ADF9_ARATH
ID ADF9_ARATH Reviewed; 141 AA.
AC O49606;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Actin-depolymerizing factor 9;
DE Short=ADF-9;
DE Short=AtADF9;
GN Name=ADF9; OrderedLocusNames=At4g34970; ORFNames=M4E13.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-141.
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=16360805; DOI=10.1016/j.jplph.2005.01.015;
RA Feng Y., Liu Q., Xue Q.;
RT "Comparative study of rice and Arabidopsis actin-depolymerizing factors
RT gene families.";
RL J. Plant Physiol. 163:69-79(2006).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18830798; DOI=10.1007/s11103-008-9398-1;
RA Burgos-Rivera B., Ruzicka D.R., Deal R.B., McKinney E.C., King-Reid L.,
RA Meagher R.B.;
RT "ACTIN DEPOLYMERIZING FACTOR9 controls development and gene expression in
RT Arabidopsis.";
RL Plant Mol. Biol. 68:619-632(2008).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21570971; DOI=10.1016/j.febslet.2011.05.019;
RA Tholl S., Moreau F., Hoffmann C., Arumugam K., Dieterle M., Moes D.,
RA Neumann K., Steinmetz A., Thomas C.;
RT "Arabidopsis actin-depolymerizing factors (ADFs) 1 and 9 display antagonist
RT activities.";
RL FEBS Lett. 585:1821-1827(2011).
CC -!- FUNCTION: Does not display typical F-actin depolymerizing activity.
CC Exhibits a high ability to stabilize and cross-link actin filaments.
CC Functions as an actin bundling protein with the highest efficiency
CC under acidic conditions (PubMed:21570971). May play a role in the
CC modulation of levels of histone H3 lysine 4 trimethylation and H3
CC lysine 9 and 14 acetylation at the FLC locus (PubMed:18830798).
CC {ECO:0000269|PubMed:18830798, ECO:0000269|PubMed:21570971}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21570971}.
CC -!- INDUCTION: By auxin, gibberellin, abscisic acid (ABA) and kinetin in
CC roots. {ECO:0000269|PubMed:21570971}.
CC -!- DISRUPTION PHENOTYPE: Developmental defects, reduced plant size, early
CC flowering and decreased number of inflorescence secondary branches.
CC {ECO:0000269|PubMed:21570971}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA17762.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80214.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022023; CAA17762.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161586; CAB80214.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86442.1; -; Genomic_DNA.
DR EMBL; BT029315; ABK32129.1; -; mRNA.
DR PIR; T05767; T05767.
DR RefSeq; NP_195223.2; NM_119663.4.
DR AlphaFoldDB; O49606; -.
DR SMR; O49606; -.
DR STRING; 3702.AT4G34970.1; -.
DR iPTMnet; O49606; -.
DR PaxDb; O49606; -.
DR PRIDE; O49606; -.
DR ProteomicsDB; 244778; -.
DR EnsemblPlants; AT4G34970.1; AT4G34970.1; AT4G34970.
DR GeneID; 829649; -.
DR Gramene; AT4G34970.1; AT4G34970.1; AT4G34970.
DR KEGG; ath:AT4G34970; -.
DR Araport; AT4G34970; -.
DR TAIR; locus:2131556; AT4G34970.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_2_2_1; -.
DR InParanoid; O49606; -.
DR OMA; HDKKITV; -.
DR OrthoDB; 1370477at2759; -.
DR PRO; PR:O49606; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49606; baseline and differential.
DR Genevisible; O49606; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:TAIR.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IDA:TAIR.
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 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..141
FT /note="Actin-depolymerizing factor 9"
FT /id="PRO_0000278101"
FT DOMAIN 8..141
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q39250"
SQ SEQUENCE 141 AA; 16370 MW; DECC3116C8318979 CRC64;
MALKTATSGM WMTDDCKKSF MEMKWKKVHR YVVYKLEEKS RKVTVDKVGA AGESYDDLAA
SLPEDDCRYA VFDFDYVTVD NCRMSKIFFI TWSPEASRIR EKMMYATSKS GLRRVLDGVH
YELQATDPTE MGFDKIQDRA K
