ID   RAD17_ARATH             Reviewed;         599 AA.
AC   Q9MBA3;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Cell cycle checkpoint protein RAD17 {ECO:0000303|Ref.1};
DE            Short=AtRAD17 {ECO:0000303|Ref.1};
DE   AltName: Full=Radiation-sensitive protein 17 {ECO:0000303|Ref.1};
GN   Name=RAD17 {ECO:0000303|Ref.1};
GN   OrderedLocusNames=At5g66130 {ECO:0000312|Araport:AT5G66130};
GN   ORFNames=K2A18.21 {ECO:0000312|EMBL:BAB10418.1};
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].
RC   STRAIN=cv. Columbia;
RA   Sugiyama H., Oguchi K., Tamura K., Takahashi H.;
RT   "Arabidopsis thaliana homolog of Schizosaccharomyces pombe rad17.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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   INDUCTION, AND FUNCTION.
RX   PubMed=15165187; DOI=10.1111/j.1365-313x.2004.02097.x;
RA   Heitzeberg F., Chen I.-P., Hartung F., Orel N., Angelis K.J., Puchta H.;
RT   "The Rad17 homologue of Arabidopsis is involved in the regulation of DNA
RT   damage repair and homologous recombination.";
RL   Plant J. 38:954-968(2004).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SNI1, AND INDUCTION BY
RP   SNI1.
RX   PubMed=24207055; DOI=10.1016/j.molcel.2013.09.019;
RA   Yan S., Wang W., Marques J., Mohan R., Saleh A., Durrant W.E., Song J.,
RA   Dong X.;
RT   "Salicylic acid activates DNA damage responses to potentiate plant
RT   immunity.";
RL   Mol. Cell 52:602-610(2013).
CC   -!- FUNCTION: Seems to be involved in regulation of DNA repair correlated
CC       to non-homologous double strand breaks (DSBs) repair. In vitro,
CC       involved in rapid but not in slow DSB repair mechanism. Required for
CC       effective immune responses that involve activation of DNA damage
CC       responses (PubMed:24207055). {ECO:0000269|PubMed:15165187,
CC       ECO:0000269|PubMed:24207055}.
CC   -!- SUBUNIT: Interacts with SNI1. {ECO:0000269|PubMed:24207055}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: By genotoxic stress and by DNA damage (PubMed:15165187).
CC       Negatively regulated by the key immune regulator SNI1
CC       (PubMed:24207055). {ECO:0000269|PubMed:15165187,
CC       ECO:0000269|PubMed:24207055}.
CC   -!- DISRUPTION PHENOTYPE: Suppressor of sni1 mutation symptoms including
CC       the accumulation of DNA damage leading to a constitutively activated
CC       DNA damage responses (DDR) and increased basal expression of
CC       pathogenesis-related (PR) genes. {ECO:0000269|PubMed:24207055}.
CC   -!- SIMILARITY: Belongs to the rad17/RAD24 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB030250; BAA90479.1; -; mRNA.
DR   EMBL; AB011474; BAB10418.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED98163.1; -; Genomic_DNA.
DR   RefSeq; NP_201414.1; NM_126011.2.
DR   AlphaFoldDB; Q9MBA3; -.
DR   BioGRID; 21987; 2.
DR   STRING; 3702.AT5G66130.1; -.
DR   iPTMnet; Q9MBA3; -.
DR   PaxDb; Q9MBA3; -.
DR   PRIDE; Q9MBA3; -.
DR   ProteomicsDB; 236306; -.
DR   EnsemblPlants; AT5G66130.1; AT5G66130.1; AT5G66130.
DR   GeneID; 836745; -.
DR   Gramene; AT5G66130.1; AT5G66130.1; AT5G66130.
DR   KEGG; ath:AT5G66130; -.
DR   Araport; AT5G66130; -.
DR   TAIR; locus:2156952; AT5G66130.
DR   eggNOG; KOG1970; Eukaryota.
DR   HOGENOM; CLU_018598_2_0_1; -.
DR   InParanoid; Q9MBA3; -.
DR   OMA; GLRVQEW; -.
DR   OrthoDB; 674169at2759; -.
DR   PhylomeDB; Q9MBA3; -.
DR   PRO; PR:Q9MBA3; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9MBA3; baseline and differential.
DR   Genevisible; Q9MBA3; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR   GO; GO:0006282; P:regulation of DNA repair; IMP:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12172; PTHR12172; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; DNA damage; Nucleotide-binding; Nucleus;
KW   Plant defense; Reference proteome.
FT   CHAIN           1..599
FT                   /note="Cell cycle checkpoint protein RAD17"
FT                   /id="PRO_0000209951"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..599
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139..146
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   599 AA;  66819 MW;  FC65E30F0CE7B18A CRC64;
     MLKKKLSLED EDDDRSYNLR SSRSNAKSKP RSSAGTATNP RASKRARLSG ASATQEDSSL
     VDKIRLSFED FDEALSGFKV SSGYERSKNT DLWVDKYRPR TLEELSVHKK KVDEVKLWFQ
     ESLDFLKNGL RNNVLLVTGQ AGVGKSATIH LITSILGVTV HEWNAPIPTI WQEHVHNTSS
     GLKYTSKLDE FENFVESTRK YGVMASSSTD GIKAPVVLLI DDLPLANGRH AFERLQNCLL
     LLVKSTQIPT VILITDHNNA DSSDQTARRM EDTQSSLERA GALKVAFNPI TKNSIKKVLQ
     RICREEHCKV TTMEIDQMAT ASGGDIRHAI TSLQLFSVKP ELNHTKIKSP RPGMEDNYHG
     NEQTMYSGLD SGISSCFGRD ETLSLFHALG KFLHNKRETD NVIISECSSS LVHDEFARLP
     LKMDAPEKVL SQAHGQAGRV VDFLHENVLD FVSDGAIEDA WCVSSYLADA DLLLADIRGK
     MSGHNNTEDV PQSAGASVAV RGVLYGNKQP CSSRWHVIRK PKLWQVEQSS IQTKKNLREQ
     RNISYEGSRV ADISVMATEY SPVLKWLSYR ASPDAFPGMG EETDEEDSDI SEDDEIQDW