ID RFA2A_ARATH Reviewed; 279 AA.
AC Q9ZQ19;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 24-JAN-2024, entry version 152.
DE RecName: Full=Replication protein A 32 kDa subunit A;
DE Short=AtRPA32A;
DE Short=RP-A p32 A;
DE AltName: Full=DNA replication protein A2 subunit A;
DE AltName: Full=Protein SUPPRESSOR OF ROS1;
DE AltName: Full=Replication factor A protein 2 A;
DE Short=AtRPA2 A;
DE Short=RF-A protein 2 A;
DE AltName: Full=Replicon protein A2 A;
GN Name=RPA2A; Synonyms=ROR1, RPA32A; OrderedLocusNames=At2g24490;
GN ORFNames=T28I24.22;
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], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH ROS1,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=16326925; DOI=10.1105/tpc.105.037507;
RA Xia R., Wang J., Liu C., Wang Y., Wang Y., Zhai J., Liu J., Hong X.,
RA Cao X., Zhu J.-K., Gong Z.;
RT "ROR1/RPA2A, a putative replication protein A2, functions in epigenetic
RT gene silencing and in regulation of meristem development in Arabidopsis.";
RL Plant Cell 18:85-103(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH ROS1.
RC STRAIN=cv. Columbia;
RX PubMed=16271867; DOI=10.1016/j.cub.2005.09.013;
RA Kapoor A., Agarwal M., Andreucci A., Zheng X., Gong Z., Hasegawa P.M.,
RA Bressan R.A., Zhu J.-K.;
RT "Mutations in a conserved replication protein suppress transcriptional gene
RT silencing in a DNA-methylation-independent manner in Arabidopsis.";
RL Curr. Biol. 15:1912-1918(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16271868; DOI=10.1016/j.cub.2005.09.044;
RA Elmayan T., Proux F., Vaucheret H.;
RT "Arabidopsis RPA2: a genetic link among transcriptional gene silencing, DNA
RT repair, and DNA replication.";
RL Curr. Biol. 15:1919-1925(2005).
RN [9]
RP INTERACTION WITH ASE1/AT3G02920; PDX2; AT5G62350; RPA1A/AT2G06510;
RP ARF1/AT1G10630; AT4G18590 AND AT3G52630.
RX PubMed=20706207; DOI=10.1038/msb.2010.53;
RA Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
RA Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y., De Bodt S.,
RA Maere S., Laukens K., Pharazyn A., Ferreira P.C.G., Eloy N., Renne C.,
RA Meyer C., Faure J.-D., Steinbrenner J., Beynon J., Larkin J.C.,
RA Van de Peer Y., Hilson P., Kuiper M., De Veylder L., Van Onckelen H.,
RA Inze D., Witters E., De Jaeger G.;
RT "Targeted interactomics reveals a complex core cell cycle machinery in
RT Arabidopsis thaliana.";
RL Mol. Syst. Biol. 6:397-397(2010).
CC -!- FUNCTION: Component of the replication protein A complex (RPA) required
CC for DNA recombination, repair and replication. The activity of RPA is
CC mediated by single-stranded DNA binding and protein interactions.
CC Required fo cell division in meristems. Involved in the maintenance of
CC transcriptional epigenetic gene silencing (TGS) at specific loci
CC (including some transposons) by regulating histone H3 acetylation,
CC 'Lys-4' and 'Lys-9' methylation. {ECO:0000269|PubMed:16271867,
CC ECO:0000269|PubMed:16271868, ECO:0000269|PubMed:16326925}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex) (By similarity). Interacts with ROS1. Binds to
CC ASE1/At3g02920, PDX2, At5g62350, RPA1A/At2g06510, ARF1/At1g10630,
CC At4g18590 and At3g52630. {ECO:0000250, ECO:0000269|PubMed:16271867,
CC ECO:0000269|PubMed:16326925, ECO:0000269|PubMed:20706207}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16271867,
CC ECO:0000269|PubMed:16326925}. Note=Redistributes to discrete nuclear
CC foci upon DNA damage. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in shoot and root meristems.
CC Present in seedlings, roots, leaves, siliques and flowers.
CC {ECO:0000269|PubMed:16271867, ECO:0000269|PubMed:16326925}.
CC -!- DEVELOPMENTAL STAGE: Accumulates essentially in meristematic active
CC tissues. In seedlings, expressed in primary roots, shoot apical
CC meristems (SAMs), cotyledons, and vascular tissues. Later observed in
CC lateral root primordia, root tips, SAMs and young leaves.
CC {ECO:0000269|PubMed:16326925}.
CC -!- PTM: Phosphorylated in a cell-cycle-dependent manner (from the S phase
CC until mitosis). In response to DNA damage, recruited to DNA-repair
CC nuclear foci, as a hypophosphorylated form (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Affected cell division in meristems but normal
CC final cell sizes. Earlier flowering and smaller plant size. Enhanced
CC sensitivity to methyl methanesulfonate (MMS), a genotoxic agent that
CC damages DNA bases. Enhanced expression of some transposons. When
CC associated with ROS1 disruption, restored silencing of some genes
CC associated with increased histone H3 acetylation and histone H3 'Lys-4'
CC methylation (H3K4me2), but decreased histone H3 'Lys-9' methylation
CC (H3K9me2) in their promoter. {ECO:0000269|PubMed:16271867,
CC ECO:0000269|PubMed:16271868, ECO:0000269|PubMed:16326925}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
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DR EMBL; DQ284987; ABB86293.1; -; mRNA.
DR EMBL; AC006403; AAD18120.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07582.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07583.1; -; Genomic_DNA.
DR EMBL; AK117537; BAC42198.1; -; mRNA.
DR EMBL; BT005433; AAO63853.1; -; mRNA.
DR EMBL; AY088525; AAM66059.1; -; mRNA.
DR PIR; C84637; C84637.
DR RefSeq; NP_001118376.1; NM_001124904.1.
DR RefSeq; NP_565571.1; NM_128010.3.
DR AlphaFoldDB; Q9ZQ19; -.
DR SMR; Q9ZQ19; -.
DR BioGRID; 2337; 8.
DR IntAct; Q9ZQ19; 6.
DR STRING; 3702.Q9ZQ19; -.
DR PaxDb; 3702-AT2G24490-2; -.
DR ProteomicsDB; 236905; -.
DR EnsemblPlants; AT2G24490.1; AT2G24490.1; AT2G24490.
DR EnsemblPlants; AT2G24490.2; AT2G24490.2; AT2G24490.
DR GeneID; 816985; -.
DR Gramene; AT2G24490.1; AT2G24490.1; AT2G24490.
DR Gramene; AT2G24490.2; AT2G24490.2; AT2G24490.
DR KEGG; ath:AT2G24490; -.
DR Araport; AT2G24490; -.
DR TAIR; AT2G24490; RPA2.
DR eggNOG; KOG3108; Eukaryota.
DR HOGENOM; CLU_051033_3_1_1; -.
DR InParanoid; Q9ZQ19; -.
DR OMA; SFGNKRY; -.
DR OrthoDB; 72010at2759; -.
DR PhylomeDB; Q9ZQ19; -.
DR PRO; PR:Q9ZQ19; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQ19; baseline and differential.
DR Genevisible; Q9ZQ19; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04478; RPA2_DBD_D; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014646; Rfa2/RPA32.
DR InterPro; IPR014892; RPA_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989:SF34; REPLICATION PROTEIN A 32 KDA SUBUNIT A; 1.
DR PANTHER; PTHR13989; REPLICATION PROTEIN A-RELATED; 1.
DR Pfam; PF08784; RPA_C; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PIRSF; PIRSF036949; RPA32; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..279
FT /note="Replication protein A 32 kDa subunit A"
FT /id="PRO_0000419968"
FT DNA_BIND 73..148
FT /note="OB"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 30980 MW; 3DD5B70FE6FC5736 CRC64;
MFSSSQFEPN SGFSGGGFMS SQPSQAYESS SSTAKNRDFQ GLVPVTVKQI TECFQSSGEK
SGLVINGISL TNVSLVGLVC DKDESKVTEV RFTLDDGTGR IDCKRWVSET FDAREMESVR
DGTYVRLSGH LKTFQGKTQL LVFSVRPIMD FNEVTFHYIE CIHFYSQNSE SQRQQVGDVT
QSVNTTFQGG SNTNQATLLN PVVSSQNNDG NGRKNLDDMI LDYLKQPACT ARQQGIHIDE
IAQQLKIPKN KLEGVVQSLE GDGLIYSTID EYHFKHVEL
//
