ADF1_ARATH
ID ADF1_ARATH Reviewed; 139 AA.
AC Q39250;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Actin-depolymerizing factor 1;
DE Short=ADF-1;
DE Short=AtADF1;
GN Name=ADF1; OrderedLocusNames=At3g46010; ORFNames=F16L2_220;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Staiger C.J., Ashworth S.L.;
RT "Actin depolymerizing factor from Arabidopsis thaliana severs polymers and
RT binds to monomers in a pH-dependent manner.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia;
RX PubMed=11414611; DOI=10.1023/a:1010687911374;
RA Dong C.-H., Kost B., Xia G.-X., Chua N.-H.;
RT "Molecular identification and characterization of the Arabidopsis AtADF1,
RT AtADF5 and AtADF6 genes.";
RL Plant Mol. Biol. 45:517-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=11402164; DOI=10.2307/3871299;
RA Dong C.-H., Xia G.-X., Hong Y., Ramachandran S., Kost B., Chua N.-H.;
RT "ADF proteins are involved in the control of flowering and regulate F-actin
RT organization, cell expansion, and organ growth in Arabidopsis.";
RL Plant Cell 13:1333-1346(2001).
RN [8]
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 [9]
RP FUNCTION.
RX PubMed=17538023; DOI=10.1091/mbc.e06-11-1041;
RA Chaudhry F., Guerin C., von Witsch M., Blanchoin L., Staiger C.J.;
RT "Identification of Arabidopsis cyclase-associated protein 1 as the first
RT nucleotide exchange factor for plant actin.";
RL Mol. Biol. Cell 18:3002-3014(2007).
RN [10]
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).
RN [11]
RP MUTAGENESIS OF LYS-82; ARG-98; LYS-100; ARG-135 AND ARG-137.
RX PubMed=23190411; DOI=10.1111/jipb.12015;
RA Dong C.H., Tang W.P., Liu J.Y.;
RT "Arabidopsis AtADF1 is functionally affected by mutations on actin binding
RT sites.";
RL J. Integr. Plant Biol. 55:250-261(2013).
RN [12]
RP PHOSPHORYLATION AT SER-6, AND MUTAGENESIS OF SER-6.
RX PubMed=23903947; DOI=10.1007/s00299-013-1482-6;
RA Dong C.H., Hong Y.;
RT "Arabidopsis CDPK6 phosphorylates ADF1 at N-terminal serine 6
RT predominantly.";
RL Plant Cell Rep. 32:1715-1728(2013).
RN [13]
RP INTERACTION WITH GRF6/AFT1, AND DISRUPTION PHENOTYPE.
RX PubMed=26345162; DOI=10.1007/s11427-015-4897-1;
RA Zhao S., Zhao Y., Guo Y.;
RT "14-3-3 lambda protein interacts with ADF1 to regulate actin cytoskeleton
RT dynamics in Arabidopsis.";
RL Sci. China Life Sci. 58:1142-1150(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11025548;
RX DOI=10.1002/1097-0134(20001115)41:3<374::aid-prot90>3.0.co;2-f;
RA Bowman G.D., Nodelman I.M., Hong Y., Chua N.-H., Lindberg U., Schutt C.E.;
RT "A comparative structural analysis of the ADF/cofilin family.";
RL Proteins 41:374-384(2000).
CC -!- FUNCTION: Actin-depolymerizing protein. Stimulates F-actin
CC depolymerization. Involved in plant development, cell organ expansion
CC and flowering by controlling breakdown of thick actin cables
CC (PubMed:11402164). Severs actin filaments or bundles and promotes actin
CC cytoskeleton disassembly (PubMed:21570971). Binds monomeric actin (G-
CC actin) with a marked preference for the ADP-loaded form and inhibits
CC the rate of nucleotide exchange on G-actin (PubMed:17538023).
CC {ECO:0000269|PubMed:11402164, ECO:0000269|PubMed:17538023,
CC ECO:0000269|PubMed:21570971}.
CC -!- SUBUNIT: Interacts with the 14-3-3-like protein GRF6/AFT1.
CC {ECO:0000269|PubMed:26345162}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21570971}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q39250-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues of all organs.
CC {ECO:0000269|PubMed:11414611}.
CC -!- PTM: Phosphorylation at Ser-6 by CPK3/CDPK6 inhibits actin-
CC depolimerizing activity. {ECO:0000269|PubMed:23903947}.
CC -!- DISRUPTION PHENOTYPE: Increased length of hypocotyls under dark-grown
CC conditions. {ECO:0000269|PubMed:26345162}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; U48938; AAB03696.1; -; mRNA.
DR EMBL; AF102173; AAC72407.1; -; Genomic_DNA.
DR EMBL; AL162459; CAB88325.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78100.1; -; Genomic_DNA.
DR EMBL; AY035154; AAK59658.1; -; mRNA.
DR EMBL; AY062940; AAL33770.1; -; mRNA.
DR EMBL; AY085853; AAM63066.1; -; mRNA.
DR RefSeq; NP_190187.1; NM_114470.3. [Q39250-1]
DR PDB; 1F7S; X-ray; 2.00 A; A=1-139.
DR PDBsum; 1F7S; -.
DR AlphaFoldDB; Q39250; -.
DR SMR; Q39250; -.
DR BioGRID; 9064; 2.
DR STRING; 3702.AT3G46010.2; -.
DR iPTMnet; Q39250; -.
DR PaxDb; Q39250; -.
DR PRIDE; Q39250; -.
DR ProteomicsDB; 244815; -. [Q39250-1]
DR EnsemblPlants; AT3G46010.1; AT3G46010.1; AT3G46010. [Q39250-1]
DR GeneID; 823744; -.
DR Gramene; AT3G46010.1; AT3G46010.1; AT3G46010. [Q39250-1]
DR KEGG; ath:AT3G46010; -.
DR Araport; AT3G46010; -.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_2_2_1; -.
DR InParanoid; Q39250; -.
DR OMA; RREFRWA; -.
DR PhylomeDB; Q39250; -.
DR EvolutionaryTrace; Q39250; -.
DR PRO; PR:Q39250; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39250; baseline and differential.
DR Genevisible; Q39250; 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:0030042; P:actin filament depolymerization; IBA:GO_Central.
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; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..139
FT /note="Actin-depolymerizing factor 1"
FT /id="PRO_0000214923"
FT DOMAIN 5..139
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 6
FT /note="Phosphoserine; by CPK3"
FT /evidence="ECO:0000269|PubMed:23903947"
FT MUTAGEN 6
FT /note="S->A,D: Loss of phosphorylation by CPK3/CDPK6."
FT /evidence="ECO:0000269|PubMed:23903947"
FT MUTAGEN 82
FT /note="K->A: Reduces binding affinity to F-actin and actin-
FT depolimerizing activity; when associated with A-135 and A-
FT 137."
FT /evidence="ECO:0000269|PubMed:23190411"
FT MUTAGEN 98
FT /note="R->A: Reduces binding affinity to both G-actin and
FT F-actin, and actin-depolimerizing activity; when associated
FT with A-100."
FT /evidence="ECO:0000269|PubMed:23190411"
FT MUTAGEN 100
FT /note="K->A: Reduces binding affinity to both G-actin and
FT F-actin, and actin-depolimerizing activity; when associated
FT with A-98."
FT /evidence="ECO:0000269|PubMed:23190411"
FT MUTAGEN 135
FT /note="R->A: Reduces binding affinity to F-actin and actin-
FT depolimerizing activity; when associated with A-82 and A-
FT 137."
FT /evidence="ECO:0000269|PubMed:23190411"
FT MUTAGEN 137
FT /note="R->A: Reduces binding affinity to F-actin and actin-
FT depolimerizing activity; when associated with A-82 and A-
FT 135."
FT /evidence="ECO:0000269|PubMed:23190411"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1F7S"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1F7S"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1F7S"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:1F7S"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:1F7S"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:1F7S"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:1F7S"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:1F7S"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1F7S"
SQ SEQUENCE 139 AA; 16113 MW; E9429E0FE23A944F CRC64;
MANAASGMAV HDDCKLRFLE LKAKRTHRFI VYKIEEKQKQ VVVEKVGQPI QTYEEFAACL
PADECRYAIY DFDFVTAENC QKSKIFFIAW CPDIAKVRSK MIYASSKDRF KRELDGIQVE
LQATDPTEMD LDVFRSRAN
