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Cofilin/actin-depolymerizing factor homolog (Protein D61) (Protein twinstar)

 CADF_DROME              Reviewed;         148 AA.
P45594; C6SV25; Q9W1C4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
27-SEP-2017, entry version 145.
RecName: Full=Cofilin/actin-depolymerizing factor homolog;
AltName: Full=Protein D61;
AltName: Full=Protein twinstar {ECO:0000303|PubMed:8522587};
Name=tsr {ECO:0000303|PubMed:8522587,
ECO:0000312|FlyBase:FBgn0011726}; Synonyms=Cadf;
ORFNames=CG4254 {ECO:0000312|FlyBase:FBgn0011726};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8183953; DOI=10.1073/pnas.91.10.4589;
Edwards K.A., Montague R.A., Shepard S., Edgar B.A., Erikson R.L.,
Kiehart D.P.;
"Identification of Drosophila cytoskeletal proteins by induction of
abnormal cell shape in fission yeast.";
Proc. Natl. Acad. Sci. U.S.A. 91:4589-4593(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL
STAGE, AND DISRUPTION PHENOTYPE.
STRAIN=Oregon-R;
PubMed=8522587; DOI=10.1083/jcb.131.5.1243;
Gunsalus K.C., Bonaccorsi S., Williams E., Verni F., Gatti M.,
Goldberg M.L.;
"Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF
homologue, result in defects in centrosome migration and
cytokinesis.";
J. Cell Biol. 131:1243-1259(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
Celniker S.E.;
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
[6]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-3.
PubMed=11027607; DOI=10.1006/bbrc.2000.3599;
Ohashi K., Hosoya T., Takahashi K., Hing H., Mizuno K.;
"A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces
actin cytoskeletal reorganization.";
Biochem. Biophys. Res. Commun. 276:1178-1185(2000).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11175754; DOI=10.1038/35055120;
Chen J., Godt D., Gunsalus K., Kiss I., Goldberg M., Laski F.A.;
"Cofilin/ADF is required for cell motility during Drosophila ovary
development and oogenesis.";
Nat. Cell Biol. 3:204-209(2001).
[8]
DEPHOSPHORYLATION.
PubMed=11832213; DOI=10.1016/S0092-8674(01)00638-9;
Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.;
"Control of actin reorganization by Slingshot, a family of
phosphatases that dephosphorylate ADF/cofilin.";
Cell 108:233-246(2002).
[9]
FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION, DISRUPTION PHENOTYPE,
AND MUTAGENESIS OF SER-3.
PubMed=15572110; DOI=10.1016/j.neuron.2004.11.014;
Ng J., Luo L.;
"Rho GTPases regulate axon growth through convergent and divergent
signaling pathways.";
Neuron 44:779-793(2004).
[10]
FUNCTION, AND MUTAGENESIS OF VAL-27 AND 139-GLU--ARG-143.
PubMed=16571634; DOI=10.1242/dev.02320;
Blair A., Tomlinson A., Pham H., Gunsalus K.C., Goldberg M.L.,
Laski F.A.;
"Twinstar, the Drosophila homolog of cofilin/ADF, is required for
planar cell polarity patterning.";
Development 133:1789-1797(2006).
[11]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18423434; DOI=10.1016/j.ydbio.2008.03.006;
Pham H., Yu H., Laski F.A.;
"Cofilin/ADF is required for retinal elongation and morphogenesis of
the Drosophila rhabdomere.";
Dev. Biol. 318:82-91(2008).
[12]
FUNCTION.
PubMed=20026655; DOI=10.1083/jcb.200908040;
von Blume J., Duran J.M., Forlanelli E., Alleaume A.M., Egorov M.,
Polishchuk R., Molina H., Malhotra V.;
"Actin remodeling by ADF/cofilin is required for cargo sorting at the
trans-Golgi network.";
J. Cell Biol. 187:1055-1069(2009).
[13]
FUNCTION.
PubMed=21205790; DOI=10.1242/dev.046870;
Zhang L., Luo J., Wan P., Wu J., Laski F., Chen J.;
"Regulation of cofilin phosphorylation and asymmetry in collective
cell migration during morphogenesis.";
Development 138:455-464(2011).
[14]
PHOSPHORYLATION.
PubMed=22912811; DOI=10.1371/journal.pone.0043145;
Siudeja K., Grzeschik N.A., Rana A., de Jong J., Sibon O.C.;
"Cofilin/Twinstar phosphorylation levels increase in response to
impaired coenzyme a metabolism.";
PLoS ONE 7:E43145-E43145(2012).
[15]
FUNCTION.
PubMed=22323606; DOI=10.1073/pnas.1118880109;
Dopie J., Skarp K.P., Rajakyla E.K., Tanhuanpaa K., Vartiainen M.K.;
"Active maintenance of nuclear actin by importin 9 supports
transcription.";
Proc. Natl. Acad. Sci. U.S.A. 109:E544-E552(2012).
[16]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27041568; DOI=10.1038/onc.2016.46;
Ko C., Kim Y.G., Le T.P., Choi K.W.;
"Twinstar/cofilin is required for regulation of epithelial integrity
and tissue growth in Drosophila.";
Oncogene 35:5144-5154(2016).
[17]
STRUCTURE BY NMR.
Shukla V.K., Maheshwari D., Jain A., Tripathi S., Kumar D., Arora A.;
"Solution structure and dynamics of Twinstar from Drosophila
melanogaster.";
Submitted (SEP-2014) to the PDB data bank.
-!- FUNCTION: Exhibits F-actin depolymerizing activity and regulates
actin cytoskeleton dynamics (PubMed:21205790). Required for
cytokinesis in both mitotic and meiotic cells and for aster
migration and separation (PubMed:8522587). Promotes cell motility
during ovary development and oogenesis (PubMed:11175754). During
larval development, required for the cell rearrangement needed for
formation of terminal filaments which are stacks of somatic cells
that are important for the initiation of ovarioles
(PubMed:11175754). Also required for border cell migration during
oogenesis (PubMed:11175754). During border cell migration,
required for actin turnover and lamellipodial protrusion
(PubMed:21205790). Required for the establishment of planar cell
polarity (PCP) where cells adopt a uniform orientation within the
plane of an epithelium (PubMed:16571634). During establishment of
PCP, required for the redistribution of the PCP core proteins fz
and stan/fmi to the proximodistal cell boundary (PubMed:16571634).
During pupal development, required for elongation of the retinal
cell body and for rhabdomere morphogenesis (PubMed:18423434).
Required for mushroom body neuroblast proliferation and axon
growth (PubMed:15572110). Plays a role in the positive regulation
of protein secretion (PubMed:20026655). Plays a role in the
regulation of nuclear localization of actin (PubMed:22323606).
Required for the maintenance of epithelial integrity by
controlling cell junctions and is also necessary for cell survival
and tissue growth through regulation of JNK and yki signaling
(PubMed:27041568). {ECO:0000269|PubMed:11175754,
ECO:0000269|PubMed:15572110, ECO:0000269|PubMed:16571634,
ECO:0000269|PubMed:18423434, ECO:0000269|PubMed:20026655,
ECO:0000269|PubMed:21205790, ECO:0000269|PubMed:22323606,
ECO:0000269|PubMed:27041568, ECO:0000269|PubMed:8522587}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
Nucleus matrix {ECO:0000250}.
-!- DEVELOPMENTAL STAGE: Expressed during all stages of development
and peaks in late larval and pupal stages. Expressed in both male
and female adults. {ECO:0000269|PubMed:8522587}.
-!- PTM: Phosphorylated in vitro by protein kinase LIMK1
(PubMed:20026655). Phosphorylation is required for inactivation of
tsr and for cell proliferation and axon growth (PubMed:15572110).
Phosphorylation is negatively regulated by the panthothenate
kinase fbl which catalyzes the first step in the conversion of
panthothenic acid to coenzyme A (PubMed:22912811).
{ECO:0000269|PubMed:11027607, ECO:0000269|PubMed:15572110,
ECO:0000269|PubMed:22912811}.
-!- PTM: Dephosphorylated by protein phosphatase ssh which activates
tsr. {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:15572110}.
-!- DISRUPTION PHENOTYPE: Late larval or pupal lethality with mutants
showing defects in cytokinesis in both mitotic and meiotic cells,
abnormal accumulation of F-actin in mature primary spermatocytes,
and defective aster migration where the asters remain in close
proximity to each other rather than separating from each other and
migrating around the periphery of the nuclear envelope as in the
wild type (PubMed:8522587). Failure of terminal filament formation
in the ovary at the third larval instar at 25 degrees Celsius but
formation occurs at 18 degrees Celsius (PubMed:11175754).
Significantly thinner retina than controls, significantly
increased F-actin levels in pupal eye disks and defective
rhabdomere morphogenesis (PubMed:18423434). Defective mushroom
body neuroblast proliferation with newly hatched larvae containing
significantly fewer neurons than controls and severe axon growth
defects with mutants failing to extend axons beyond the peduncle
(PubMed:15572110). RNAi-mediated knockdown in the wing results in
increased F-actin levels, altered subcellular location of the
transcriptional coactivator yki, strong expression of the yki
target genes wg and ex, cell extrusion from the basement membrane,
reduced levels of the junction proteins dlg1, arm and shg, up-
regulation of Rho1, apoptosis and JNK signaling (PubMed:27041568).
{ECO:0000269|PubMed:11175754, ECO:0000269|PubMed:15572110,
ECO:0000269|PubMed:18423434, ECO:0000269|PubMed:27041568,
ECO:0000269|PubMed:8522587}.
-!- MISCELLANEOUS: The name 'twinstar' derives from the characteristic
aberrant arrangement of asters seen in mutants.
{ECO:0000303|PubMed:8522587}.
-!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
{ECO:0000305}.
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EMBL; U08217; AAA19856.1; -; mRNA.
EMBL; U24490; AAC46962.1; -; mRNA.
EMBL; U24676; AAC46963.1; -; Genomic_DNA.
EMBL; AE013599; AAF47146.1; -; Genomic_DNA.
EMBL; BT089017; ACT98664.1; -; mRNA.
PIR; A57569; A57569.
RefSeq; NP_477034.1; NM_057686.4.
UniGene; Dm.763; -.
PDB; 2MV2; NMR; -; A=1-148.
PDBsum; 2MV2; -.
ProteinModelPortal; P45594; -.
SMR; P45594; -.
BioGrid; 63422; 45.
DIP; DIP-20149N; -.
IntAct; P45594; 48.
MINT; MINT-901240; -.
STRING; 7227.FBpp0072097; -.
iPTMnet; P45594; -.
PaxDb; P45594; -.
PRIDE; P45594; -.
EnsemblMetazoa; FBtr0072188; FBpp0072097; FBgn0011726.
GeneID; 37841; -.
KEGG; dme:Dmel_CG4254; -.
CTD; 37841; -.
FlyBase; FBgn0011726; tsr.
eggNOG; KOG1735; Eukaryota.
eggNOG; ENOG41122P5; LUCA.
GeneTree; ENSGT00730000112650; -.
InParanoid; P45594; -.
KO; K05765; -.
OMA; QMLPEKD; -.
OrthoDB; EOG091G0TDH; -.
PhylomeDB; P45594; -.
ChiTaRS; tsr; fly.
GenomeRNAi; 37841; -.
PRO; PR:P45594; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0011726; -.
ExpressionAtlas; P45594; differential.
Genevisible; P45594; DM.
GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
GO; GO:0003779; F:actin binding; IMP:FlyBase.
GO; GO:0030042; P:actin filament depolymerization; IMP:UniProtKB.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0030041; P:actin filament polymerization; IMP:FlyBase.
GO; GO:0000915; P:actomyosin contractile ring assembly; TAS:FlyBase.
GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
GO; GO:0051299; P:centrosome separation; IMP:UniProtKB.
GO; GO:0048749; P:compound eye development; IGI:FlyBase.
GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
GO; GO:0010669; P:epithelial structure maintenance; IMP:UniProtKB.
GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
GO; GO:0008585; P:female gonad development; IMP:FlyBase.
GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
GO; GO:0033206; P:meiotic cytokinesis; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
CDD; cd11286; ADF_cofilin_like; 1.
Gene3D; 3.40.20.10; -; 1.
InterPro; IPR002108; ADF-H.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom.
InterPro; IPR017904; ADF/Cofilin.
PANTHER; PTHR11913; PTHR11913; 1.
Pfam; PF00241; Cofilin_ADF; 1.
SMART; SM00102; ADF; 1.
PROSITE; PS51263; ADF_H; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell cycle; Cell division;
Complete proteome; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 148 Cofilin/actin-depolymerizing factor
homolog.
/FTId=PRO_0000214916.
DOMAIN 4 143 ADF-H. {ECO:0000255|PROSITE-
ProRule:PRU00599}.
MOTIF 19 23 Nuclear localization signal.
{ECO:0000255}.
MUTAGEN 3 3 S->A: Abolishes in vitro phosphorylation
by LIMK1. Partial rescue of both the
defective neuroblast proliferation and
defective axon growth seen in null
mutants. {ECO:0000269|PubMed:11027607,
ECO:0000269|PubMed:15572110}.
MUTAGEN 3 3 S->E: No rescue of the defective
neuroblast proliferation seen in null
mutants but partial rescue of the
defective axon growth.
{ECO:0000269|PubMed:15572110}.
MUTAGEN 27 27 V->Q: Defective distal orientation of
wing hairs and incorrect localization of
the planar cell polarity proteins fz and
stan/fmi; when associated with 139-AAALA-
143. {ECO:0000269|PubMed:16571634}.
MUTAGEN 139 143 EEKLR->AAALA: Defective distal
orientation of wing hairs and incorrect
localization of the planar cell polarity
proteins fz and stan/fmi; when associated
with Q-27. {ECO:0000269|PubMed:16571634}.
HELIX 9 20 {ECO:0000244|PDB:2MV2}.
STRAND 26 32 {ECO:0000244|PDB:2MV2}.
TURN 33 35 {ECO:0000244|PDB:2MV2}.
STRAND 36 43 {ECO:0000244|PDB:2MV2}.
HELIX 49 59 {ECO:0000244|PDB:2MV2}.
STRAND 61 63 {ECO:0000244|PDB:2MV2}.
STRAND 65 77 {ECO:0000244|PDB:2MV2}.
STRAND 80 94 {ECO:0000244|PDB:2MV2}.
HELIX 101 113 {ECO:0000244|PDB:2MV2}.
HELIX 114 116 {ECO:0000244|PDB:2MV2}.
STRAND 122 127 {ECO:0000244|PDB:2MV2}.
TURN 130 132 {ECO:0000244|PDB:2MV2}.
HELIX 135 144 {ECO:0000244|PDB:2MV2}.
SEQUENCE 148 AA; 17153 MW; 24F7216033859620 CRC64;
MASGVTVSDV CKTTYEEIKK DKKHRYVIFY IRDEKQIDVE TVADRNAEYD QFLEDIQKCG
PGECRYGLFD FEYMHQCQGT SESSKKQKLF LMSWCPDTAK VKKKMLYSSS FDALKKSLVG
VQKYIQATDL SEASREAVEE KLRATDRQ


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