SPIR_DROME
ID SPIR_DROME Reviewed; 1020 AA.
AC Q9U1K1; Q5U0Z8; Q8INV3; Q8INV4; Q8INV5; Q8SXP3; Q8T8P8; Q9U4F0; Q9U4F1;
AC Q9VIN3; Q9VIN4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein spire;
GN Name=spir {ECO:0000312|FlyBase:FBgn0003475};
GN Synonyms=p150-Spir {ECO:0000312|EMBL:CAB62901.1}; ORFNames=CG10076;
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] {ECO:0000305, ECO:0000312|EMBL:AAF23615.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, INTERACTION WITH
RP RHO1; RAC1 AND CDC42, DEVELOPMENTAL STAGE, ACTIN-BINDING, AND DISRUPTION
RP PHENOTYPE.
RC TISSUE=Ovary {ECO:0000269|PubMed:10556052};
RX PubMed=10556052; DOI=10.1242/dev.126.23.5267;
RA Wellington A., Emmons S., James B., Calley J., Grover M., Tolias P.,
RA Manseau L.;
RT "Spire contains actin binding domains and is related to ascidian posterior
RT end mark-5.";
RL Development 126:5267-5274(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB62901.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH BSK,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC TISSUE=Embryo {ECO:0000269|PubMed:10744979};
RX PubMed=10744979; DOI=10.1016/s0960-9822(00)00388-2;
RA Otto I.M., Raabe T., Rennefahrt U.E.E., Bork P., Rapp U.R., Kerkhoff E.;
RT "The p150-Spir protein provides a link between c-Jun N-terminal kinase
RT function and actin reorganization.";
RL Curr. Biol. 10:345-348(2000).
RN [3] {ECO:0000312|EMBL:AAF53884.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF53884.2}
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAL90241.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D), AND RNA EDITING
RP OF POSITION 734.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC Head {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 [6] {ECO:0000305, ECO:0000312|EMBL:AAV36979.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1020 (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAV36979.1}; 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=15674283; DOI=10.1038/nature03241;
RA Quinlan M.E., Heuser J.E., Kerkhoff E., Mullins R.D.;
RT "Drosophila Spire is an actin nucleation factor.";
RL Nature 433:382-388(2005).
RN [8] {ECO:0000305}
RP RNA EDITING OF POSITION 734.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
RN [9]
RP INTERACTION WITH WASH.
RX PubMed=19633175; DOI=10.1242/dev.035246;
RA Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E.,
RA Parkhurst S.M.;
RT "Wash functions downstream of Rho and links linear and branched actin
RT nucleation factors.";
RL Development 136:2849-2860(2009).
RN [10]
RP FUNCTION, INTERACTION WITH CAPU, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-232.
RX PubMed=21730168; DOI=10.1073/pnas.1105703108;
RA Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W.,
RA Quinlan M.E., Eck M.J.;
RT "Structure and function of the interacting domains of Spire and Fmn-family
RT formins.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 448-485 IN COMPLEX WITH ACTIN, AND
RP FUNCTION.
RX PubMed=20538977; DOI=10.1073/pnas.1005347107;
RA Ducka A.M., Joel P., Popowicz G.M., Trybus K.M., Schleicher M.,
RA Noegel A.A., Huber R., Holak T.A., Sitar T.;
RT "Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2
RT (WH2) domains of Spire and the implication for filament nucleation.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11757-11762(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 428-485 IN COMPLEX WITH ACTIN.
RX PubMed=22334675; DOI=10.1074/jbc.m111.317792;
RA Chen C.K., Sawaya M.R., Phillips M.L., Reisler E., Quinlan M.E.;
RT "Multiple forms of Spire-actin complexes and their functional
RT consequences.";
RL J. Biol. Chem. 287:10684-10692(2012).
CC -!- FUNCTION: Acts as an actin nucleation factor, remains associated with
CC the slow-growing pointed end of the new filament. Promotes dissociation
CC of capu from the barbed end of actin filaments. Involved in
CC intracellular vesicle transport along actin fibers, providing a novel
CC link between actin cytoskeleton dynamics and intracellular transport.
CC Required for localization of determinants within the developing oocyte
CC to the posterior pole and to the dorsal anterior corner. Links Rho
CC family signaling and Jnk function to the actin cytoskeleton.
CC {ECO:0000269|PubMed:10556052, ECO:0000269|PubMed:10744979,
CC ECO:0000269|PubMed:15674283, ECO:0000269|PubMed:20538977,
CC ECO:0000269|PubMed:21730168}.
CC -!- SUBUNIT: Interacts with bsk, Rho1, Rac1, Cdc42 and wash. Interacts with
CC capu. {ECO:0000269|PubMed:10556052, ECO:0000269|PubMed:10744979,
CC ECO:0000269|PubMed:19633175, ECO:0000269|PubMed:20538977,
CC ECO:0000269|PubMed:21730168, ECO:0000269|PubMed:22334675}.
CC -!- INTERACTION:
CC Q9U1K1-1; P10987: Act5C; NbExp=6; IntAct=EBI-3431623, EBI-130188;
CC Q9U1K1-1; Q95RI5: fax; NbExp=2; IntAct=EBI-3431623, EBI-147695;
CC Q9U1K1-1; P68135: ACTA1; Xeno; NbExp=6; IntAct=EBI-3431623, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10744979}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10744979}. Cell membrane
CC {ECO:0000269|PubMed:21730168}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21730168}; Cytoplasmic side
CC {ECO:0000269|PubMed:21730168}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:21730168}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21730168}; Cytoplasmic side
CC {ECO:0000269|PubMed:21730168}. Note=Punctate spots in perinuclear
CC region and cytoplasm. {ECO:0000269|PubMed:10744979}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A {ECO:0000269|PubMed:10744979};
CC IsoId=Q9U1K1-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:10556052}; Synonyms=Long
CC {ECO:0000269|PubMed:10556052};
CC IsoId=Q9U1K1-2; Sequence=VSP_052602;
CC Name=C {ECO:0000269|PubMed:10731132};
CC IsoId=Q9U1K1-3; Sequence=VSP_052599, VSP_052600;
CC Name=D {ECO:0000269|PubMed:10556052}; Synonyms=Short
CC {ECO:0000269|PubMed:10556052};
CC IsoId=Q9U1K1-4; Sequence=VSP_052601, VSP_052603, VSP_052604;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:10556052}.
CC -!- DOMAIN: Binds to actin monomers via the WH2 domain.
CC {ECO:0000269|PubMed:10556052}.
CC -!- DOMAIN: The Spir-box targets binding to intracellular membrane
CC structures. {ECO:0000250|UniProtKB:Q08AE8}.
CC -!- PTM: Phosphorylated by Jnk kinase (bsk). {ECO:0000269|PubMed:10744979}.
CC -!- RNA EDITING: Modified_positions=734 {ECO:0000269|PubMed:12537569,
CC ECO:0000269|PubMed:17018572}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- DISRUPTION PHENOTYPE: Flies display premature microtubule-dependent
CC cytoplasmic streaming; failure in the orientation of microtubule plus
CC ends towards the posterior pole. {ECO:0000269|PubMed:10556052}.
CC -!- SIMILARITY: Belongs to the spire family. {ECO:0000305}.
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DR EMBL; AF184975; AAF23615.1; -; mRNA.
DR EMBL; AF184976; AAF23616.1; -; mRNA.
DR EMBL; AJ238876; CAB62901.1; -; mRNA.
DR EMBL; AE014134; AAF53884.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN11070.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11071.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11072.2; -; Genomic_DNA.
DR EMBL; AY075586; AAL68390.1; -; mRNA.
DR EMBL; AY089503; AAL90241.1; -; mRNA.
DR EMBL; BT016094; AAV36979.1; -; mRNA.
DR RefSeq; NP_001246102.1; NM_001259173.1.
DR RefSeq; NP_001286100.1; NM_001299171.1.
DR RefSeq; NP_524854.2; NM_080115.3. [Q9U1K1-2]
DR RefSeq; NP_724254.1; NM_165323.3. [Q9U1K1-1]
DR RefSeq; NP_724255.1; NM_165324.2. [Q9U1K1-4]
DR RefSeq; NP_724256.2; NM_165325.3. [Q9U1K1-3]
DR PDB; 3MMV; X-ray; 2.80 A; X=429-447.
DR PDB; 3MN5; X-ray; 1.50 A; S=448-485.
DR PDB; 3MN6; X-ray; 2.00 A; X/Y/Z=397-415.
DR PDB; 3MN7; X-ray; 2.00 A; S=441-479.
DR PDB; 3MN9; X-ray; 2.00 A; X=372-390.
DR PDB; 3UE5; X-ray; 2.76 A; B=428-485.
DR PDB; 4EFH; X-ray; 2.48 A; B=428-485.
DR PDBsum; 3MMV; -.
DR PDBsum; 3MN5; -.
DR PDBsum; 3MN6; -.
DR PDBsum; 3MN7; -.
DR PDBsum; 3MN9; -.
DR PDBsum; 3UE5; -.
DR PDBsum; 4EFH; -.
DR AlphaFoldDB; Q9U1K1; -.
DR SMR; Q9U1K1; -.
DR BioGRID; 69994; 20.
DR DIP; DIP-17301N; -.
DR ELM; Q9U1K1; -.
DR IntAct; Q9U1K1; 13.
DR STRING; 7227.FBpp0080884; -.
DR PaxDb; Q9U1K1; -.
DR DNASU; 45931; -.
DR EnsemblMetazoa; FBtr0081352; FBpp0080884; FBgn0003475. [Q9U1K1-1]
DR EnsemblMetazoa; FBtr0081353; FBpp0080885; FBgn0003475. [Q9U1K1-2]
DR EnsemblMetazoa; FBtr0081354; FBpp0080886; FBgn0003475. [Q9U1K1-4]
DR EnsemblMetazoa; FBtr0081355; FBpp0080887; FBgn0003475. [Q9U1K1-3]
DR GeneID; 45931; -.
DR KEGG; dme:Dmel_CG10076; -.
DR UCSC; CG10076-RA; d. melanogaster. [Q9U1K1-1]
DR CTD; 45931; -.
DR FlyBase; FBgn0003475; spir.
DR VEuPathDB; VectorBase:FBgn0003475; -.
DR eggNOG; ENOG502QQPN; Eukaryota.
DR GeneTree; ENSGT00390000003058; -.
DR InParanoid; Q9U1K1; -.
DR OMA; GPPRMCT; -.
DR PhylomeDB; Q9U1K1; -.
DR SignaLink; Q9U1K1; -.
DR BioGRID-ORCS; 45931; 0 hits in 3 CRISPR screens.
DR ChiTaRS; spir; fly.
DR EvolutionaryTrace; Q9U1K1; -.
DR GenomeRNAi; 45931; -.
DR PRO; PR:Q9U1K1; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003475; Expressed in second segment of antenna (Drosophila) and 51 other tissues.
DR ExpressionAtlas; Q9U1K1; baseline and differential.
DR Genevisible; Q9U1K1; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; TAS:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IMP:FlyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:FlyBase.
DR GO; GO:0051639; P:actin filament network formation; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0030029; P:actin filament-based process; IDA:FlyBase.
DR GO; GO:0045010; P:actin nucleation; IDA:FlyBase.
DR GO; GO:0007304; P:chorion-containing eggshell formation; HMP:FlyBase.
DR GO; GO:0036089; P:cleavage furrow formation; IBA:GO_Central.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IBA:GO_Central.
DR GO; GO:0048193; P:Golgi vesicle transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0030717; P:oocyte karyosome formation; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0040038; P:polar body extrusion after meiotic divisions; IBA:GO_Central.
DR GO; GO:0007315; P:pole plasm assembly; IMP:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; TAS:FlyBase.
DR GO; GO:0007316; P:pole plasm RNA localization; IMP:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:FlyBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011019; KIND_dom.
DR InterPro; IPR029901; Spire.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21345; PTHR21345; 1.
DR Pfam; PF16474; KIND; 2.
DR SMART; SM00750; KIND; 1.
DR SMART; SM00246; WH2; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51377; KIND; 1.
DR PROSITE; PS51082; WH2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell membrane;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Developmental protein;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW RNA editing; Transport.
FT CHAIN 1..1020
FT /note="Protein spire"
FT /id="PRO_0000309573"
FT DOMAIN 90..327
FT /note="KIND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00709"
FT DOMAIN 399..417
FT /note="WH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT DOMAIN 463..480
FT /note="WH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..725
FT /note="Spir-box"
FT REGION 799..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 2..96
FT /note="TEHQAEEQADTPPTKVKATPTPTPSGKFKDAKEDAFLSTSPDSANGDAQHKL
FT PADQLAMSSSAHPQQAGQARPLILQAFHRCSSPEQCVTLHDIL -> EARPAKRSTAAS
FT VFRSHHMPRESDLVDIGSDASLYCGSDGESSQAQSTSTSTPNPQTSSDQDLDQPQPTPR
FT AAPRASASNNPPTPKPRQAIRSSK (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052599"
FT VAR_SEQ 97..491
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052600"
FT VAR_SEQ 338
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10556052,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052601"
FT VAR_SEQ 585..614
FT /note="MEPAKQVPPPEEPSFTKDEYHKFYDTALES -> T (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10556052, ECO:0000303|Ref.6"
FT /id="VSP_052602"
FT VAR_SEQ 585..586
FT /note="ME -> SI (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10556052,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052603"
FT VAR_SEQ 587..1020
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10556052,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_052604"
FT VARIANT 734
FT /note="K -> R (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
FT MUTAGEN 232
FT /note="Y->K: Abolishes interaction with capu."
FT /evidence="ECO:0000269|PubMed:21730168"
FT CONFLICT 53
FT /note="L -> M (in Ref. 1; AAF23615/AAF23616)"
FT /evidence="ECO:0000305"
FT CONFLICT 885
FT /note="V -> A (in Ref. 1; AAF23615)"
FT /evidence="ECO:0000305"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:3MN5"
SQ SEQUENCE 1020 AA; 114867 MW; 010CD024F9ABC078 CRC64;
MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ HKLPADQLAM
SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK APLSEDQAWA LIHQFAGLYH
QVAVQAHTCA ADYEAALPTG FELHFHRDGS VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV
DQPDHSASSS GDSSVINRAF DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP
EDEECQVSQE LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC
RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNEAG AEKLIKASES SATTQQELAK
LGFNDWARFW VQVIDELRRG VRLKKSNHER TPIEYELTPY EILMGDIRAK KYQLRKVMVN
GDIPPRVKKD AHAMILEFIR SRPPLKKASD RQLGPPRMCE PSPREQLMES IRKGKELKQI
TPPEAPTLRE RVLPSANSTL SRSRQRLIKV DFSKFQDDDL FYDENSISSS HSTAATHQHH
PHFAEMHRCS QPKMPPYPFG GYMVPSQARQ DCRETASLMR PRRTMEPAKQ VPPPEEPSFT
KDEYHKFYDT ALESYDLATQ CESRRASLRR HTIVGCQSNL DETHSMPPTR PESRQSDDVS
KETPKRSPAE QTHPSDEGSS TSSLGPWNKS FMDKQTWMER GDDRLSVTLA EIVHIRSVMT
KAELEGLPMD VRVKEDVEKR RVCFLCLRTR FSFFGPWGIQ CKLCQRTVCA KCYTKMRIPS
EHFRNVPLVL ISPSLLSSPA SSSTPSPSHH AQQAHSSSTG NIMDDQFPKS LIERLLRSES
DRKTRSTVGS APSSPKHQRS NMSTPGISVG PGASSSSAAA TGQAVEALHD QATMSSSYSA
AMRPSGVHQQ QKQHYNNAMS RSMEGPRSLP VHSPAYRPLS NNSTLERKSR FSRGFNLFSS
GSHLAQTQEQ KENLRGEQVT VCNDCQGLVN EITSSVKQKR SSARNRTIQN LTLDLTPVWK
