RFA2A_ORYSJ
ID RFA2A_ORYSJ Reviewed; 279 AA.
AC Q6K9U2; A0A0P0VRK3; B9F4N4; Q9AVM2; Q9FY12;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Replication protein A 32 kDa subunit A;
DE Short=OsRPA32A;
DE AltName: Full=OsRPA32-1;
DE AltName: Full=Replication factor A protein 2A;
DE AltName: Full=Replication protein A 2A;
GN Name=RPA2A; Synonyms=RPA32A;
GN OrderedLocusNames=Os02g0829100, LOC_Os02g58220;
GN ORFNames=OJ1124_D06.4, OsJ_08977;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=11470540; DOI=10.1016/s0378-1119(01)00555-8;
RA Ishibashi T., Kimura S., Furukawa T., Hatanaka M., Hashimoto J.,
RA Sakaguchi K.;
RT "Two types of replication protein A 70 kDa subunit in rice, Oryza sativa:
RT molecular cloning, characterization, and cellular & tissue distribution.";
RL Gene 272:335-343(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lorbiecke R., Fabian T., Huss S., Sauter M.;
RT "Transcript levels of replication proteins A1 (RPA1) and A2 (RPA2) are
RT upregulated in an S phase-specific manner in rice.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP INTERACTION WITH RPA1A; RPA1B AND RPA3.
RX PubMed=15978034; DOI=10.1111/j.1742-4658.2005.04719.x;
RA Ishibashi T., Koga A., Yamamoto T., Uchiyama Y., Mori Y., Hashimoto J.,
RA Kimura S., Sakaguchi K.;
RT "Two types of replication protein A in seed plants.";
RL FEBS J. 272:3270-3281(2005).
RN [9]
RP INTERACTION WITH RPA1B AND RPA3.
RX PubMed=16428324; DOI=10.1093/jb/mvj014;
RA Ishibashi T., Kimura S., Sakaguchi K.;
RT "A higher plant has three different types of RPA heterotrimeric complex.";
RL J. Biochem. 139:99-104(2006).
RN [10]
RP INDUCTION BY GAMMA IRRADIATION.
RX PubMed=25124817; DOI=10.1093/jhered/esu025;
RA Hayashi G., Shibato J., Imanaka T., Cho K., Kubo A., Kikuchi S., Satoh K.,
RA Kimura S., Ozawa S., Fukutani S., Endo S., Ichikawa K., Agrawal G.K.,
RA Shioda S., Fukumoto M., Rakwal R.;
RT "Unraveling low-level gamma radiation--responsive changes in expression of
RT early and late genes in leaves of rice seedlings at Iitate Village,
RT Fukushima.";
RL J. Hered. 105:723-738(2014).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex) (By similarity). Interacts with RPA1A, RPA1B and
CC RPA3. {ECO:0000250, ECO:0000269|PubMed:15978034,
CC ECO:0000269|PubMed:16428324}.
CC -!- INTERACTION:
CC Q6K9U2; Q9SDK9: RPA3; NbExp=5; IntAct=EBI-849513, EBI-849521;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11470540}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, roots, shoot apical
CC meristem (SAM), young leaves, flag leaves and ears, and at lower levels
CC in mature leaves. {ECO:0000269|PubMed:11470540}.
CC -!- INDUCTION: Repressed by sucrose starvation (PubMed:11470540). Induced
CC by gamma irradiation (PubMed:25124817). {ECO:0000269|PubMed:11470540,
CC ECO:0000269|PubMed:25124817}.
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 -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE58102.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB037145; BAB40535.1; -; mRNA.
DR EMBL; AJ278822; CAC03572.1; -; mRNA.
DR EMBL; AP004043; BAD22936.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF10518.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS81724.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE58102.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK103235; BAG95966.1; -; mRNA.
DR RefSeq; XP_015624204.1; XM_015768718.1.
DR AlphaFoldDB; Q6K9U2; -.
DR SMR; Q6K9U2; -.
DR IntAct; Q6K9U2; 1.
DR STRING; 4530.OS02T0829100-01; -.
DR PaxDb; Q6K9U2; -.
DR PRIDE; Q6K9U2; -.
DR EnsemblPlants; Os02t0829100-01; Os02t0829100-01; Os02g0829100.
DR GeneID; 4331236; -.
DR Gramene; Os02t0829100-01; Os02t0829100-01; Os02g0829100.
DR KEGG; osa:4331236; -.
DR eggNOG; KOG3108; Eukaryota.
DR HOGENOM; CLU_051033_3_1_1; -.
DR InParanoid; Q6K9U2; -.
DR OMA; DEHHFKA; -.
DR OrthoDB; 924826at2759; -.
DR PlantReactome; R-OSA-9645850; Activation of pre-replication complex.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; Q6K9U2; OS.
DR GO; GO:0000781; C:chromosome, telomeric region; IBA:GO_Central.
DR GO; GO:0005662; C:DNA replication factor A complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PTHR13989; 1.
DR Pfam; PF08784; RPA_C; 1.
DR PIRSF; PIRSF036949; RPA32; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..279
FT /note="Replication protein A 32 kDa subunit A"
FT /id="PRO_0000422623"
FT DNA_BIND 71..145
FT /note="OB"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 90
FT /note="T -> M (in Ref. 1; BAB40535)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="F -> L (in Ref. 1; BAB40535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30082 MW; EA953E8D120A8913 CRC64;
MMSFSQPDAF SPSQFTSSQN AAADSTTPSK SRGASSTMPL TVKQISEAQQ SGITGEKGAP
FVVDGVETAN VRLVGLVSGK TERNTDVSFT IDDGTGRLDF IRWVNDGADS AETAAVQNGM
YVSVIGSLKG LQERKRATAF AIRPVTDYNE VTLHFIQCVR MHLENTKSQI GSPAKTYSAM
GSSSSNGFSE MTTPTSVKSN PAPVLSVTNG SKTDLNTEVL NVFREPANVE SEHGVHIDEI
VKRFRLPEAK IKVAIDYLAD IGHIYSTIDE SHYKSAFNE
