RFA1A_ARATH
ID RFA1A_ARATH Reviewed; 640 AA.
AC Q9SKI4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit A;
DE Short=AtRPA70A;
DE AltName: Full=AtRPA1-3;
DE AltName: Full=Replication factor A protein 1A;
DE AltName: Full=Replication protein A 1A;
DE Short=AtRPA1A;
GN Name=RPA1A; Synonyms=RPA70A; OrderedLocusNames=At2g06510; ORFNames=T12H3.6;
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=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 [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].
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 [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 DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19153602; DOI=10.1038/emboj.2008.295;
RA Osman K., Sanchez-Moran E., Mann S.C., Jones G.H., Franklin F.C.;
RT "Replication protein A (AtRPA1a) is required for class I crossover
RT formation but is dispensable for meiotic DNA break repair.";
RL EMBO J. 28:394-404(2009).
RN [7]
RP FUNCTION, INTERACTION WITH RPA2A, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19812063; DOI=10.1093/pcp/pcp140;
RA Takashi Y., Kobayashi Y., Tanaka K., Tamura K.;
RT "Arabidopsis replication protein A 70a is required for DNA damage response
RT and telomere length homeostasis.";
RL Plant Cell Physiol. 50:1965-1976(2009).
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. Plays
CC an essential role at later stages of meiotic recombination events
CC required for the formation of class I crossovers. Is essential for
CC normal progression through meiosis in pollen mother cells. Is involved
CC in repair of double-strand DNA breaks (DSBs) induced by genotoxic
CC stresses, but does not seem to be required for the repair of meiotic
CC DSBs. {ECO:0000269|PubMed:19153602, ECO:0000269|PubMed:19812063}.
CC -!- SUBUNIT: Heterotrimer of RPA1, RPA2 and RPA3 (canonical replication
CC protein A complex) (By similarity). Interacts with RPA2A. {ECO:0000250,
CC ECO:0000269|PubMed:19812063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19153602}.
CC Note=Associated with meiotic chromosomes from leptotene through to
CC early pachytene.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SKI4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stalks and flower buds.
CC {ECO:0000269|PubMed:19812063}.
CC -!- INDUCTION: By the genotoxic agents methyl methanesulfonate (MMS) and
CC bleomycin. {ECO:0000269|PubMed:19812063}.
CC -!- DISRUPTION PHENOTYPE: There are differing accounts of the mutant
CC phenotypes. According to an early study with a limited number of
CC progeny from different sources (PubMed:15978034), it is embryonic
CC lethal when homozygous. However, a more recent study describes
CC homozygous lines that show normal vegetative growth, but reduced
CC fertility and meiotic defects (PubMed:19153602).
CC {ECO:0000269|PubMed:15978034, ECO:0000269|PubMed:19153602}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AC006420; AAD25150.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06010.1; -; Genomic_DNA.
DR EMBL; AK118699; BAC43293.1; -; mRNA.
DR EMBL; BT005946; AAO64881.1; -; mRNA.
DR PIR; B84478; B84478.
DR RefSeq; NP_178690.1; NM_126648.4. [Q9SKI4-1]
DR AlphaFoldDB; Q9SKI4; -.
DR SMR; Q9SKI4; -.
DR BioGRID; 604; 2.
DR IntAct; Q9SKI4; 1.
DR STRING; 3702.AT2G06510.1; -.
DR iPTMnet; Q9SKI4; -.
DR PaxDb; Q9SKI4; -.
DR ProteomicsDB; 236894; -. [Q9SKI4-1]
DR EnsemblPlants; AT2G06510.1; AT2G06510.1; AT2G06510. [Q9SKI4-1]
DR GeneID; 815209; -.
DR Gramene; AT2G06510.1; AT2G06510.1; AT2G06510. [Q9SKI4-1]
DR KEGG; ath:AT2G06510; -.
DR Araport; AT2G06510; -.
DR TAIR; locus:2054577; AT2G06510.
DR eggNOG; KOG0851; Eukaryota.
DR InParanoid; Q9SKI4; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q9SKI4; -.
DR PRO; PR:Q9SKI4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKI4; baseline and differential.
DR Genevisible; Q9SKI4; AT.
DR GO; GO:0000785; C:chromatin; IDA:TAIR.
DR GO; GO:0005662; C:DNA replication factor A complex; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0048232; P:male gamete generation; IMP:TAIR.
DR GO; GO:0007141; P:male meiosis I; IMP:TAIR.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IGI:TAIR.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IBA:GO_Central.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR CDD; cd04477; RPA1N; 1.
DR DisProt; DP01085; -.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR InterPro; IPR007199; Rep_factor-A_N.
DR InterPro; IPR031657; REPA_OB_2.
DR InterPro; IPR004591; Rfa1.
DR PANTHER; PTHR23273; PTHR23273; 1.
DR Pfam; PF04057; Rep-A_N; 1.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF16900; REPA_OB_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00617; rpa1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA recombination; DNA repair;
KW DNA replication; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..640
FT /note="Replication protein A 70 kDa DNA-binding subunit A"
FT /id="PRO_0000422615"
FT DNA_BIND 211..293
FT /note="OB"
FT ZN_FING 503..529
FT /note="C4-type"
FT /evidence="ECO:0000255"
SQ SEQUENCE 640 AA; 72243 MW; 96A941DDFE0B08A9 CRC64;
MPVSLTPNAI TAIHDGDVNL KPLLQVLEIK MIGRSQERSQ ERYRFLISDG VSAQHAMVAV
QLNDRVKSGQ FEKGSIVQLI DYICSDVKGR KLIVVLNMET IVQQSETIGN PTIFGETDTE
AQKTFSGTGN IPPPNRVVFN EPMVQHSVNR APPRGVNIQN QANNTPSFRP SVQPSYQPPA
SYRNHGPIMK NEAPARVIPI AALNPYQGRW AIKARVTAKG DIRRYNNAKG DGKVFSFDLL
DYDGGEIRVT CFNALVDRFY DVTEVGKVYL ISKGSLKPAQ KNFNHLKNEW EIFLESTSTV
ELCPDEDGSI PKQQFSFRPI SDIENAENNT ILDVIGVVTS VNPSVPILRK NGMETHRRIL
NLKDESGKAV EVTLWGEFCN RDGRQLEEMV DSAFHPVLAI KAGKVSDFSG KSVGTISSTQ
LFINPDFPEA HKLRTWFDYG GKDTASFSIS RDTMPGGVSR NEIRKNVSQI KEEGLGRSDK
PDWITVKATI SFIKTDSFCY TACPLMIGDK QCNKKVTRSG TNRWLCDRCN QESDECDYRY
LLQVQIQDHT GLTWITAFQE TGEEIMGCPA KKLYAMKYEL EKEEEFAEIV RDRLFHQYML
KLKIKEESYG DEQRVKMTVV KVDKVNYTSE SKYMLDLLVR
