ADF2_ARATH
ID ADF2_ARATH Reviewed; 137 AA.
AC Q39251; Q9LZT2;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Actin-depolymerizing factor 2;
DE Short=ADF-2;
DE Short=AtADF2;
GN Name=ADF2; OrderedLocusNames=At3g46000; ORFNames=F16L2_210;
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 [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 [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].
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 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 [6]
RP INTERACTION WITH AIP1-1.
RX PubMed=12417710; DOI=10.1105/tpc.005363;
RA Allwood E.G., Anthony R.G., Smertenko A.P., Reichelt S., Drobak B.K.,
RA Doonan J.H., Weeds A.G., Hussey P.J.;
RT "Regulation of the pollen-specific actin-depolymerizing factor LlADF1.";
RL Plant Cell 14:2915-2927(2002).
RN [7]
RP FUNCTION.
RX PubMed=15563618; DOI=10.1104/pp.104.050799;
RA Ketelaar T., Anthony R.G., Hussey P.J.;
RT "Green fluorescent protein-mTalin causes defects in actin organization and
RT cell expansion in Arabidopsis and inhibits actin depolymerizing factor's
RT actin depolymerizing activity in vitro.";
RL Plant Physiol. 136:3990-3998(2004).
RN [8]
RP FUNCTION, AND 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).
CC -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
CC actin) and binds to actin monomers (PubMed:15563618, PubMed:19794115).
CC Required for normal cell growth, plant development, cell organ
CC expansion and flowering. Essential for root-knot nematode infection
CC (PubMed:19794115). {ECO:0000269|PubMed:15563618,
CC ECO:0000269|PubMed:19794115}.
CC -!- SUBUNIT: Interacts with AIP1-1. {ECO:0000269|PubMed:12417710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q39250}.
CC -!- INDUCTION: By the root-knot nematode Meloidogyne incognita.
CC {ECO:0000269|PubMed:19794115}.
CC -!- MISCELLANEOUS: Plants silencing ADF2 show net stabilization of F-actin
CC that blocks cell maturation and root-knot nematode development and
CC reproduction. {ECO:0000269|PubMed:19794115}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U48939; AAB03697.1; -; mRNA.
DR EMBL; AL162459; CAB82824.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78099.1; -; Genomic_DNA.
DR EMBL; AF370482; AAK43859.1; -; mRNA.
DR EMBL; AF386925; AAK62370.1; -; mRNA.
DR EMBL; AY064660; AAL47369.1; -; mRNA.
DR EMBL; BT000377; AAN15696.1; -; mRNA.
DR PIR; T47540; T47540.
DR RefSeq; NP_001327290.1; NM_001339233.1.
DR RefSeq; NP_566882.1; NM_114469.5.
DR AlphaFoldDB; Q39251; -.
DR SMR; Q39251; -.
DR STRING; 3702.AT3G46000.1; -.
DR iPTMnet; Q39251; -.
DR PaxDb; Q39251; -.
DR PRIDE; Q39251; -.
DR ProteomicsDB; 244763; -.
DR EnsemblPlants; AT3G46000.1; AT3G46000.1; AT3G46000.
DR GeneID; 823743; -.
DR Gramene; AT3G46000.1; AT3G46000.1; AT3G46000.
DR KEGG; ath:AT3G46000; -.
DR Araport; AT3G46000; -.
DR TAIR; locus:2077107; AT3G46000.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_2_2_1; -.
DR InParanoid; Q39251; -.
DR OMA; ECKYAIY; -.
DR PhylomeDB; Q39251; -.
DR PRO; PR:Q39251; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39251; baseline and differential.
DR Genevisible; Q39251; AT.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0006952; P:defense response; IEA:UniProtKB-KW.
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; Cytoplasm; Cytoskeleton; Phosphoprotein; Plant defense;
KW Reference proteome.
FT CHAIN 1..137
FT /note="Actin-depolymerizing factor 2"
FT /id="PRO_0000214924"
FT DOMAIN 5..137
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q39250"
SQ SEQUENCE 137 AA; 15745 MW; BE28852817394046 CRC64;
MANAASGMAV HDDCKLKFME LKAKRTFRTI VYKIEDKQVI VEKLGEPEQS YDDFAASLPA
DDCRYCIYDF DFVTAENCQK SKIFFIAWSP DTAKVRDKMI YASSKDRFKR ELDGIQVELQ
ATDPTEMGLD VFKSRTN
