ENA_DROME
ID ENA_DROME Reviewed; 980 AA.
AC Q8T4F7; A4UZP3; B7YZL0; Q24035; Q86NN6; Q8MMB3; Q9V8R3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein enabled;
GN Name=ena; Synonyms=enb; ORFNames=CG15112;
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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
RP INTERACTION WITH ABL AND SRC, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=7535279; DOI=10.1101/gad.9.5.521;
RA Gertler F.B., Comer A.R., Juang J.-L., Ahern S.M., Clark M.J., Liebl E.C.,
RA Hoffmann F.M.;
RT "Enabled, a dosage-sensitive suppressor of mutations in the Drosophila Abl
RT tyrosine kinase, encodes an Abl substrate with SH3 domain-binding
RT properties.";
RL Genes Dev. 9:521-533(1995).
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 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=15790972; DOI=10.1242/dev.01736;
RA Forsthoefel D.J., Liebl E.C., Kolodziej P.A., Seeger M.A.;
RT "The Abelson tyrosine kinase, the Trio GEF and Enabled interact with the
RT Netrin receptor Frazzled in Drosophila.";
RL Development 132:1983-1994(2005).
RN [7]
RP PHOSPHORYLATION AT TYR-425; TYR-607; TYR-625; TYR-650; TYR-666 AND TYR-826.
RX PubMed=9418863; DOI=10.1128/mcb.18.1.152;
RA Comer A.R., Ahern-Djamali S.M., Juang J.-L., Jackson P.D., Hoffmann F.M.;
RT "Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase
RT regulates the in vivo function and protein-protein interactions of
RT Enabled.";
RL Mol. Cell. Biol. 18:152-160(1998).
RN [8]
RP INTERACTION WITH CHIC.
RX PubMed=10220404; DOI=10.1073/pnas.96.9.4977;
RA Ahern-Djamali S.M., Bachmann C., Hua P., Reddy S.K., Kastenmeier A.S.,
RA Walter U., Hoffmann F.M.;
RT "Identification of profilin and src homology 3 domains as binding partners
RT for Drosophila enabled.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4977-4982(1999).
RN [9]
RP INTERACTION WITH ROBO.
RX PubMed=10892742; DOI=10.1016/s0092-8674(00)80883-1;
RA Bashaw G.J., Kidd T., Murray D., Pawson T., Goodman C.S.;
RT "Repulsive axon guidance: Abelson and Enabled play opposing roles
RT downstream of the roundabout receptor.";
RL Cell 101:703-715(2000).
RN [10]
RP INTERACTION WITH ZYX102EF.
RX PubMed=12594038; DOI=10.1016/s0378-1119(02)01173-3;
RA Renfranz P.J., Siegrist S.E., Stronach B.E., Macalma T., Beckerle M.C.;
RT "Molecular and phylogenetic characterization of Zyx102, a Drosophila
RT orthologue of the zyxin family that interacts with Drosophila Enabled.";
RL Gene 305:13-26(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=14762109; DOI=10.1242/jcs.00921;
RA Biyasheva A., Svitkina T., Kunda P., Baum B., Borisy G.;
RT "Cascade pathway of filopodia formation downstream of SCAR.";
RL J. Cell Sci. 117:837-848(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905; SER-914 AND SER-924, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Functions, together with Abl, trio and fra, in a complex
CC signaling network that regulates axon guidance at the CNS midline.
CC Required in part for robo-mediated repulsive axon guidance. May be
CC involved in lamellipodial dynamics. {ECO:0000269|PubMed:15790972}.
CC -!- SUBUNIT: Interacts with Abl and Src SH3 domains. Binds, in vitro and in
CC vivo, the cytoplasmic domain of robo. Interacts with Zyx102EF and chic.
CC {ECO:0000269|PubMed:10220404, ECO:0000269|PubMed:10892742,
CC ECO:0000269|PubMed:12594038, ECO:0000269|PubMed:7535279}.
CC -!- INTERACTION:
CC Q8T4F7; P00522: Abl; NbExp=2; IntAct=EBI-466810, EBI-534090;
CC Q8T4F7; P25843: chic; NbExp=3; IntAct=EBI-466810, EBI-156199;
CC Q8T4F7; P16621: Lar; NbExp=2; IntAct=EBI-466810, EBI-668630;
CC Q8T4F7; P05480: Src; Xeno; NbExp=2; IntAct=EBI-466810, EBI-298680;
CC -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
CC {ECO:0000269|PubMed:14762109}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14762109}. Note=Expressed at the leading edge of
CC lamellipodia. Colocalizes with chic at the periphery of cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4; Synonyms=F;
CC IsoId=Q8T4F7-4; Sequence=Displayed;
CC Name=1; Synonyms=B;
CC IsoId=Q8T4F7-1; Sequence=VSP_037651, VSP_037652, VSP_019865,
CC VSP_037653;
CC Name=2; Synonyms=A, C, E;
CC IsoId=Q8T4F7-2; Sequence=VSP_017574, VSP_017575;
CC Name=3; Synonyms=D;
CC IsoId=Q8T4F7-3; Sequence=VSP_017574, VSP_017575, VSP_019865,
CC VSP_019866;
CC -!- TISSUE SPECIFICITY: Expressed in axons of the embryonic nervous system.
CC {ECO:0000269|PubMed:7535279}.
CC -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC thymosin-like domain required for G-actin binding. The KLKR motif
CC within this block is essential for the G-actin binding and for actin
CC polymerization. Block B is required for F-actin binding and subcellular
CC location, and Block C for tetramerization.
CC -!- PTM: Tyrosine phosphorylated on multiple sites by Abl kinase. In vitro,
CC phosphorylation on specific tyrosine residues inhibits interaction with
CC Abl and Src SH3 domains. {ECO:0000269|PubMed:17372656,
CC ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:7535279,
CC ECO:0000269|PubMed:9418863}.
CC -!- SIMILARITY: Belongs to the Ena/VASP family. {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; U21123; AAA85120.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57598.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68438.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68439.2; -; Genomic_DNA.
DR EMBL; AE013599; AAX52696.1; -; Genomic_DNA.
DR EMBL; AE013599; AAX52697.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83163.1; -; Genomic_DNA.
DR EMBL; AY084210; AAL89948.1; -; mRNA.
DR EMBL; BT004488; AAO42652.1; -; mRNA.
DR PIR; A56154; A56154.
DR RefSeq; NP_001014536.1; NM_001014536.2. [Q8T4F7-2]
DR RefSeq; NP_001014537.1; NM_001014537.3. [Q8T4F7-3]
DR RefSeq; NP_001137709.1; NM_001144237.2. [Q8T4F7-4]
DR RefSeq; NP_725857.1; NM_166329.2. [Q8T4F7-2]
DR RefSeq; NP_725858.1; NM_166330.2. [Q8T4F7-2]
DR RefSeq; NP_725859.2; NM_166331.3. [Q8T4F7-1]
DR AlphaFoldDB; Q8T4F7; -.
DR SMR; Q8T4F7; -.
DR BioGRID; 62866; 68.
DR IntAct; Q8T4F7; 33.
DR STRING; 7227.FBpp0113115; -.
DR iPTMnet; Q8T4F7; -.
DR PaxDb; Q8T4F7; -.
DR PRIDE; Q8T4F7; -.
DR EnsemblMetazoa; FBtr0086582; FBpp0085766; FBgn0000578. [Q8T4F7-2]
DR EnsemblMetazoa; FBtr0086583; FBpp0085767; FBgn0000578. [Q8T4F7-2]
DR EnsemblMetazoa; FBtr0086584; FBpp0085768; FBgn0000578. [Q8T4F7-1]
DR EnsemblMetazoa; FBtr0100174; FBpp0099530; FBgn0000578. [Q8T4F7-3]
DR EnsemblMetazoa; FBtr0100176; FBpp0099532; FBgn0000578. [Q8T4F7-2]
DR EnsemblMetazoa; FBtr0114623; FBpp0113115; FBgn0000578. [Q8T4F7-4]
DR GeneID; 37201; -.
DR KEGG; dme:Dmel_CG15112; -.
DR UCSC; CG15112-RA; d. melanogaster.
DR CTD; 37201; -.
DR FlyBase; FBgn0000578; ena.
DR VEuPathDB; VectorBase:FBgn0000578; -.
DR eggNOG; KOG4590; Eukaryota.
DR GeneTree; ENSGT00940000171456; -.
DR InParanoid; Q8T4F7; -.
DR OrthoDB; 1161962at2759; -.
DR PhylomeDB; Q8T4F7; -.
DR Reactome; R-DME-446353; Cell-extracellular matrix interactions.
DR SignaLink; Q8T4F7; -.
DR BioGRID-ORCS; 37201; 0 hits in 3 CRISPR screens.
DR ChiTaRS; ena; fly.
DR GenomeRNAi; 37201; -.
DR PRO; PR:Q8T4F7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000578; Expressed in eye disc (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q8T4F7; baseline and differential.
DR Genevisible; Q8T4F7; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR GO; GO:0032433; C:filopodium tip; IDA:FlyBase.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IGI:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IGI:FlyBase.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IGI:FlyBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:FlyBase.
DR GO; GO:0060288; P:formation of a compartment boundary; IMP:FlyBase.
DR GO; GO:0007390; P:germ-band shortening; IMP:FlyBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:FlyBase.
DR GO; GO:0008258; P:head involution; IMP:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:FlyBase.
DR GO; GO:0031346; P:positive regulation of cell projection organization; IDA:FlyBase.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IPI:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:1990255; P:subsynaptic reticulum organization; IMP:FlyBase.
DR GO; GO:0007396; P:suture of dorsal opening; IMP:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR038023; VASP_sf.
DR InterPro; IPR014885; VASP_tetra.
DR InterPro; IPR000697; WH1/EVH1_dom.
DR Pfam; PF08776; VASP_tetra; 1.
DR Pfam; PF00568; WH1; 1.
DR SMART; SM00461; WH1; 1.
DR SUPFAM; SSF118370; SSF118370; 1.
DR PROSITE; PS50229; WH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell projection; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..980
FT /note="Protein enabled"
FT /id="PRO_0000227757"
FT DOMAIN 146..407
FT /note="WH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..980
FT /note="EVH2"
FT REGION 791..810
FT /note="EVH2 block A"
FT REGION 837..854
FT /note="EVH2 block B"
FT REGION 947..980
FT /note="EVH2 block C"
FT MOTIF 800..803
FT /note="KLKR"
FT COMPBIAS 570..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9418863"
FT MOD_RES 607
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9418863"
FT MOD_RES 625
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9418863"
FT MOD_RES 650
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9418863"
FT MOD_RES 666
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9418863"
FT MOD_RES 826
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9418863"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2..297
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_017574"
FT VAR_SEQ 147
FT /note="L -> F (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037651"
FT VAR_SEQ 148..298
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037652"
FT VAR_SEQ 298
FT /note="A -> T (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_017575"
FT VAR_SEQ 482
FT /note="S -> SRNSL (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.5"
FT /id="VSP_019865"
FT VAR_SEQ 563
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_019866"
FT VAR_SEQ 932
FT /note="K -> KQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037653"
FT CONFLICT 120
FT /note="Q -> H (in Ref. 4; AAL89948)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..493
FT /note="Missing (in Ref. 4; AAL89948)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="G -> S (in Ref. 1; AAA85120)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="I -> F (in Ref. 1; AAA85120 and 4; AAL89948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 104824 MW; 7B084A0AEC098297 CRC64;
MAMKKLYAKT SFTSKKPSSA ANSTPILAYH QQQHQQPGNG ICEFQVVAPG HSGELMIRRS
QSMHHKMSPP VGGLGSKSEY YSIEELQELD LLDYRHPMYH HYQQQELRQR YHEHEQLVLQ
LPKATSPKAG PIYEAPQRSQ QQQDQMLYVP TAAQRDSSSS AAATSIASSS TLTSSPSPSS
SSSLIFSTLR KCVSPSNPSV NPNQPSKTQP SKLGCSMSFS IRTTTATAAT AAAANAATAT
LSTQQQQQQA QQQHKQHLYS NIHHYLIRQQ QQKQHYTLQR RHNSVKDKFI GGITTIFAEQ
SIIGARASVM VYDDNQKKWV PSGSSSGLSK VQIYHHQQNN TFRVVGRKLQ DHEVVINCSI
LKGLKYNQAT ATFHQWRDSK FVYGLNFSSQ NDAENFARAM MHALEVLSGR VANNPGGPPT
NGNGYEEDMG YRTMTSEDAA ILRQNNSIGG HVTPSAQTPT SQTNQNNIPQ SPPTPQGHHR
TSSAPPAPQP QQQQQQQQAQ QMGQPGSHYG PTGNGPTSNG LPQQVNSQIP PAPQQQPQQQ
QFQQQQQQQQ YQQMVQAGYA PSQQYQQPHY VLSNSNPNLT VHQYPTQQAQ QQPPQAPQPP
LQNGGMYMVG HGHLPSSASA NSVVYASQQQ MLPQAHPQAP QAPTMPGPGY GGPPVPPPQQ
QAENPYGQVP MPPPMNPSQQ QQPGQVPLNR MSSQGGPGGP PAPAPPPPPP SFGGAAGGGP
PPPAPPQMFN GAPPPPAMGG GPPPAPPAPP AMGGGPPPAP GGPGAPPPPP PPPGLGGAPK
KEDPQADLMG SLASQLQQIK LKKNKVTTSA PENSGSSTSS GGSGNYGTIG RSSNGMASMM
DEMAKTLARR RAQAEKKDPD PEAEVKKRPW EKSNTLPHKL SGGAGSGSAG SGHEGANGNS
GGAGSNTTNS GGESPRPMRK RFGSASEETI LKVNGDGLSL ALSNGDLDTL KAEIVREMRL
EIQKVKNEII DAIKSEFNRR
