ADF4_ARATH
ID ADF4_ARATH Reviewed; 139 AA.
AC Q9ZSK3; B9DGG7; Q94A13; Q9FJE7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Actin-depolymerizing factor 4;
DE Short=ADF-4;
DE Short=AtADF4;
GN Name=ADF4; OrderedLocusNames=At5g59890; ORFNames=MMN10.13;
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 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 [8]
RP INDUCTION.
RX PubMed=19794115; DOI=10.1105/tpc.109.069104;
RA Clement M., Ketelaar T., Rodiuc N., Banora M.Y., Smertenko A., Engler G.,
RA Abad P., Hussey P.J., de Almeida Engler J.;
RT "Actin-depolymerizing factor2-mediated actin dynamics are essential for
RT root-knot nematode infection of Arabidopsis.";
RL Plant Cell 21:2963-2979(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19346440; DOI=10.1104/pp.109.137604;
RA Tian M., Chaudhry F., Ruzicka D.R., Meagher R.B., Staiger C.J., Day B.;
RT "Arabidopsis actin-depolymerizing factor AtADF4 mediates defense signal
RT transduction triggered by the Pseudomonas syringae effector AvrPphB.";
RL Plant Physiol. 150:815-824(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22010035; DOI=10.1105/tpc.111.090670;
RA Henty J.L., Bledsoe S.W., Khurana P., Meagher R.B., Day B., Blanchoin L.,
RA Staiger C.J.;
RT "Arabidopsis actin depolymerizing factor4 modulates the stochastic dynamic
RT behavior of actin filaments in the cortical array of epidermal cells.";
RL Plant Cell 23:3711-3726(2011).
RN [11]
RP FUNCTION, PHOSPHORYLATION AT SER-6, AND MUTAGENESIS OF SER-6.
RX PubMed=23144618; DOI=10.1371/journal.ppat.1003006;
RA Porter K., Shimono M., Tian M., Day B.;
RT "Arabidopsis Actin-Depolymerizing Factor-4 links pathogen perception,
RT defense activation and transcription to cytoskeletal dynamics.";
RL PLoS Pathog. 8:E1003006-E1003006(2012).
RN [12]
RP FUNCTION.
RX PubMed=24464292; DOI=10.1105/tpc.113.122499;
RA Henty-Ridilla J.L., Li J., Day B., Staiger C.J.;
RT "ACTIN DEPOLYMERIZING FACTOR4 regulates actin dynamics during innate immune
RT signaling in Arabidopsis.";
RL Plant Cell 26:340-352(2014).
CC -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
CC actin) and binds to actin monomers (PubMed:19346440, PubMed:22010035).
CC Contributes to the stochastic dynamic turnover of actin filaments
CC (PubMed:22010035). Binds monomeric actin (G-actin) with a marked
CC preference for the ADP-loaded form and inhibits the rate of nucleotide
CC exchange on G-actin. Involved in resistance triggered by the effector
CC AvrPphB of Pseudomonas syringae pv tomato (Pst). May modulate the
CC AvrPphB-RPS5-mediated defense signal transduction pathway
CC (PubMed:19346440). During AvrPphB-triggered resistance signaling
CC pathway, involved in the control of MPK3 and MPK6 activation, via the
CC coordinated regulation of actin cytoskeletal dynamics and RPS5
CC resistance gene transcription (PubMed:23144618). During innate immune
CC response triggered by the bacterial elf26 peptide, the inhibition of
CC ADF4 regulates actin dynamics in order to execute key events associated
CC with pattern-triggered immunity (PTI), such as cell wall fortification
CC and transcriptional activation of defense gene markers
CC (PubMed:24464292). {ECO:0000269|PubMed:19346440,
CC ECO:0000269|PubMed:22010035, ECO:0000269|PubMed:23144618,
CC ECO:0000269|PubMed:24464292}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19346440}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZSK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZSK3-2; Sequence=VSP_008903;
CC -!- INDUCTION: By the root-knot nematode Meloidogyne incognita.
CC {ECO:0000269|PubMed:19794115}.
CC -!- PTM: Phosphorylation at Ser-6 is required for resistance to Pseudomonas
CC syringae pv tomato AvrPphB. {ECO:0000269|PubMed:23144618}.
CC -!- DISRUPTION PHENOTYPE: Increased root length under light-grown
CC conditions. Increased length of hypocotyls under dark-grown conditions.
CC Altered architecture of the actin cytoskeleton in hypocotyl cells
CC (PubMed:22010035). Compromised resistance in response to Pseudomonas
CC syringae pv tomato expressing AvrPphB (PubMed:19346440).
CC {ECO:0000269|PubMed:19346440, ECO:0000269|PubMed:22010035}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; AF102822; AAD09110.1; -; mRNA.
DR EMBL; AB015475; BAB08357.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97247.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97248.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70922.1; -; Genomic_DNA.
DR EMBL; AY050460; AAK91473.1; -; mRNA.
DR EMBL; AY090336; AAL90997.1; -; mRNA.
DR EMBL; AY084757; AAM61326.1; -; mRNA.
DR EMBL; AK317148; BAH19834.1; -; mRNA.
DR RefSeq; NP_001318843.1; NM_001345374.1. [Q9ZSK3-2]
DR RefSeq; NP_568916.2; NM_125382.2. [Q9ZSK3-2]
DR RefSeq; NP_851228.1; NM_180897.3. [Q9ZSK3-1]
DR AlphaFoldDB; Q9ZSK3; -.
DR SMR; Q9ZSK3; -.
DR BioGRID; 21355; 1.
DR STRING; 3702.AT5G59890.1; -.
DR iPTMnet; Q9ZSK3; -.
DR PaxDb; Q9ZSK3; -.
DR PRIDE; Q9ZSK3; -.
DR ProteomicsDB; 244693; -. [Q9ZSK3-1]
DR EnsemblPlants; AT5G59890.1; AT5G59890.1; AT5G59890. [Q9ZSK3-1]
DR EnsemblPlants; AT5G59890.2; AT5G59890.2; AT5G59890. [Q9ZSK3-2]
DR EnsemblPlants; AT5G59890.3; AT5G59890.3; AT5G59890. [Q9ZSK3-2]
DR GeneID; 836111; -.
DR Gramene; AT5G59890.1; AT5G59890.1; AT5G59890. [Q9ZSK3-1]
DR Gramene; AT5G59890.2; AT5G59890.2; AT5G59890. [Q9ZSK3-2]
DR Gramene; AT5G59890.3; AT5G59890.3; AT5G59890. [Q9ZSK3-2]
DR KEGG; ath:AT5G59890; -.
DR Araport; AT5G59890; -.
DR TAIR; locus:2168063; AT5G59890.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_2_2_1; -.
DR InParanoid; Q9ZSK3; -.
DR OMA; KRTHRYA; -.
DR PhylomeDB; Q9ZSK3; -.
DR PRO; PR:Q9ZSK3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9ZSK3; baseline and differential.
DR Genevisible; Q9ZSK3; AT.
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:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0002758; P:innate immune response-activating signal transduction; IMP: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 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Plant defense; Reference proteome.
FT CHAIN 1..139
FT /note="Actin-depolymerizing factor 4"
FT /id="PRO_0000214926"
FT DOMAIN 5..139
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23144618"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_008903"
FT MUTAGEN 6
FT /note="S->A,D: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:23144618"
FT CONFLICT 117
FT /note="I -> R (in Ref. 1; AAD09110)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="L -> W (in Ref. 1; AAD09110)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 139 AA; 16034 MW; 57F95F557F42F863 CRC64;
MANAASGMAV HDDCKLRFLE LKAKRTHRFI VYKIEEKQKQ VIVEKVGEPI LTYEDFAASL
PADECRYAIY DFDFVTAENC QKSKIFFIAW CPDVAKVRSK MIYASSKDRF KRELDGIQVE
LQATDPTEMD LDVLKSRVN
