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 24-JAN-2024, entry version 164. 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 Head RC {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}. 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; 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; 7227-FBpp0080884; -. 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 AGR; FB:FBgn0003475; -. 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 OrthoDB; 2900844at2759; -. 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 cell types or tissues. DR ExpressionAtlas; Q9U1K1; baseline and differential. 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 CDD; cd15748; FYVE_SPIR; 1. DR CDD; cd22068; WH2_DmSpire_r3-like; 1. DR CDD; cd22069; WH2_DmSpire_r4; 1. DR CDD; cd22078; WH2_Spire1_r2-like; 1. DR CDD; cd22065; WH2_Spire_1-2_r1; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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:SF3; PROTEIN SPIRE; 1. DR PANTHER; PTHR21345; SPIRE; 1. DR Pfam; PF16474; KIND; 2. DR SMART; SM00750; KIND; 1. DR SMART; SM00246; WH2; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS51377; KIND; 1. DR PROSITE; PS51082; WH2; 2. DR Genevisible; Q9U1K1; DM. 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 //