase.
PfamiView protein in Pfam
PF10250. O-FucT. 1 hit.

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti371E → V in AAM50020 (PubMed:12537569).Curated1
Sequence conflicti389K → E in BAC55010 (PubMed:12917292).Curated1
Sequence conflicti389K → E in AAX33443 (Ref. 4) Curated1

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.
FBtr0339959; FBpp0308981; FBgn0033901.
GeneIDi36564.
KEGGidme:Dmel_CG12366.

Similar proteinsi

Entry informationi

Entry nameiOFUT1_DROME
AccessioniPrimary (citable) accession number: Q9V6X7
Secondary accession number(s): Q5BIC9, Q86SA7, Q8MSR1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 2000
Last modified: September 27, 2017
This is version 129 of the entry and version 1 of the sequence. See 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