DUSK3_DROME
ID DUSK3_DROME Reviewed; 411 AA.
AC Q9VVW5; Q86P14; Q95SV1; Q9VVW4;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Dual specificity protein phosphatase Mpk3 {ECO:0000250|UniProtKB:Q16828};
DE EC=3.1.3.16 {ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:15033693};
DE EC=3.1.3.48 {ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:15033693};
DE AltName: Full=Drosophila MKP3 {ECO:0000303|PubMed:12810595};
DE Short=DMKP3 {ECO:0000303|PubMed:12810595};
DE AltName: Full=Mitogen-activated protein kinase phosphatase 3 {ECO:0000250|UniProtKB:Q16828, ECO:0000312|EMBL:AAF49192.2};
DE Short=MAP kinase phosphatase 3 {ECO:0000250|UniProtKB:Q16828};
DE Short=MKP-3 {ECO:0000250|UniProtKB:Q16828};
GN Name=Mkp3; ORFNames=CG14080;
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] (ISOFORM B), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, INTERACTION WITH RL, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 56-ARG-ARG-57 AND CYS-302.
RX PubMed=11742539; DOI=10.1042/bj3610143;
RA Kim S.H., Kwon H.B., Kim Y.S., Ryu J.H., Kim K.S., Ahn Y., Lee W.J.,
RA Choi K.Y.;
RT "Isolation and characterization of a Drosophila homologue of mitogen-
RT activated protein kinase phosphatase-3 which has a high substrate
RT specificity towards extracellular-signal-regulated kinase.";
RL Biochem. J. 361:143-151(2002).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39540.1}; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=15033693; DOI=10.1196/annals.1299.007;
RA Kim S.E., Kim S.H., Choi K.Y.;
RT "Regulation of Drosophila MKP-3 by Drosophila ERK.";
RL Ann. N. Y. Acad. Sci. 1010:51-61(2003).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12810595; DOI=10.1242/dev.00568;
RA Rintelen F., Hafen E., Nairz K.;
RT "The Drosophila dual-specificity ERK phosphatase DMKP3 cooperates with the
RT ERK tyrosine phosphatase PTP-ER.";
RL Development 130:3479-3490(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14701731; DOI=10.1128/mcb.24.2.573-583.2004;
RA Kim M., Cha G.H., Kim S., Lee J.H., Park J., Koh H., Choi K.Y., Chung J.;
RT "MKP-3 has essential roles as a negative regulator of the Ras/mitogen-
RT activated protein kinase pathway during Drosophila development.";
RL Mol. Cell. Biol. 24:573-583(2004).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF TYR-316.
RX PubMed=15704110; DOI=10.1002/dvdy.20227;
RA Gomez A.R., Lopez-Varea A., Molnar C., de la Calle-Mustienes E.,
RA Ruiz-Gomez M., Gomez-Skarmeta J.L., de Celis J.F.;
RT "Conserved cross-interactions in Drosophila and Xenopus between Ras/MAPK
RT signaling and the dual-specificity phosphatase MKP3.";
RL Dev. Dyn. 232:695-708(2005).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16831830; DOI=10.1242/dev.02482;
RA Cela C., Llimargas M.;
RT "Egfr is essential for maintaining epithelial integrity during tracheal
RT remodelling in Drosophila.";
RL Development 133:3115-3125(2006).
CC -!- FUNCTION: Negatively regulates the activity of members of the MAP
CC kinase family in response to changes in the cellular environment. Has a
CC specificity for the ERK family. Acts as negative regulator in a variety
CC of developmental processes including cell differentiation and
CC proliferation controlled by the Ras/ERK pathway. Suppresses the
CC photoreceptor cell differentiation and wing vein formation. Required
CC for proper oogenesis and early embryogenesis. Functions autonomously in
CC a subset of photoreceptor progenitor cells in eye imaginal disks.
CC Appears also to be required in surrounding non-neuronal cells for
CC ommatidial patterning and photoreceptor differentiation. Plays a role
CC in the maintenance of epithelial integrity during tracheal development.
CC {ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:12810595,
CC ECO:0000269|PubMed:14701731, ECO:0000269|PubMed:15033693,
CC ECO:0000269|PubMed:15704110, ECO:0000269|PubMed:16831830}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:15033693};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:15033693};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:15033693};
CC -!- ACTIVITY REGULATION: Activity abolished by tyrosine phosphatase
CC inhibitor sodium vanadate. Activated by rl.
CC {ECO:0000269|PubMed:11742539, ECO:0000269|PubMed:15033693}.
CC -!- SUBUNIT: Interacts (via N-terminal region) with phosphorylated rl.
CC {ECO:0000269|PubMed:11742539}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11742539}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|EMBL:AAF49192.2};
CC IsoId=Q9VVW5-1; Sequence=Displayed;
CC Name=A {ECO:0000312|EMBL:AAF49193.2};
CC IsoId=Q9VVW5-2; Sequence=VSP_041148;
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in eye and wing imaginal
CC disks. Enriched in ovary. {ECO:0000269|PubMed:14701731}.
CC -!- DEVELOPMENTAL STAGE: Low expression in the various developmental
CC stages, although relatively high levels detected in 8 to 12 h embryos,
CC as well as in pupae and adults, particularly in the head region.
CC Expressed in third-instar eye imaginal disks posterior to the
CC morphogenetic furrow where photoreceptor differentiation occurs.
CC Preferentially detected in wing imaginal disks in two stripes of cells
CC interrupted at the dorsoventral boundary, which correspond to the
CC developing veins L3 and L4. In pupal wings the maximal levels of
CC expression are present in all longitudinal veins, with low levels
CC detected in most intervein cells. Uniformly distributed in the
CC syncytial blastoderm (stage 4). At early stage 5, accumulates at the
CC embryonic poles and is absent from the central region. This pattern
CC evolves very rapidly with the formation of a third central domain of
CC expression from 85% to 40% egg length. In older embryos, the main
CC places where high levels accumulate correspond to the invaginating
CC mesoderm, the tracheal pits at stage 11, the visceral mesoderm at stage
CC 13, the heart, the midline and the apodema. Expression in tracheal
CC branches at later stages. {ECO:0000269|PubMed:11742539,
CC ECO:0000269|PubMed:12810595, ECO:0000269|PubMed:15704110,
CC ECO:0000269|PubMed:16831830}.
CC -!- DISRUPTION PHENOTYPE: Homozygous embryonic lethal, while hypomorphic
CC alleles (reduction in gene dosage) lead to extra photoreceptor cells in
CC the eye, ectopic veins in wings and severe defects in oogenesis in
CC females. Females with the germ line mutation lay only a small number of
CC eggs. The laid eggs are abnormal, approximately 77% of the laid eggs
CC are shorter and some display severe defects in chorion formation. These
CC embryos could not escape the embryonic stage and progress beyond the
CC two-nuclei stage. Null mutants are viable and fertile exhibiting a
CC mild, but significant increase in wing vein material. They are slightly
CC rough eyed. Null mutation affects the R3 and R4 photoreceptors with a
CC low penetrance resulting in either the loss of one cell of the R3/R4
CC pair or in the misdifferentiation of these photoreceptors. R3 and R4
CC are often symmetrically arranged in the eye in opposite to the
CC asymmetrical positions they adopt in wild-type ommatidium. Ommatidia of
CC the null mutants often contain a mystery cell having differentiated as
CC a photoreceptor. Null mutants also exhibit mild delay in tracheal
CC branching. Delay in 12% dorsal branches (DBs) compared with 0.3% in
CC wild-type between metameres 4 to 8 that have reached the dorsal midline
CC at stage 14-15. Null mutants have defects in cell intercalation.
CC {ECO:0000269|PubMed:12810595, ECO:0000269|PubMed:14701731,
CC ECO:0000269|PubMed:16831830}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39540.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY043264; AAK85311.1; -; mRNA.
DR EMBL; AE014296; AAF49192.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF49193.2; -; Genomic_DNA.
DR EMBL; AY060472; AAL25511.1; -; mRNA.
DR EMBL; BT003536; AAO39540.1; ALT_INIT; mRNA.
DR RefSeq; NP_001262032.1; NM_001275103.1. [Q9VVW5-1]
DR RefSeq; NP_649087.1; NM_140830.2. [Q9VVW5-1]
DR RefSeq; NP_730385.1; NM_168785.1. [Q9VVW5-2]
DR AlphaFoldDB; Q9VVW5; -.
DR SMR; Q9VVW5; -.
DR BioGRID; 65359; 8.
DR STRING; 7227.FBpp0305422; -.
DR PaxDb; Q9VVW5; -.
DR PRIDE; Q9VVW5; -.
DR DNASU; 40081; -.
DR EnsemblMetazoa; FBtr0075035; FBpp0074802; FBgn0036844. [Q9VVW5-1]
DR EnsemblMetazoa; FBtr0075036; FBpp0074803; FBgn0036844. [Q9VVW5-2]
DR EnsemblMetazoa; FBtr0333220; FBpp0305422; FBgn0036844. [Q9VVW5-1]
DR GeneID; 40081; -.
DR KEGG; dme:Dmel_CG14080; -.
DR UCSC; CG14080-RA; d. melanogaster.
DR UCSC; CG14080-RB; d. melanogaster. [Q9VVW5-1]
DR CTD; 40081; -.
DR FlyBase; FBgn0036844; Mkp3.
DR VEuPathDB; VectorBase:FBgn0036844; -.
DR eggNOG; KOG1717; Eukaryota.
DR GeneTree; ENSGT00940000169406; -.
DR InParanoid; Q9VVW5; -.
DR OMA; IEFDRWA; -.
DR PhylomeDB; Q9VVW5; -.
DR Reactome; R-DME-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-DME-202670; ERKs are inactivated.
DR Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
DR SignaLink; Q9VVW5; -.
DR BioGRID-ORCS; 40081; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40081; -.
DR PRO; PR:Q9VVW5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036844; Expressed in anlage and 73 other tissues.
DR ExpressionAtlas; Q9VVW5; baseline and differential.
DR Genevisible; Q9VVW5; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IDA:FlyBase.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0007474; P:imaginal disc-derived wing vein specification; IMP:FlyBase.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IMP:FlyBase.
DR GO; GO:0002385; P:mucosal immune response; IMP:FlyBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007428; P:primary branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:FlyBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:FlyBase.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..411
FT /note="Dual specificity protein phosphatase Mpk3"
FT /id="PRO_0000408762"
FT DOMAIN 22..149
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 214..358
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 184..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_041148"
FT MUTAGEN 56..57
FT /note="RR->AA: Reduces binding affinity to substrate by
FT approximately 18-fold."
FT /evidence="ECO:0000269|PubMed:11742539"
FT MUTAGEN 302
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11742539"
FT MUTAGEN 316
FT /note="Y->N: Causes the differentiation of ectopic vein
FT stretches in several regions of the wing. Shows elimination
FT of distal stretches of longitunal veins L2-L5. Causes
FT substitution of the wing by proximal hinge tissue. Affects
FT the development of macrochaetae or the formation of the
FT thorax."
FT /evidence="ECO:0000269|PubMed:15704110"
FT CONFLICT 208
FT /note="H -> L (in Ref. 1; AAK85311 and 4; AAL25511)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="T -> A (in Ref. 1; AAK85311 and 4; AAL25511)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 45792 MW; D3C689BC953B29E3 CRC64;
MPETEHETCS KEWLQSQLRS LDSKDLILLD CRGSHEYSES HIRGAVNLCI PSIVLRRLAV
GKIDLASTIK SPELKQRIQS GYKLCWFILY NGEGVPGQNQ EIAGAGSLAV AMDSIISILH
RRLKQDGCRV VALQDGFNNF RQAFPEWCED DNQTHSKEIE SSRNVQTDQL MGLRSLRIST
TQSDSACSSS AESSDCESSS HHHHHHSHHN YNEAPVEIIP GLLFLGNATH SCDSEALKKY
NIKYVLNVTP DLPNKFKESG DIKYLQIPIT DHYSQDLAIH FPDAIQFIEE ARSASSVVLV
HCLAGVSRSV TVTLAYLMHT RGLSLNDAFA MVRDRKPDVS PNFHFMQQLL SFESQLRLRP
GSRFSCSCIA PDCNCMQTTG FMATHLANAT GVSPDSGIEF DRWTPSDTGL K
