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Protein

Fringe glycosyltransferase

Gene

fng

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Glycosyltransferase involved in the elongation of O-linked ligands to activate Notch signaling. Possesses fucose-specific beta-1,3-N-acetylglucosaminyltransferase activity; extends the O-linked fucose on the Notch EGF repeats. Boundary-specific cell-signaling molecule that is responsible for dorsal-ventral cell interactions during wing development.5 Publications

Catalytic activityi

Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose residue of a fucosylated protein acceptor.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei164 – 1641SubstrateBy similarity
Binding sitei237 – 2371SubstrateBy similarity
Metal bindingi238 – 2381ManganeseBy similarity
Active sitei327 – 3271By similarity
Metal bindingi351 – 3511ManganeseBy similarity

GO - Molecular functioni

  • acetylglucosaminyltransferase activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity Source: FlyBase
  • UDP-glycosyltransferase activity Source: FlyBase

GO - Biological processi

  • cell fate specification Source: FlyBase
  • compound eye development Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • cuticle pattern formation Source: FlyBase
  • dorsal/ventral lineage restriction, imaginal disc Source: FlyBase
  • dorsal/ventral pattern formation, imaginal disc Source: FlyBase
  • female germ-line stem cell population maintenance Source: FlyBase
  • fucose metabolic process Source: FlyBase
  • germarium-derived egg chamber formation Source: FlyBase
  • imaginal disc-derived leg segmentation Source: FlyBase
  • imaginal disc-derived wing margin morphogenesis Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • Notch signaling pathway Source: FlyBase
  • oogenesis Source: FlyBase
  • positive regulation of Notch signaling pathway Source: FlyBase
  • protein O-linked glycosylation Source: FlyBase
  • regulation of Notch signaling pathway Source: FlyBase
  • wing disc dorsal/ventral pattern formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

SignaLinkiQ24342.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Fringe glycosyltransferase (EC:2.4.1.222)
Alternative name(s):
O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
Gene namesi
Name:fng
ORF Names:CG10580
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0011591. fng.

Subcellular locationi

  • Golgi apparatus membrane 1 Publication; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence analysisAdd
BLAST
Transmembranei16 – 3419Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 412378LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: FlyBase
  • Golgi apparatus Source: FlyBase
  • Golgi medial cisterna Source: FlyBase
  • Golgi stack Source: FlyBase
  • integral component of Golgi membrane Source: InterPro
  • integral component of membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi236 – 2383DDD → NNN: Abolishes activity. 1 Publication
Mutagenesisi236 – 2361D → A: Abolishes activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Fringe glycosyltransferasePRO_0000219175Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi204 ↔ 215By similarity
Disulfide bondi233 ↔ 297By similarity
Disulfide bondi400 ↔ 409By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ24342.
PRIDEiQ24342.

Expressioni

Tissue specificityi

Expressed in dorsal cells.

Gene expression databases

BgeeiQ24342.
GenevisibleiQ24342. DM.

Interactioni

Protein-protein interaction databases

BioGridi65569. 10 interactions.
IntActiQ24342. 1 interaction.
MINTiMINT-133040.
STRINGi7227.FBpp0077925.

Structurei

3D structure databases

ProteinModelPortaliQ24342.
SMRiQ24342. Positions 146-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
GeneTreeiENSGT00390000009913.
InParanoidiQ24342.
KOiK05948.
OMAiWISRNAQ.
OrthoDBiEOG7ZSHTD.
PhylomeDBiQ24342.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q24342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSLTVLSPP QRFKRILQAM MLAVAVVYMT LLLYQSAYGY PGIQVPHSQV
60 70 80 90 100
DALASEAVTT HRDQLLQDYV QSSTPTQPGA GAPAASPTTV IIRKDIRSFN
110 120 130 140 150
FSDIEVSERP TATLLTELAR RSRNGELLRD LSQRAVTATP QPPVTELDDI
160 170 180 190 200
FISVKTTKNY HDTRLALIIK TWFQLARDQT WFFTDTDDHY YQEKTKGHLI
210 220 230 240 250
NTKCSQGHFR KALCCKMSAE LDVFLESGKK WFCHFDDDNY VNVPRLVKLL
260 270 280 290 300
DEYSPSVDWY LGKPSISSPL EIHLDSKNTT TNKKITFWFA TGGAGFCLSR
310 320 330 340 350
ALTLKMLPIA GGGKFISIGD KIRFPDDVTM GFIIEHLLKV PLTVVDNFHS
360 370 380 390 400
HLEPMEFIRQ DTFQDQVSFS YAHMKNQWNV IKVDGFDMKT DPKRFYSLHC
410
QLFPYFSFCP PR
Length:412
Mass (Da):46,992
Last modified:November 1, 1996 - v1
Checksum:i0B1D23EFC4B7686B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35770 mRNA. Translation: AAA64525.1.
AE014296 Genomic DNA. Translation: AAF51658.2.
AY070927 mRNA. Translation: AAL48549.1.
PIRiA55376.
RefSeqiNP_524191.1. NM_079467.3.
UniGeneiDm.4336.

Genome annotation databases

EnsemblMetazoaiFBtr0078267; FBpp0077925; FBgn0011591.
GeneIDi40314.
KEGGidme:Dmel_CG10580.
UCSCiCG10580-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35770 mRNA. Translation: AAA64525.1.
AE014296 Genomic DNA. Translation: AAF51658.2.
AY070927 mRNA. Translation: AAL48549.1.
PIRiA55376.
RefSeqiNP_524191.1. NM_079467.3.
UniGeneiDm.4336.

3D structure databases

ProteinModelPortaliQ24342.
SMRiQ24342. Positions 146-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65569. 10 interactions.
IntActiQ24342. 1 interaction.
MINTiMINT-133040.
STRINGi7227.FBpp0077925.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

PaxDbiQ24342.
PRIDEiQ24342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078267; FBpp0077925; FBgn0011591.
GeneIDi40314.
KEGGidme:Dmel_CG10580.
UCSCiCG10580-RA. d. melanogaster.

Organism-specific databases

CTDi40314.
FlyBaseiFBgn0011591. fng.

Phylogenomic databases

eggNOGiENOG410II9W. Eukaryota.
ENOG410XS8Y. LUCA.
GeneTreeiENSGT00390000009913.
InParanoidiQ24342.
KOiK05948.
OMAiWISRNAQ.
OrthoDBiEOG7ZSHTD.
PhylomeDBiQ24342.

Enzyme and pathway databases

SignaLinkiQ24342.

Miscellaneous databases

GenomeRNAii40314.
PROiQ24342.

Gene expression databases

BgeeiQ24342.
GenevisibleiQ24342. DM.

Family and domain databases

InterProiIPR017374. Fringe.
IPR003378. Fringe-like.
[Graphical view]
PfamiPF02434. Fringe. 1 hit.
[Graphical view]
PIRSFiPIRSF038073. B-acetylgalactosaminyltfrase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fringe, a boundary-specific signaling molecule, mediates interactions between dorsal and ventral cells during Drosophila wing development."
    Irvine K.D., Wieschaus E.
    Cell 79:595-606(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Wing imaginal disk.
  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. "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].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "A family of mammalian Fringe genes implicated in boundary determination and the Notch pathway."
    Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D., Vogt T.F.
    Development 124:2245-2254(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-44.
  6. "Secreted fringe-like signaling molecules may be glycosyltransferases."
    Yuan Y.P., Schultz J., Mlodzik M., Bork P.
    Cell 88:9-11(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO THE LEX1 FAMILY.
  7. Cited for: FUNCTION.
  8. "Glycosyltransferase activity of Fringe modulates Notch-Delta interactions."
    Bruckner K., Perez L., Clausen H., Cohen S.
    Nature 406:411-415(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 236-ASP--ASP-238.
  9. "The notch signalling regulator fringe acts in the Golgi apparatus and requires the glycosyltransferase signature motif DXD."
    Munro S., Freeman M.
    Curr. Biol. 10:813-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-236.
  10. "Notch signaling: Fringe really is a glycosyltransferase."
    Blair S.S.
    Curr. Biol. 10:R608-R612(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiFNG_DROME
AccessioniPrimary (citable) accession number: Q24342
Secondary accession number(s): Q9VP97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.