ARP5_ARATH
ID ARP5_ARATH Reviewed; 724 AA.
AC Q940Z2; C0Z2X1; C8YXA1; F4J9R3; Q9C7A3; Q9LHH0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Actin-related protein 5 {ECO:0000303|PubMed:19679120};
GN Name=ARP5 {ECO:0000303|PubMed:19679120};
GN OrderedLocusNames=At3g12380 {ECO:0000312|Araport:AT3G12380};
GN ORFNames=MQC3.19 {ECO:0000312|EMBL:BAB03145.1},
GN T2E22.30 {ECO:0000312|EMBL:AAG51035.1};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=19679120; DOI=10.1016/j.ydbio.2009.08.006;
RA Kandasamy M.K., McKinney E.C., Deal R.B., Smith A.P., Meagher R.B.;
RT "Arabidopsis actin-related protein ARP5 in multicellular development and
RT DNA repair.";
RL Dev. Biol. 335:22-32(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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] (ISOFORM 3).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
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 [7]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=11891255; DOI=10.1104/pp.010906;
RA McKinney E.C., Kandasamy M.K., Meagher R.B.;
RT "Arabidopsis contains ancient classes of differentially expressed actin-
RT related protein genes.";
RL Plant Physiol. 128:997-1007(2002).
RN [8]
RP REVIEW, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15063870; DOI=10.1016/j.tplants.2004.02.004;
RA Kandasamy M.K., Deal R.B., McKinney E.C., Meagher R.B.;
RT "Plant actin-related proteins.";
RL Trends Plant Sci. 9:196-202(2004).
RN [9]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH EEN.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=31418686; DOI=10.7554/elife.47835;
RA Zander M., Willige B.C., He Y., Nguyen T.A., Langford A.E., Nehring R.,
RA Howell E., McGrath R., Bartlett A., Castanon R., Nery J.R., Chen H.,
RA Zhang Z., Jupe F., Stepanova A., Schmitz R.J., Lewsey M.G., Chory J.,
RA Ecker J.R.;
RT "Epigenetic silencing of a multifunctional plant stress regulator.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Probable subunit of a chromatin-remodeling complex. Involved
CC in DNA repair. Required for multicellular development of all organs.
CC {ECO:0000269|PubMed:19679120}.
CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex
CC (Probable). Interacts with EEN (PubMed:31418686).
CC {ECO:0000269|PubMed:31418686, ECO:0000305|PubMed:31418686}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10907853}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:19679120}. Cytoplasm
CC {ECO:0000269|PubMed:19679120}. Note=Localized in the nucleoplasm of
CC interphase cells (PubMed:19679120). However, dispersed into the
CC cytoplasm in dividing cells at metaphase (PubMed:19679120).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q940Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q940Z2-2; Sequence=VSP_041305;
CC Name=3;
CC IsoId=Q940Z2-3; Sequence=VSP_041304;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in seedlings, roots, leaves,
CC buds, flowers and siliques. {ECO:0000269|PubMed:19679120}.
CC -!- DISRUPTION PHENOTYPE: Moderately dwarfed plants with small organs
CC composed of small-sized cells (PubMed:19679120). Higher density of
CC developmentally delayed stomata (PubMed:19679120). Hypersensitivity to
CC DNA-damaging reagents such as hydroxyurea, methylmethane sulfonate, and
CC bleocin (PubMed:19679120). Differential expression of several genes
CC (PubMed:31418686). The double mutant ref6-1 arp5-1 is insensitive to
CC ethylene (ET) and exhibits reduced levels of EIN2 associated with a
CC shift of the chromatin landscape to a repressive state at its locus
CC (e.g. H3K27me3 and H2A.Z) (PubMed:31418686).
CC {ECO:0000269|PubMed:19679120, ECO:0000269|PubMed:31418686}.
CC -!- SIMILARITY: Belongs to the actin family. ARP5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03145.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; FJ850973; ACV53017.1; -; Genomic_DNA.
DR EMBL; FJ850974; ACV53018.1; -; mRNA.
DR EMBL; AP002047; BAB03145.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069474; AAG51035.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75190.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75191.1; -; Genomic_DNA.
DR EMBL; AY052346; AAK96538.1; -; mRNA.
DR EMBL; BT001061; AAN46815.1; -; mRNA.
DR EMBL; AK318935; BAH57050.1; -; mRNA.
DR RefSeq; NP_001189870.1; NM_001202941.1. [Q940Z2-2]
DR RefSeq; NP_566422.4; NM_112073.5. [Q940Z2-1]
DR AlphaFoldDB; Q940Z2; -.
DR BioGRID; 5750; 1.
DR IntAct; Q940Z2; 1.
DR STRING; 3702.AT3G12380.2; -.
DR iPTMnet; Q940Z2; -.
DR PaxDb; Q940Z2; -.
DR PRIDE; Q940Z2; -.
DR ProteomicsDB; 246980; -. [Q940Z2-1]
DR EnsemblPlants; AT3G12380.1; AT3G12380.1; AT3G12380. [Q940Z2-1]
DR EnsemblPlants; AT3G12380.2; AT3G12380.2; AT3G12380. [Q940Z2-2]
DR GeneID; 820416; -.
DR Gramene; AT3G12380.1; AT3G12380.1; AT3G12380. [Q940Z2-1]
DR Gramene; AT3G12380.2; AT3G12380.2; AT3G12380. [Q940Z2-2]
DR KEGG; ath:AT3G12380; -.
DR Araport; AT3G12380; -.
DR TAIR; locus:2092452; AT3G12380.
DR eggNOG; KOG0681; Eukaryota.
DR InParanoid; Q940Z2; -.
DR OMA; TNWNHQE; -.
DR OrthoDB; 344271at2759; -.
DR PRO; PR:Q940Z2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940Z2; baseline and differential.
DR Genevisible; Q940Z2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:TAIR.
DR GO; GO:0030029; P:actin filament-based process; TAS:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0080036; P:regulation of cytokinin-activated signaling pathway; IMP:CACAO.
DR GO; GO:0010082; P:regulation of root meristem growth; IMP:CACAO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR027664; Arp5.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF16; PTHR11937:SF16; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA damage; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..724
FT /note="Actin-related protein 5"
FT /id="PRO_0000320532"
FT REGION 358..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 1..134
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_041304"
FT VAR_SEQ 56
FT /note="A -> ATVLLSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_041305"
FT CONFLICT 55
FT /note="K -> R (in Ref. 6; BAH57050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 83053 MW; C807056B2BEC91B0 CRC64;
MAFVSRIRRQ SDYNTYPSSI PIVIDNGASY FRIGWAGETE PRVVFRNIVQ RPRHKATGET
VTIVGDLDPS MMKYFDCTRS GPRSPFDSNV VYQFEIMEYI LDYAFDRLGA NGSGIDHPIL
ITECACNPVQ SRSKMAELLF ETYGVPAVAF GVDAAFSYKY NQLHGICKKD GIVLCPGFTT
THSIPFVDGE PIYKGSSRTN IGGYHVTDYL KQLLSLKYPF HSSRFTWEKA EDLKLEHCYI
APDYASEIRL FQEGRKEAEE KTSYWQLPWI PPPTEVPPSE EEIARKAAIR EKQGQRLREM
AEAKRVSKIN DMENQLISLR FLLKQVDQVE EDDIPTFLSD TGYASRQELE STITKVTQSL
RKARGEPKNE PAEYEENPDS LNNEKYPLMN VPDDILTPEQ LKDKKRQMFL KTTAEGRLRA
RQKRNEEELE KEKRNQLEEE RRRENPESYL EELQAQYKEV LERVEQKKRL KTNGSSNGNN
KSGGIGRGER LSAAQRERMR LLTTAAFDRG KGEDTFGSRD EDWQLYKLMS KDNDDDDEQP
DSDEAELARL SSRLQEIDPT FVQKVEGELS QTSGEVPRVR PLTEEDYKIV IGIERFRCPE
ILFHPNLIGI DQVGLDEMAG TSIRRLPHDE KELEERLTSS ILMTGGCSLL PGMNERLECG
IRMIRPCGSP INVVRAMDPV LDAWRGASAF AANLNFLGNA FTKMDYDEKG EDWLRNYQIR
YNYL
