RFA1_DANRE
ID RFA1_DANRE Reviewed; 601 AA.
AC Q6NY74;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Replication protein A 70 kDa DNA-binding subunit;
DE Short=RP-A p70;
DE AltName: Full=Replication factor A protein 1;
DE Short=RF-A protein 1;
GN Name=rpa1; ORFNames=wu:fi14b08;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: As part of the heterotrimeric replication protein A complex
CC (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates,
CC that form during DNA replication or upon DNA stress. It prevents their
CC reannealing and in parallel, recruits and activates different proteins
CC and complexes involved in DNA metabolism. Thereby, it plays an
CC essential role both in DNA replication and the cellular response to DNA
CC damage. {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBUNIT: Component of the heterotrimeric canonical replication protein
CC A complex (RPA). {ECO:0000250|UniProtKB:P27694}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus,
CC PML body {ECO:0000250|UniProtKB:P27694}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AY648787; AAT68105.1; -; mRNA.
DR EMBL; BC066711; AAH66711.1; -; mRNA.
DR RefSeq; NP_956105.2; NM_199811.2.
DR AlphaFoldDB; Q6NY74; -.
DR SMR; Q6NY74; -.
DR STRING; 7955.ENSDARP00000029067; -.
DR iPTMnet; Q6NY74; -.
DR PaxDb; Q6NY74; -.
DR PRIDE; Q6NY74; -.
DR Ensembl; ENSDART00000032880; ENSDARP00000029067; ENSDARG00000003938.
DR GeneID; 327491; -.
DR KEGG; dre:327491; -.
DR CTD; 6117; -.
DR ZFIN; ZDB-GENE-030912-3; rpa1.
DR eggNOG; KOG0851; Eukaryota.
DR GeneTree; ENSGT00390000012403; -.
DR HOGENOM; CLU_012393_2_1_1; -.
DR InParanoid; Q6NY74; -.
DR OMA; VRVTIWG; -.
DR OrthoDB; 1189265at2759; -.
DR PhylomeDB; Q6NY74; -.
DR TreeFam; TF105241; -.
DR Reactome; R-DRE-110312; Translesion synthesis by REV1.
DR Reactome; R-DRE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-DRE-110320; Translesion Synthesis by POLH.
DR Reactome; R-DRE-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-DRE-176187; Activation of ATR in response to replication stress.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DRE-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR Reactome; R-DRE-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-DRE-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DRE-5655862; Translesion synthesis by POLK.
DR Reactome; R-DRE-5656121; Translesion synthesis by POLI.
DR Reactome; R-DRE-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DRE-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-DRE-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DRE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DRE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-DRE-5696400; Dual Incision in GG-NER.
DR Reactome; R-DRE-6782135; Dual incision in TC-NER.
DR Reactome; R-DRE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DRE-6783310; Fanconi Anemia Pathway.
DR Reactome; R-DRE-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DRE-68962; Activation of the pre-replicative complex.
DR Reactome; R-DRE-69166; Removal of the Flap Intermediate.
DR Reactome; R-DRE-69473; G2/M DNA damage checkpoint.
DR PRO; PR:Q6NY74; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 15.
DR Bgee; ENSDARG00000003938; Expressed in testis and 31 other tissues.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
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:0007507; P:heart development; IMP:ZFIN.
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:0034502; P:protein localization to chromosome; ISS:UniProtKB.
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 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 DNA replication; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..601
FT /note="Replication protein A 70 kDa DNA-binding subunit"
FT /id="PRO_0000097265"
FT DNA_BIND 184..268
FT /note="OB"
FT REGION 107..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 601 AA; 66631 MW; 420CA417C5E3981B CRC64;
MTVRLSEGAI ESLSKGTEVN NPILQCVNIR KIDGGNGVSR FRVMMSDGLH TMSSFMLSTQ
LNPMAEQNQL ATNCVCVLKR SVTNVLKDGR RVVVILDIEV LKSADQMPGK IGDPTPYVEG
QSKAPSTAPA PTARPLQPQN GSDGSTYRPS AQSFGKKPMA APNTPGGSSK VVPIASLNPY
QSKWTIRARV TNKSAIRTWS NSRGDGKLFS MELVDESGEI RATGFNNEVD KFFSLIEQGK
VFYISKGTLK IANKQFSSLK NDYEMTLNGE TSIIPCEDSN DVPMLQCDFV SIADLESREK
DTILDVIGVC KNAEDVARIM TKNSREVSKR NIQLIDMSGR VIQLTMWGSD AETFDGSGQP
ILAIKGARLS DFGGRSLSTL YSSTVMINPD IPEAYKLRGW YDKEGHALDG QSMTELRGPG
GGGNTNWKTL AEVKNEHLGH GDKADYFSCI ATIVYIRKEN CLYQACPSKD CNKKVVDQQN
GMFRCEKCDK EFPDFKYRLM LSANIADFGD NQWVTCFQDT AETLLGQNSS YLGQLKDTNE
AAFDEVFQHA NFNTFVFRNR VKLETYNDES RIKVTVVDAK PVDHREYSKR LIINIRKLAA
Q
