ARS1_ARATH
ID ARS1_ARATH Reviewed; 313 AA.
AC Q9M8S7; A2RVV3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Protein ABA AND ROS SENSITIVE 1 {ECO:0000303|PubMed:26583028};
GN Name=ARS1 {ECO:0000303|PubMed:26583028};
GN OrderedLocusNames=At3g02860 {ECO:0000312|Araport:AT3G02860};
GN ORFNames=F13E7.20 {ECO:0000312|EMBL:AAF26974.1};
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 [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 [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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=26583028; DOI=10.3389/fpls.2015.00963;
RA Baek D., Cha J.Y., Kang S., Park B., Lee H.J., Hong H., Chun H.J.,
RA Kim D.H., Kim M.C., Lee S.Y., Yun D.J.;
RT "The Arabidopsis a zinc finger domain protein ARS1 is essential for seed
RT germination and ROS homeostasis in response to ABA and oxidative stress.";
RL Front. Plant Sci. 6:963-963(2015).
CC -!- FUNCTION: Essential for breaking seed dormancy before seed germination
CC (PubMed:26583028). Prevents reactive oxygen species (ROS) accumulation
CC in response to abscisic acid (ABA) and oxidative stress, probably by
CC repressing the accumulation of ABA-induced ROS-scavenging enzymes (e.g.
CC CSD3) (PubMed:26583028). {ECO:0000269|PubMed:26583028}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:26583028}. Cytoplasm {ECO:0000269|PubMed:26583028}.
CC Note=Translocates from the nucleus to the cytoplasm in response to
CC abscisic acid (ABA) and oxidative stress (e.g. hydrogen peroxide
CC H(2)O(2) and methyl viologen (MV)). {ECO:0000269|PubMed:26583028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9M8S7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9M8S7-2; Sequence=VSP_061043;
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques and, to a lower
CC extent, in roots (PubMed:26583028). Barely deteclable in leaves and
CC stems (PubMed:26583028). {ECO:0000269|PubMed:26583028}.
CC -!- INDUCTION: Slightly induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:26583028}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to abscisic acid (ABA) during
CC seed germination and to methyl viologen (MV) at the seedling stage,
CC associated with a reduced expression of the superoxide dismutase CSD3
CC and an enhanced accumulation of reactive oxygen species (ROS) after ABA
CC treatment. {ECO:0000269|PubMed:26583028}.
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DR EMBL; AC018363; AAF26974.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73867.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73868.1; -; Genomic_DNA.
DR EMBL; AK229101; BAF00979.1; -; mRNA.
DR EMBL; BT030094; ABN04832.1; -; mRNA.
DR RefSeq; NP_566185.1; NM_111154.4. [Q9M8S7-2]
DR RefSeq; NP_850505.1; NM_180174.2. [Q9M8S7-1]
DR AlphaFoldDB; Q9M8S7; -.
DR SMR; Q9M8S7; -.
DR IntAct; Q9M8S7; 4.
DR STRING; 3702.AT3G02860.2; -.
DR PaxDb; Q9M8S7; -.
DR ProteomicsDB; 181696; -.
DR ProteomicsDB; 181707; -.
DR EnsemblPlants; AT3G02860.1; AT3G02860.1; AT3G02860. [Q9M8S7-2]
DR EnsemblPlants; AT3G02860.2; AT3G02860.2; AT3G02860. [Q9M8S7-1]
DR GeneID; 821212; -.
DR Gramene; AT3G02860.1; AT3G02860.1; AT3G02860. [Q9M8S7-2]
DR Gramene; AT3G02860.2; AT3G02860.2; AT3G02860. [Q9M8S7-1]
DR KEGG; ath:AT3G02860; -.
DR Araport; AT3G02860; -.
DR TAIR; locus:2075422; AT3G02860.
DR eggNOG; KOG3032; Eukaryota.
DR HOGENOM; CLU_058140_1_0_1; -.
DR InParanoid; Q9M8S7; -.
DR OMA; EQIECYK; -.
DR OrthoDB; 1458826at2759; -.
DR PhylomeDB; Q9M8S7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8S7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005681; C:spliceosomal complex; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0033260; P:nuclear DNA replication; IBA:GO_Central.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR.
DR GO; GO:0048838; P:release of seed from dormancy; IMP:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR InterPro; IPR040050; ZNF830-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13278; PTHR13278; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Stress response; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..313
FT /note="Protein ABA AND ROS SENSITIVE 1"
FT /id="PRO_0000452700"
FT ZN_FING 39..61
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT REGION 115..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 232..271
FT /evidence="ECO:0000255"
FT MOTIF 5..12
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 274..281
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 151..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 117
FT /note="Missing (in isoform 2)"
FT /id="VSP_061043"
SQ SEQUENCE 313 AA; 35210 MW; 742B41C814C05F4A CRC64;
MDAQAKKKAM FRSKLNAKKK DTRIDSPLVR YNESDQPVCR VCNVVLKSES LWDVHQASRK
HHEAIDSLKA SAAGVQRGSK PAETRPTKIE ALAKSSNSQT SSGLPPNFFE NREPARAEVE
PAKSKNLEQS KHTIGSETNK SKGPLPAGFF DNQKTDSSNT KTTSEPKQSQ TQTTGPETKP
MVNGNLPTGF FDNKEADLLA HGIKLVKPDI KDEYKEFEKL IQDDLQVVDS RMEEEEVDAA
ETIEEEEQRE QRSYKEKVEI LKRKKMELKA ARLAKRSKTS EGSVKKPKKT EEESPSDEED
DEDSAVDWRA QHL
