EXT1_DROME
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 03-AUG-2022, entry version 153.
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 and 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.FBpp0305367; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR GlyGen; Q9V730; 3 sites.
DR PaxDb; Q9V730; -.
DR PRIDE; Q9V730; -.
DR EnsemblMetazoa; FBtr0087495; FBpp0086624; FBgn0265974.
DR EnsemblMetazoa; FBtr0333164; FBpp0305367; FBgn0265974.
DR GeneID; 36614; -.
DR KEGG; dme:Dmel_CG10117; -.
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; VSPGHEF; -.
DR OrthoDB; 789556at2759; -.
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 tissues.
DR ExpressionAtlas; Q9V730; baseline and differential.
DR Genevisible; Q9V730; DM.
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:0016021; C:integral component of 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:0016757; F:glycosyltransferase 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; IEA:UniProtKB-UniPathway.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISS:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
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 561..565
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 581..583
FT /ligand="substrate"
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 611
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 666..670
FT /ligand="substrate"
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
