ID EXT1_DROME Reviewed; 760 AA. AC Q9V730; O76796; Q5BI21; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Exostosin-1; DE EC=2.4.1.224 {ECO:0000269|PubMed:16303756}; DE EC=2.4.1.225 {ECO:0000269|PubMed:16303756}; DE AltName: Full=Protein tout-velu; DE Short=TTV {ECO:0000303|PubMed:16303756}; GN Name=ttv; Synonyms=DEXT1; ORFNames=CG10117; 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], FUNCTION, MEMBRANE TOPOLOGY, AND DEVELOPMENTAL RP STAGE. RX PubMed=9665133; DOI=10.1038/27932; RA Bellaiche Y., The I., Perrimon N.; RT "Tout-velu is a Drosophila homologue of the putative tumour suppressor EXT- RT 1 and is needed for Hh diffusion."; RL Nature 394:85-88(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16303756; DOI=10.1074/jbc.m509138200; RA Izumikawa T., Egusa N., Taniguchi F., Sugahara K., Kitagawa H.; RT "Heparan sulfate polymerization in Drosophila."; RL J. Biol. Chem. 281:1929-1934(2006). RN [3] 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP FUNCTION IN HH PATHWAY, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=10549295; DOI=10.1016/s1097-2765(00)80214-2; RA The I., Bellaiche Y., Perrimon N.; RT "Hedgehog movement is regulated through tout velu-dependent synthesis of a RT heparan sulfate proteoglycan."; RL Mol. Cell 4:633-639(1999). RN [7] RP ENZYME ACTIVITY. RX PubMed=10644674; DOI=10.1074/jbc.275.4.2269; RA Toyoda H., Kinoshita-Toyoda A., Selleck S.B.; RT "Structural analysis of glycosaminoglycans in Drosophila and Caenorhabditis RT elegans and demonstration that tout-velu, a Drosophila gene related to EXT RT tumor suppressors, affects heparan sulfate in vivo."; RL J. Biol. Chem. 275:2269-2275(2000). RN [8] RP FUNCTION IN HH PATHWAY. RX PubMed=10806213; DOI=10.1074/jbc.m003540200; RA Toyoda H., Kinoshita-Toyoda A., Fox B., Selleck S.B.; RT "Structural analysis of glycosaminoglycans in animals bearing mutations in RT sugarless, sulfateless, and tout-velu. Drosophila homologues of vertebrate RT genes encoding glycosaminoglycan biosynthetic enzymes."; RL J. Biol. Chem. 275:21856-21861(2000). RN [9] RP FUNCTION IN HH PATHWAY. RX PubMed=12586063; DOI=10.1016/s1534-5807(03)00031-5; RA Gallet A., Rodriguez R., Ruel L., Therond P.P.; RT "Cholesterol modification of hedgehog is required for trafficking and RT movement, revealing an asymmetric cellular response to hedgehog."; RL Dev. Cell 4:191-204(2003). RN [10] RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF RP GLY-447. RX PubMed=14645127; DOI=10.1242/dev.00913; RA Takei Y., Ozawa Y., Sato M., Watanabe A., Tabata T.; RT "Three Drosophila EXT genes shape morphogen gradients through synthesis of RT heparan sulfate proteoglycans."; RL Development 131:73-82(2004). RN [11] RP FUNCTION IN HH PATHWAY, AND DISRUPTION PHENOTYPE. RX PubMed=14729575; DOI=10.1242/dev.00958; RA Han C., Belenkaya T.Y., Wang B., Lin X.; RT "Drosophila glypicans control the cell-to-cell movement of Hedgehog by a RT dynamin-independent process."; RL Development 131:601-611(2004). RN [12] RP FUNCTION. RX PubMed=14998928; DOI=10.1242/dev.01051; RA Han C., Belenkaya T.Y., Khodoun M., Tauchi M., Lin X., Lin X.; RT "Distinct and collaborative roles of Drosophila EXT family proteins in RT morphogen signalling and gradient formation."; RL Development 131:1563-1575(2004). RN [13] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=15056609; DOI=10.1242/dev.01061; RA Bornemann D.J., Duncan J.E., Staatz W., Selleck S., Warrior R.; RT "Abrogation of heparan sulfate synthesis in Drosophila disrupts the RT Wingless, Hedgehog and Decapentaplegic signaling pathways."; RL Development 131:1927-1938(2004). RN [14] RP INTERACTION WITH SAU, AND SUBCELLULAR LOCATION. RX PubMed=23720043; DOI=10.1242/dev.087171; RA Chang W.L., Chang C.W., Chang Y.Y., Sung H.H., Lin M.D., Chang S.C., RA Chen C.H., Huang C.W., Tung K.S., Chou T.B.; RT "The Drosophila GOLPH3 homolog regulates the biosynthesis of heparan RT sulfate proteoglycans by modulating the retrograde trafficking of RT exostosins."; RL Development 140:2798-2807(2013). CC -!- FUNCTION: Glycosyltransferase required for the biosynthesis of heparan- CC sulfate and responsible for the alternating addition of beta-1-4-linked CC glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine CC (GlcNAc) units to nascent heparan sulfate chains. Botv is the trigger CC of heparan sulfate chain initiation and polymerization takes place by a CC complex of ttv and sotv. Plays a central role in the diffusion of CC morphogens hedgehog (hh), wingless (wg) and decapentaplegic (dpp) via CC its role in heparan sulfate proteoglycans (HSPGs) biosynthesis which CC are required for movement of hh, dpp and wg morphogens. CC {ECO:0000269|PubMed:10549295, ECO:0000269|PubMed:10806213, CC ECO:0000269|PubMed:12586063, ECO:0000269|PubMed:14645127, CC ECO:0000269|PubMed:14729575, ECO:0000269|PubMed:14998928, CC ECO:0000269|PubMed:15056609, ECO:0000269|PubMed:16303756, CC ECO:0000269|PubMed:9665133}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)- CC beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L- CC seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{alpha-D- CC GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n)-(1->4)-beta-D- CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl- CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:16213, Rhea:RHEA-COMP:12621, CC Rhea:RHEA-COMP:12623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416; CC EC=2.4.1.224; Evidence={ECO:0000269|PubMed:16303756}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16214; CC Evidence={ECO:0000269|PubMed:16303756}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-O-{alpha-D-GlcNAc-[(1->4)-beta-D-GlcA-(1->4)-alpha-D- CC GlcNAc](n)-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal- CC (1->4)-beta-D-Xyl}-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3- CC O-{[(1->4)-beta-D-GlcA-(1->4)-alpha-D-GlcNAc](n+1)-(1->4)-beta-D- CC GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl- CC [protein] + H(+) + UDP; Xref=Rhea:RHEA:20908, Rhea:RHEA-COMP:12623, CC Rhea:RHEA-COMP:14295, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132415, ChEBI:CHEBI:132416; CC EC=2.4.1.225; Evidence={ECO:0000269|PubMed:16303756}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20909; CC Evidence={ECO:0000269|PubMed:16303756}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q9ES89}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. CC -!- PATHWAY: Glycan metabolism; heparin biosynthesis. CC -!- SUBUNIT: Interacts with sau (PubMed:23720043). CC -!- INTERACTION: CC Q9V730; Q9Y169: sotv; NbExp=3; IntAct=EBI-166374, EBI-142791; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type CC II membrane protein. Golgi apparatus membrane; Single-pass type II CC membrane protein. Note=Localization to the Golgi may be regulated by CC sau (PubMed:23720043). CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in early embryos. Later (in CC stage 10 embryos), it is expressed at higher level in the nervous CC system. Ubiquitously expressed in wing imaginal disk. CC {ECO:0000269|PubMed:10549295, ECO:0000269|PubMed:14645127}. CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. CC {ECO:0000269|PubMed:9665133}. CC -!- DISRUPTION PHENOTYPE: According to some authors (PubMed:10549295) ttv CC mutants have no effect on wg signaling, while according to others CC (PubMed:14645127, PubMed:14729575, PubMed:15056609) wg signaling is CC affected. Such discrepancy may be explained by the fact that the CC absence of ttv could be partially compensated by the intact sotv CC protein. {ECO:0000269|PubMed:10549295, ECO:0000269|PubMed:14645127, CC ECO:0000269|PubMed:14729575, ECO:0000269|PubMed:15056609}. CC -!- MISCELLANEOUS: 'Tout velu' means 'very hairy' in French. CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC32397.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF083889; AAC32397.1; ALT_FRAME; mRNA. DR EMBL; AB221351; BAE78509.1; -; mRNA. DR EMBL; AE013599; AAF58236.1; -; Genomic_DNA. DR EMBL; BT021403; AAX33551.1; -; mRNA. DR RefSeq; NP_001260971.1; NM_001274042.1. DR RefSeq; NP_477231.1; NM_057883.3. DR AlphaFoldDB; Q9V730; -. DR SMR; Q9V730; -. DR BioGRID; 62362; 10. DR IntAct; Q9V730; 5. DR STRING; 7227.FBpp0423167; -. DR CAZy; GT47; Glycosyltransferase Family 47. DR CAZy; GT64; Glycosyltransferase Family 64. DR GlyCosmos; Q9V730; 3 sites, No reported glycans. DR GlyGen; Q9V730; 3 sites. DR PaxDb; 7227-FBpp0305367; -. DR EnsemblMetazoa; FBtr0087495; FBpp0086624; FBgn0265974. DR EnsemblMetazoa; FBtr0333164; FBpp0305367; FBgn0265974. DR GeneID; 36614; -. DR KEGG; dme:Dmel_CG10117; -. DR AGR; FB:FBgn0265974; -. DR CTD; 36614; -. DR FlyBase; FBgn0265974; ttv. DR VEuPathDB; VectorBase:FBgn0265974; -. DR eggNOG; KOG1021; Eukaryota. DR GeneTree; ENSGT00940000163960; -. DR HOGENOM; CLU_013906_4_1_1; -. DR InParanoid; Q9V730; -. DR OMA; RNRYMWN; -. DR PhylomeDB; Q9V730; -. DR BRENDA; 2.4.1.224; 1994. DR BRENDA; 2.4.1.225; 1994. DR Reactome; R-DME-2022928; HS-GAG biosynthesis. DR SignaLink; Q9V730; -. DR UniPathway; UPA00378; -. DR UniPathway; UPA00756; -. DR UniPathway; UPA00862; -. DR BioGRID-ORCS; 36614; 1 hit in 3 CRISPR screens. DR GenomeRNAi; 36614; -. DR PRO; PR:Q9V730; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0265974; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other cell types or tissues. DR ExpressionAtlas; Q9V730; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:FlyBase. DR GO; GO:0050508; F:glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; ISS:UniProtKB. DR GO; GO:0015020; F:glucuronosyltransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050509; F:N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; IDA:FlyBase. DR GO; GO:0007411; P:axon guidance; IGI:FlyBase. DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase. DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IMP:UniProtKB. DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IMP:UniProtKB. DR GO; GO:0015014; P:heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process; IDA:FlyBase. DR GO; GO:0030210; P:heparin biosynthetic process; IMP:UniProtKB. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISS:UniProtKB. DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR InterPro; IPR004263; Exostosin. DR InterPro; IPR040911; Exostosin_GT47. DR InterPro; IPR015338; GT64. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR48261; ACETYLGLUCOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR48261:SF2; EXOSTOSIN-1-LIKE; 1. DR Pfam; PF03016; Exostosin; 1. DR Pfam; PF09258; Glyco_transf_64; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR Genevisible; Q9V730; DM. PE 1: Evidence at protein level; KW Developmental protein; Disulfide bond; Endoplasmic reticulum; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix; Wnt signaling pathway. FT CHAIN 1..760 FT /note="Exostosin-1" FT /id="PRO_0000149664" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..25 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 26..760 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 540..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 670 FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 437 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 565 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 581 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 582 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 583 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 583 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 669 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 670 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT BINDING 713 FT /ligand="UDP-N-acetyl-alpha-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:57705" FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 327 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 476 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 668..716 FT /evidence="ECO:0000250|UniProtKB:Q9ES89" FT MUTAGEN 447 FT /note="G->D: In ttv205; induces defects in wing patterning FT due to impaired movement of morphogens." FT /evidence="ECO:0000269|PubMed:14645127" SQ SEQUENCE 760 AA; 87309 MW; F6369F0BA206DEA9 CRC64; MQAKKRYILV FVSCAFLAYA YFGGYRLKVS PLRPRRAQHE SAKDGGVQPH EQLPSFLGAH DMQELQLLQS NQSKSLDSSK HLVTRKPDCR METCFDFTRC YDRFLVYIYP PEPLNSLGAA PPTSANYQKI LTAIQESRYY TSDPTAACLF VLGIDTLDRD SLSEDYVRNV PSRLARLPYW NNGRNHIIFN LYSGTWPDYA ENSLGFDAGE AILAKASMGV LQLRHGFDVS IPLFHKQFPL RAGATGTVQS NNFPANKKYL LAFKGKRYVH GIGSETRNSL FHLHNGRDMV LVTTCRHGKS WRELQDNRCD EDNREYDRYD YETLLQNSTF CLVPRGRRLG SFRFLEALQA GCIPVLLSNA WVLPFESKID WKQAAIWADE RLLLQVPDIV RSIPAERIFA LRQQTQVLWE RYFGSIEKIV FTTFEIIRER LPDYPVRSSL VWNSSPGALL TLPTFADSSR YMPFLLNSMG AEPRHNYTAV IYVQIGAALG PNAALYKLVR TITKSQFVER ILVLWAADRP LPLKKRWPPT SHIPLHVISL GGSTRSQGAG PTSQTTEGRP SISQRFLPYD EIQTDAVLSL DEDAILNTDE LDFAYTVWRD FPERIVGYPA RAHFWDDSKN AWGYTSKWTN YYSIVLTGAA FYHRYYNYLY TNWLSLLLLK TVQQSSNCED ILMNLLVSHV TRKPPIKVTQ RKGYKDRETG RSPWNDPDHF IQRQSCLNTF AAVFGYMPLI RSNLRMDPML YRDPVSNLRK KYRQIELVGS //