RFC1_ARATH
ID RFC1_ARATH Reviewed; 956 AA.
AC Q9C587;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Replication factor C subunit 1;
DE Short=AtRFC1;
DE AltName: Full=Activator 1 large subunit;
DE AltName: Full=Activator 1 subunit 1;
GN Name=RFC1; OrderedLocusNames=At5g22010; ORFNames=T6G21;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17556804;
RA Xia S.T., Xiao L.T., Bi D.L., Zhu Z.H.;
RT "Arabidopsis replication factor C subunit 1 plays an important role in
RT embryogenesis.";
RL Zhi Wu Sheng Li Yu Fen Zi Sheng Wu Xue Xue Bao 33:179-187(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=20639449; DOI=10.1105/tpc.110.076349;
RA Liu Q., Wang J., Miki D., Xia R., Yu W., He J., Zheng Z., Zhu J.K.,
RA Gong Z.;
RT "DNA replication factor C1 mediates genomic stability and transcriptional
RT gene silencing in Arabidopsis.";
RL Plant Cell 22:2336-2352(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22974522; DOI=10.1111/tpj.12024;
RA Liu Y., Deng Y., Li G., Zhao J.;
RT "Replication factor C1 (RFC1) is required for double-strand break repair
RT during meiotic homologous recombination in Arabidopsis.";
RL Plant J. 73:154-165(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23144629; DOI=10.1371/journal.pgen.1003039;
RA Wang Y., Cheng Z., Huang J., Shi Q., Hong Y., Copenhaver G.P., Gong Z.,
RA Ma H.;
RT "The DNA replication factor RFC1 is required for interference-sensitive
RT meiotic crossovers in Arabidopsis thaliana.";
RL PLoS Genet. 8:E1003039-E1003039(2012).
CC -!- FUNCTION: Plays a role as mediator of transcriptional gene silencing
CC (TGS), DNA replication, DNA repair, hypersensitive response (HR) and
CC telomere length regulation. Is required in meiosis for DNA double-
CC strand break (DSB) repair during meiotic homologous recombination. May
CC participate in the RAD51-mediated recombination intermediate repair
CC process. Is important for lagging strand synthesis. Promotes meiotic
CC recombination via a specific pathway for crossovers (COs) that involves
CC the formation of double Holliday Junction (dHJ) intermediates.
CC {ECO:0000269|PubMed:17556804, ECO:0000269|PubMed:20639449,
CC ECO:0000269|PubMed:22974522, ECO:0000269|PubMed:23144629}.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex with RFC1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20639449,
CC ECO:0000269|PubMed:22974522}. Note=Localizes to the chromosomes during
CC zygotene and pachytene.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in flowers and siliques,
CC and at lower levels in roots, stems and leaves.
CC {ECO:0000269|PubMed:20639449, ECO:0000269|PubMed:22974522}.
CC -!- DISRUPTION PHENOTYPE: The rfc1-1 EMS mutants show reduced plant growth
CC and organ size, and early flowering (PubMed:20639449). The rfc1-2 T-DNA
CC mutants have normal vegetative growth, but have greatly reduced
CC fertility due to a meiotic defect and produce short seed pods with very
CC few seeds (PubMed:23144629). The rfc1-3 T-DNA mutant is embryonic
CC lethal when homozygous (PubMed:23144629). {ECO:0000269|PubMed:17556804,
CC ECO:0000269|PubMed:20639449, ECO:0000269|PubMed:22974522,
CC ECO:0000269|PubMed:23144629}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000305}.
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DR EMBL; AL589883; CAC34494.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92968.1; -; Genomic_DNA.
DR EMBL; BT014965; AAT47816.1; -; mRNA.
DR RefSeq; NP_680188.1; NM_147883.6.
DR AlphaFoldDB; Q9C587; -.
DR SMR; Q9C587; -.
DR STRING; 3702.AT5G22010.1; -.
DR iPTMnet; Q9C587; -.
DR PaxDb; Q9C587; -.
DR PRIDE; Q9C587; -.
DR ProteomicsDB; 236216; -.
DR EnsemblPlants; AT5G22010.1; AT5G22010.1; AT5G22010.
DR GeneID; 832261; -.
DR Gramene; AT5G22010.1; AT5G22010.1; AT5G22010.
DR KEGG; ath:AT5G22010; -.
DR Araport; AT5G22010; -.
DR TAIR; locus:504956441; AT5G22010.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_003574_4_0_1; -.
DR InParanoid; Q9C587; -.
DR OMA; PVGAENC; -.
DR OrthoDB; 307415at2759; -.
DR PhylomeDB; Q9C587; -.
DR PRO; PR:Q9C587; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C587; baseline and differential.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:TAIR.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IMP:TAIR.
DR GO; GO:0000003; P:reproduction; IMP:TAIR.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:TAIR.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF48019; SSF48019; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW DNA-binding; Meiosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..956
FT /note="Replication factor C subunit 1"
FT /id="PRO_0000422629"
FT DOMAIN 202..292
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..893
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 399..406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 956 AA; 104378 MW; 955E2C3DB562088B CRC64;
MSDIRKWFMK AHEKGNGSAP KSTSSKAGPV KNAAETAPIK SEQASEDLET ADRRKTSKYF
GKDKTKVKDE KEVEAIPAKR KLKTESDDLV KPRPRKVTKV VDDDDDDFDV PISRKTRDTT
PSKKLKSGSG RGIASKTVDN DDDDDGEDKE TPLKSAGRGR GGRAAPGAST GGRGRGGGRG
GFMNFGERKD PPHKGEKEVP EGTPDCLAGL TFVISGTLDS LEREEAEDLI KRHGGRITGS
VSKKTTYLLC DEDIGGRKSE KAKELGTKFL TEDGLFDIIR SSKPVKKSLP ERSNKGTEKI
CAPPKTSPQK EETRGKPLAK SSPKKVPPAK GKNKIIETSL PWTEKYRPKV PNEIVGNQSL
VTQLHNWLSH WHDQFGGTGS KGKGKKLNDA GSKKAVLLSG TPGIGKTTSA KLVSQMLGFQ
AVEVNASDSR GKANSNIAKG IGGSNANSVK ELVNNEAMAA NFDRSKHPKT VLIMDEVDGM
SAGDRGGVAD LIASIKISKI PIICICNDRY SQKLKSLVNY CLPLNYRKPT KQQMAKRLMH
IAKAEGLEIN EIALEELAER VNGDIRLAVN QLQYMSLSMS VIKYDDIRQR LLSSAKDEDI
SPFTAVDKLF GYNGGKLRMD ERIDLSMSDP DLVPLLIQEN YLNYRPSGKD EAKRMDLLAR
AAESIADGDI INVQIRRYRQ WQLSQSCCVA SSILPASLLH GSREVLEQGE RNFNRFGGWL
GKNSTAGKNR RLMEDLHVHV LASRESSAGR ETLRVDYLPL LLSRLTSPLQ TLPKDEAVSE
VVDFMNSYSI SQEDFDTILE LGKFKGRENP MEGVPPPVKA ALTKKYNEMN KTRMVRVADM
VQLPGVKKAP KKRIAAMLEP TVDSLRDEDG EPLADNEEGN GSDAEEDSEE ATDGEKLESN
LKNLNARGIQ VELDLKGAGS SGSRKAAGKG RGRGKAADTS AEKKATGRGS GAKRKR
