CADF_DROME
ID CADF_DROME Reviewed; 148 AA.
AC P45594; C6SV25; Q9W1C4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cofilin/actin-depolymerizing factor homolog;
DE AltName: Full=Protein D61;
DE AltName: Full=Protein twinstar {ECO:0000303|PubMed:8522587};
GN Name=tsr {ECO:0000303|PubMed:8522587, ECO:0000312|FlyBase:FBgn0011726};
GN Synonyms=Cadf; ORFNames=CG4254 {ECO:0000312|FlyBase:FBgn0011726};
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].
RX PubMed=8183953; DOI=10.1073/pnas.91.10.4589;
RA Edwards K.A., Montague R.A., Shepard S., Edgar B.A., Erikson R.L.,
RA Kiehart D.P.;
RT "Identification of Drosophila cytoskeletal proteins by induction of
RT abnormal cell shape in fission yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4589-4593(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=Oregon-R;
RX PubMed=8522587; DOI=10.1083/jcb.131.5.1243;
RA Gunsalus K.C., Bonaccorsi S., Williams E., Verni F., Gatti M.,
RA Goldberg M.L.;
RT "Mutations in twinstar, a Drosophila gene encoding a cofilin/ADF homologue,
RT result in defects in centrosome migration and cytokinesis.";
RL J. Cell Biol. 131:1243-1259(1995).
RN [3]
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 [4]
RP GENOME REANNOTATION.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-3.
RX PubMed=11027607; DOI=10.1006/bbrc.2000.3599;
RA Ohashi K., Hosoya T., Takahashi K., Hing H., Mizuno K.;
RT "A Drosophila homolog of LIM-kinase phosphorylates cofilin and induces
RT actin cytoskeletal reorganization.";
RL Biochem. Biophys. Res. Commun. 276:1178-1185(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11175754; DOI=10.1038/35055120;
RA Chen J., Godt D., Gunsalus K., Kiss I., Goldberg M., Laski F.A.;
RT "Cofilin/ADF is required for cell motility during Drosophila ovary
RT development and oogenesis.";
RL Nat. Cell Biol. 3:204-209(2001).
RN [8]
RP DEPHOSPHORYLATION.
RX PubMed=11832213; DOI=10.1016/s0092-8674(01)00638-9;
RA Niwa R., Nagata-Ohashi K., Takeichi M., Mizuno K., Uemura T.;
RT "Control of actin reorganization by Slingshot, a family of phosphatases
RT that dephosphorylate ADF/cofilin.";
RL Cell 108:233-246(2002).
RN [9]
RP FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-3.
RX PubMed=15572110; DOI=10.1016/j.neuron.2004.11.014;
RA Ng J., Luo L.;
RT "Rho GTPases regulate axon growth through convergent and divergent
RT signaling pathways.";
RL Neuron 44:779-793(2004).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF VAL-27 AND 139-GLU--ARG-143.
RX PubMed=16571634; DOI=10.1242/dev.02320;
RA Blair A., Tomlinson A., Pham H., Gunsalus K.C., Goldberg M.L., Laski F.A.;
RT "Twinstar, the Drosophila homolog of cofilin/ADF, is required for planar
RT cell polarity patterning.";
RL Development 133:1789-1797(2006).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18423434; DOI=10.1016/j.ydbio.2008.03.006;
RA Pham H., Yu H., Laski F.A.;
RT "Cofilin/ADF is required for retinal elongation and morphogenesis of the
RT Drosophila rhabdomere.";
RL Dev. Biol. 318:82-91(2008).
RN [12]
RP FUNCTION.
RX PubMed=20026655; DOI=10.1083/jcb.200908040;
RA von Blume J., Duran J.M., Forlanelli E., Alleaume A.M., Egorov M.,
RA Polishchuk R., Molina H., Malhotra V.;
RT "Actin remodeling by ADF/cofilin is required for cargo sorting at the
RT trans-Golgi network.";
RL J. Cell Biol. 187:1055-1069(2009).
RN [13]
RP FUNCTION.
RX PubMed=21205790; DOI=10.1242/dev.046870;
RA Zhang L., Luo J., Wan P., Wu J., Laski F., Chen J.;
RT "Regulation of cofilin phosphorylation and asymmetry in collective cell
RT migration during morphogenesis.";
RL Development 138:455-464(2011).
RN [14]
RP PHOSPHORYLATION.
RX PubMed=22912811; DOI=10.1371/journal.pone.0043145;
RA Siudeja K., Grzeschik N.A., Rana A., de Jong J., Sibon O.C.;
RT "Cofilin/Twinstar phosphorylation levels increase in response to impaired
RT coenzyme a metabolism.";
RL PLoS ONE 7:E43145-E43145(2012).
RN [15]
RP FUNCTION.
RX PubMed=22323606; DOI=10.1073/pnas.1118880109;
RA Dopie J., Skarp K.P., Rajakyla E.K., Tanhuanpaa K., Vartiainen M.K.;
RT "Active maintenance of nuclear actin by importin 9 supports
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E544-E552(2012).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27041568; DOI=10.1038/onc.2016.46;
RA Ko C., Kim Y.G., Le T.P., Choi K.W.;
RT "Twinstar/cofilin is required for regulation of epithelial integrity and
RT tissue growth in Drosophila.";
RL Oncogene 35:5144-5154(2016).
RN [17]
RP STRUCTURE BY NMR.
RA Shukla V.K., Maheshwari D., Jain A., Tripathi S., Kumar D., Arora A.;
RT "Solution structure and dynamics of Twinstar from Drosophila
RT melanogaster.";
RL Submitted (SEP-2014) to the PDB data bank.
CC -!- FUNCTION: Exhibits F-actin depolymerizing activity and regulates actin
CC cytoskeleton dynamics (PubMed:21205790). Required for cytokinesis in
CC both mitotic and meiotic cells and for aster migration and separation
CC (PubMed:8522587). Promotes cell motility during ovary development and
CC oogenesis (PubMed:11175754). During larval development, required for
CC the cell rearrangement needed for formation of terminal filaments which
CC are stacks of somatic cells that are important for the initiation of
CC ovarioles (PubMed:11175754). Also required for border cell migration
CC during oogenesis (PubMed:11175754). During border cell migration,
CC required for actin turnover and lamellipodial protrusion
CC (PubMed:21205790). Required for the establishment of planar cell
CC polarity (PCP) where cells adopt a uniform orientation within the plane
CC of an epithelium (PubMed:16571634). During establishment of PCP,
CC required for the redistribution of the PCP core proteins fz and
CC stan/fmi to the proximodistal cell boundary (PubMed:16571634). During
CC pupal development, required for elongation of the retinal cell body and
CC for rhabdomere morphogenesis (PubMed:18423434). Required for mushroom
CC body neuroblast proliferation and axon growth (PubMed:15572110). Plays
CC a role in the positive regulation of protein secretion
CC (PubMed:20026655). Plays a role in the regulation of nuclear
CC localization of actin (PubMed:22323606). Required for the maintenance
CC of epithelial integrity by controlling cell junctions and is also
CC necessary for cell survival and tissue growth through regulation of JNK
CC and yki signaling (PubMed:27041568). {ECO:0000269|PubMed:11175754,
CC ECO:0000269|PubMed:15572110, ECO:0000269|PubMed:16571634,
CC ECO:0000269|PubMed:18423434, ECO:0000269|PubMed:20026655,
CC ECO:0000269|PubMed:21205790, ECO:0000269|PubMed:22323606,
CC ECO:0000269|PubMed:27041568, ECO:0000269|PubMed:8522587}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC matrix {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all stages of development and
CC peaks in late larval and pupal stages. Expressed in both male and
CC female adults. {ECO:0000269|PubMed:8522587}.
CC -!- PTM: Phosphorylated in vitro by protein kinase LIMK1 (PubMed:20026655).
CC Phosphorylation is required for inactivation of tsr and for cell
CC proliferation and axon growth (PubMed:15572110). Phosphorylation is
CC negatively regulated by the panthothenate kinase fbl which catalyzes
CC the first step in the conversion of panthothenic acid to coenzyme A
CC (PubMed:22912811). {ECO:0000269|PubMed:11027607,
CC ECO:0000269|PubMed:15572110, ECO:0000269|PubMed:22912811}.
CC -!- PTM: Dephosphorylated by protein phosphatase ssh which activates tsr.
CC {ECO:0000269|PubMed:11832213, ECO:0000269|PubMed:15572110}.
CC -!- DISRUPTION PHENOTYPE: Late larval or pupal lethality with mutants
CC showing defects in cytokinesis in both mitotic and meiotic cells,
CC abnormal accumulation of F-actin in mature primary spermatocytes, and
CC defective aster migration where the asters remain in close proximity to
CC each other rather than separating from each other and migrating around
CC the periphery of the nuclear envelope as in the wild type
CC (PubMed:8522587). Failure of terminal filament formation in the ovary
CC at the third larval instar at 25 degrees Celsius but formation occurs
CC at 18 degrees Celsius (PubMed:11175754). Significantly thinner retina
CC than controls, significantly increased F-actin levels in pupal eye
CC disks and defective rhabdomere morphogenesis (PubMed:18423434).
CC Defective mushroom body neuroblast proliferation with newly hatched
CC larvae containing significantly fewer neurons than controls and severe
CC axon growth defects with mutants failing to extend axons beyond the
CC peduncle (PubMed:15572110). RNAi-mediated knockdown in the wing results
CC in increased F-actin levels, altered subcellular location of the
CC transcriptional coactivator yki, strong expression of the yki target
CC genes wg and ex, cell extrusion from the basement membrane, reduced
CC levels of the junction proteins dlg1, arm and shg, up-regulation of
CC Rho1, apoptosis and JNK signaling (PubMed:27041568).
CC {ECO:0000269|PubMed:11175754, ECO:0000269|PubMed:15572110,
CC ECO:0000269|PubMed:18423434, ECO:0000269|PubMed:27041568,
CC ECO:0000269|PubMed:8522587}.
CC -!- MISCELLANEOUS: The name 'twinstar' derives from the characteristic
CC aberrant arrangement of asters seen in mutants.
CC {ECO:0000303|PubMed:8522587}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; U08217; AAA19856.1; -; mRNA.
DR EMBL; U24490; AAC46962.1; -; mRNA.
DR EMBL; U24676; AAC46963.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47146.1; -; Genomic_DNA.
DR EMBL; BT089017; ACT98664.1; -; mRNA.
DR PIR; A57569; A57569.
DR RefSeq; NP_477034.1; NM_057686.4.
DR PDB; 2MV2; NMR; -; A=1-148.
DR PDBsum; 2MV2; -.
DR AlphaFoldDB; P45594; -.
DR BMRB; P45594; -.
DR SMR; P45594; -.
DR BioGRID; 63422; 45.
DR DIP; DIP-20149N; -.
DR IntAct; P45594; 37.
DR STRING; 7227.FBpp0072097; -.
DR iPTMnet; P45594; -.
DR PaxDb; P45594; -.
DR PRIDE; P45594; -.
DR DNASU; 37841; -.
DR EnsemblMetazoa; FBtr0072188; FBpp0072097; FBgn0011726.
DR GeneID; 37841; -.
DR KEGG; dme:Dmel_CG4254; -.
DR CTD; 37841; -.
DR FlyBase; FBgn0011726; tsr.
DR VEuPathDB; VectorBase:FBgn0011726; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_3_1_1; -.
DR InParanoid; P45594; -.
DR OMA; ITFYSWS; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; P45594; -.
DR SignaLink; P45594; -.
DR BioGRID-ORCS; 37841; 0 hits in 3 CRISPR screens.
DR ChiTaRS; tsr; fly.
DR GenomeRNAi; 37841; -.
DR PRO; PR:P45594; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0011726; Expressed in eye disc (Drosophila) and 25 other tissues.
DR ExpressionAtlas; P45594; baseline and differential.
DR Genevisible; P45594; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IMP:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IMP:UniProtKB.
DR GO; GO:0030043; P:actin filament fragmentation; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030041; P:actin filament polymerization; IMP:FlyBase.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; TAS:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
DR GO; GO:0051299; P:centrosome separation; IMP:UniProtKB.
DR GO; GO:0048749; P:compound eye development; IGI:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0010669; P:epithelial structure maintenance; IMP:UniProtKB.
DR GO; GO:0001737; P:establishment of imaginal disc-derived wing hair orientation; IMP:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:FlyBase.
DR GO; GO:0008585; P:female gonad development; IMP:FlyBase.
DR GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0033206; P:meiotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0016319; P:mushroom body development; IMP:FlyBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..148
FT /note="Cofilin/actin-depolymerizing factor homolog"
FT /id="PRO_0000214916"
FT DOMAIN 4..143
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOTIF 19..23
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MUTAGEN 3
FT /note="S->A: Abolishes in vitro phosphorylation by LIMK1.
FT Partial rescue of both the defective neuroblast
FT proliferation and defective axon growth seen in null
FT mutants."
FT /evidence="ECO:0000269|PubMed:11027607,
FT ECO:0000269|PubMed:15572110"
FT MUTAGEN 3
FT /note="S->E: No rescue of the defective neuroblast
FT proliferation seen in null mutants but partial rescue of
FT the defective axon growth."
FT /evidence="ECO:0000269|PubMed:15572110"
FT MUTAGEN 27
FT /note="V->Q: Defective distal orientation of wing hairs and
FT incorrect localization of the planar cell polarity proteins
FT fz and stan/fmi; when associated with 139-AAALA-143."
FT /evidence="ECO:0000269|PubMed:16571634"
FT MUTAGEN 139..143
FT /note="EEKLR->AAALA: Defective distal orientation of wing
FT hairs and incorrect localization of the planar cell
FT polarity proteins fz and stan/fmi; when associated with Q-
FT 27."
FT /evidence="ECO:0000269|PubMed:16571634"
FT HELIX 9..20
FT /evidence="ECO:0007829|PDB:2MV2"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2MV2"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2MV2"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2MV2"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:2MV2"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2MV2"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:2MV2"
FT STRAND 80..94
FT /evidence="ECO:0007829|PDB:2MV2"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:2MV2"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2MV2"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2MV2"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2MV2"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:2MV2"
SQ SEQUENCE 148 AA; 17153 MW; 24F7216033859620 CRC64;
MASGVTVSDV CKTTYEEIKK DKKHRYVIFY IRDEKQIDVE TVADRNAEYD QFLEDIQKCG
PGECRYGLFD FEYMHQCQGT SESSKKQKLF LMSWCPDTAK VKKKMLYSSS FDALKKSLVG
VQKYIQATDL SEASREAVEE KLRATDRQ
