FNG_DROME
ID FNG_DROME Reviewed; 412 AA.
AC Q24342; Q9VP97;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Fringe glycosyltransferase;
DE EC=2.4.1.222;
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=fng; ORFNames=CG10580;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Wing imaginal disk;
RX PubMed=7954826; DOI=10.1016/0092-8674(94)90545-2;
RA Irvine K.D., Wieschaus E.;
RT "Fringe, a boundary-specific signaling molecule, mediates interactions
RT between dorsal and ventral cells during Drosophila wing development.";
RL Cell 79:595-606(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PROTEIN SEQUENCE OF 40-44.
RX PubMed=9187150; DOI=10.1242/dev.124.11.2245;
RA Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D.,
RA Vogt T.F.;
RT "A family of mammalian Fringe genes implicated in boundary determination
RT and the Notch pathway.";
RL Development 124:2245-2254(1997).
RN [6]
RP SIMILARITY TO THE LEX1 FAMILY.
RX PubMed=9019410; DOI=10.1016/s0092-8674(00)81852-8;
RA Yuan Y.P., Schultz J., Mlodzik M., Bork P.;
RT "Secreted fringe-like signaling molecules may be glycosyltransferases.";
RL Cell 88:9-11(1997).
RN [7]
RP FUNCTION.
RX PubMed=10935626; DOI=10.1038/35019000;
RA Moloney D.J., Panin V.M., Johnston S.H., Chen J., Shao L., Wilson R.,
RA Wang Y., Stanley P., Irvine K.D., Haltiwanger R.S., Vogt T.F.;
RT "Fringe is a glycosyltransferase that modifies Notch.";
RL Nature 406:369-375(2000).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF 236-ASP--ASP-238.
RX PubMed=10935637; DOI=10.1038/35019075;
RA Bruckner K., Perez L., Clausen H., Cohen S.;
RT "Glycosyltransferase activity of Fringe modulates Notch-Delta
RT interactions.";
RL Nature 406:411-415(2000).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-236.
RX PubMed=10899003; DOI=10.1016/s0960-9822(00)00578-9;
RA Munro S., Freeman M.;
RT "The notch signalling regulator fringe acts in the Golgi apparatus and
RT requires the glycosyltransferase signature motif DXD.";
RL Curr. Biol. 10:813-820(2000).
RN [10]
RP FUNCTION.
RX PubMed=10985380; DOI=10.1016/s0960-9822(00)00633-3;
RA Blair S.S.;
RT "Notch signaling: Fringe really is a glycosyltransferase.";
RL Curr. Biol. 10:R608-R612(2000).
CC -!- FUNCTION: Glycosyltransferase involved in the elongation of O-linked
CC ligands to activate Notch signaling. Possesses fucose-specific beta-
CC 1,3-N-acetylglucosaminyltransferase activity; extends the O-linked
CC fucose on the Notch EGF repeats. Boundary-specific cell-signaling
CC molecule that is responsible for dorsal-ventral cell interactions
CC during wing development. {ECO:0000269|PubMed:10899003,
CC ECO:0000269|PubMed:10935626, ECO:0000269|PubMed:10935637,
CC ECO:0000269|PubMed:10985380, ECO:0000269|PubMed:7954826}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-
CC (1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-
CC COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-
CC N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-
CC (1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-
CC COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:10899003}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:10899003}.
CC -!- TISSUE SPECIFICITY: Expressed in dorsal cells.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; L35770; AAA64525.1; -; mRNA.
DR EMBL; AE014296; AAF51658.2; -; Genomic_DNA.
DR EMBL; AY070927; AAL48549.1; -; mRNA.
DR PIR; A55376; A55376.
DR RefSeq; NP_524191.1; NM_079467.3.
DR AlphaFoldDB; Q24342; -.
DR SMR; Q24342; -.
DR BioGRID; 65569; 19.
DR IntAct; Q24342; 1.
DR MINT; Q24342; -.
DR STRING; 7227.FBpp0077925; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q24342; -.
DR DNASU; 40314; -.
DR EnsemblMetazoa; FBtr0078267; FBpp0077925; FBgn0011591.
DR GeneID; 40314; -.
DR KEGG; dme:Dmel_CG10580; -.
DR UCSC; CG10580-RA; d. melanogaster.
DR CTD; 40314; -.
DR FlyBase; FBgn0011591; fng.
DR VEuPathDB; VectorBase:FBgn0011591; -.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000164195; -.
DR HOGENOM; CLU_056611_0_0_1; -.
DR InParanoid; Q24342; -.
DR OMA; SENKMRP; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; Q24342; -.
DR SignaLink; Q24342; -.
DR BioGRID-ORCS; 40314; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40314; -.
DR PRO; PR:Q24342; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011591; Expressed in eye disc (Drosophila) and 52 other tissues.
DR Genevisible; Q24342; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:FlyBase.
DR GO; GO:0005795; C:Golgi stack; IDA:FlyBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033829; F:O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity; IDA:FlyBase.
DR GO; GO:0048749; P:compound eye development; IDA:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0035017; P:cuticle pattern formation; IMP:FlyBase.
DR GO; GO:0007450; P:dorsal/ventral pattern formation, imaginal disc; IDA:FlyBase.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:FlyBase.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IDA:FlyBase.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:FlyBase.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0043393; P:regulation of protein binding; IDA:FlyBase.
DR GO; GO:0048100; P:wing disc anterior/posterior pattern formation; IMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase.
DR InterPro; IPR017374; Fringe.
DR InterPro; IPR003378; Fringe-like.
DR Pfam; PF02434; Fringe; 1.
DR PIRSF; PIRSF038073; B-acetylgalactosaminyltfrase; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Direct protein sequencing; Disulfide bond;
KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..412
FT /note="Fringe glycosyltransferase"
FT /id="PRO_0000219175"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 327
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT DISULFID 204..215
FT /evidence="ECO:0000250"
FT DISULFID 233..297
FT /evidence="ECO:0000250"
FT DISULFID 400..409
FT /evidence="ECO:0000250"
FT MUTAGEN 236..238
FT /note="DDD->NNN: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:10935637"
FT MUTAGEN 236
FT /note="D->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:10899003"
SQ SEQUENCE 412 AA; 46992 MW; 0B1D23EFC4B7686B CRC64;
MMSLTVLSPP QRFKRILQAM MLAVAVVYMT LLLYQSAYGY PGIQVPHSQV DALASEAVTT
HRDQLLQDYV QSSTPTQPGA GAPAASPTTV IIRKDIRSFN FSDIEVSERP TATLLTELAR
RSRNGELLRD LSQRAVTATP QPPVTELDDI FISVKTTKNY HDTRLALIIK TWFQLARDQT
WFFTDTDDHY YQEKTKGHLI NTKCSQGHFR KALCCKMSAE LDVFLESGKK WFCHFDDDNY
VNVPRLVKLL DEYSPSVDWY LGKPSISSPL EIHLDSKNTT TNKKITFWFA TGGAGFCLSR
ALTLKMLPIA GGGKFISIGD KIRFPDDVTM GFIIEHLLKV PLTVVDNFHS HLEPMEFIRQ
DTFQDQVSFS YAHMKNQWNV IKVDGFDMKT DPKRFYSLHC QLFPYFSFCP PR
