ID   ATR_ARATH               Reviewed;        2702 AA.
AC   Q9FKS4; Q9MAZ4;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Serine/threonine-protein kinase ATR;
DE            Short=AtATR;
DE            EC=2.7.11.1;
DE   AltName: Full=Ataxia telangiectasia-mutated and Rad3-related homolog;
DE   AltName: Full=DNA repair protein ATR;
DE   AltName: Full=Rad3-like protein;
DE            Short=AtRAD3;
GN   Name=ATR; Synonyms=RAD3; OrderedLocusNames=At5g40820; ORFNames=MHK7.5;
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 mRNA for AtRAD3, complete cds.";
RL   Submitted (MAR-2000) 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   FUNCTION, AND INDUCTION.
RX   PubMed=15075397; DOI=10.1105/tpc.018903;
RA   Culligan K., Tissier A., Britt A.;
RT   "ATR regulates a G2-phase cell-cycle checkpoint in Arabidopsis thaliana.";
RL   Plant Cell 16:1091-1104(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=16166376; DOI=10.1101/gad.1333805;
RA   Vespa L., Couvillion M., Spangler E., Shippen D.E.;
RT   "ATM and ATR make distinct contributions to chromosome end protection and
RT   the maintenance of telomeric DNA in Arabidopsis.";
RL   Genes Dev. 19:2111-2115(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=15772150; DOI=10.1091/mbc.e04-10-0890;
RA   Friesner J.D., Liu B., Culligan K., Britt A.B.;
RT   "Ionizing radiation-dependent gamma-H2AX focus formation requires ataxia
RT   telangiectasia mutated and ataxia telangiectasia mutated and Rad3-
RT   related.";
RL   Mol. Biol. Cell 16:2566-2576(2005).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY 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: Probable serine/threonine kinase. Plays a central role in
CC       cell-cycle regulation by transmitting DNA damage signals to downstream
CC       effectors of cell-cycle progression. May recognize the substrate
CC       consensus sequence [ST]-Q and phosphorylate histone variant H2AX to
CC       form H2AXS139ph at sites of DNA damage, thereby regulating DNA damage
CC       response mechanism. Seems to be required for the G2-phase checkpoint in
CC       response to replication blocks but not absolutely required in the G2-
CC       arrest response to double-strand breaks. May also be involved in the
CC       meiosis process. Required for the basal expression of RNR1
CC       (ribonucleotide reductase large subunit). Acts in concert with
CC       telomerase to maintain telomeric DNA tracts. Not required for telomere
CC       length homeostasis. Required for effective immune responses that
CC       involve activation of DNA damage responses (PubMed:24207055).
CC       {ECO:0000269|PubMed:15075397, ECO:0000269|PubMed:15772150,
CC       ECO:0000269|PubMed:16166376, ECO:0000269|PubMed:24207055}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- INDUCTION: Strongly induced by replication blocking agents (UVB,
CC       aphidicolin and hydroxyurea) but only mildly induced by DNA damaging
CC       agents (gamma-radiation) (PubMed:15075397). Negatively regulated by the
CC       key immune regulator SNI1 (PubMed:24207055).
CC       {ECO:0000269|PubMed:15075397, 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   -!- MISCELLANEOUS: Loss-of-function mutations (T-DNA insertion) are
CC       hypersensitive to replication antagonists, including UV light,
CC       aphidicolin, and hydroxyurea, and are defective in G2 checkpoints
CC       induced by these agents.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11344.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB040133; BAA92828.1; -; mRNA.
DR   EMBL; AB011477; BAB11344.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94599.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM71086.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM71087.1; -; Genomic_DNA.
DR   RefSeq; NP_001332642.1; NM_001344357.1.
DR   RefSeq; NP_001332643.1; NM_001344356.1.
DR   RefSeq; NP_198898.2; NM_123447.3.
DR   STRING; 3702.AT5G40820.1; -.
DR   PaxDb; Q9FKS4; -.
DR   PRIDE; Q9FKS4; -.
DR   ProteomicsDB; 241008; -.
DR   EnsemblPlants; AT5G40820.1; AT5G40820.1; AT5G40820.
DR   EnsemblPlants; AT5G40820.3; AT5G40820.3; AT5G40820.
DR   EnsemblPlants; AT5G40820.4; AT5G40820.4; AT5G40820.
DR   GeneID; 834082; -.
DR   Gramene; AT5G40820.1; AT5G40820.1; AT5G40820.
DR   Gramene; AT5G40820.3; AT5G40820.3; AT5G40820.
DR   Gramene; AT5G40820.4; AT5G40820.4; AT5G40820.
DR   KEGG; ath:AT5G40820; -.
DR   Araport; AT5G40820; -.
DR   TAIR; locus:2164481; AT5G40820.
DR   eggNOG; KOG0890; Eukaryota.
DR   HOGENOM; CLU_000178_2_0_1; -.
DR   InParanoid; Q9FKS4; -.
DR   OMA; WWSYLPD; -.
DR   PhylomeDB; Q9FKS4; -.
DR   PRO; PR:Q9FKS4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FKS4; baseline and differential.
DR   Genevisible; Q9FKS4; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; 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; IGI:TAIR.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
DR   GO; GO:0051321; P:meiotic cell cycle; IGI:TAIR.
DR   GO; GO:0032504; P:multicellular organism reproduction; IGI:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0033044; P:regulation of chromosome organization; IGI:TAIR.
DR   GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR   GO; GO:0006282; P:regulation of DNA repair; IMP:UniProtKB.
DR   GO; GO:0032204; P:regulation of telomere maintenance; IGI:TAIR.
DR   GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:TAIR.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR   GO; GO:0043247; P:telomere maintenance in response to DNA damage; TAS:TAIR.
DR   GO; GO:0007004; P:telomere maintenance via telomerase; IMP:TAIR.
DR   Gene3D; 1.10.1070.11; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR012993; UME.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF08064; UME; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SMART; SM00802; UME; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; DNA damage; DNA repair; Kinase;
KW   Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..2702
FT                   /note="Serine/threonine-protein kinase ATR"
FT                   /id="PRO_0000088838"
FT   DOMAIN          1646..2255
FT                   /note="FAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT   DOMAIN          2366..2678
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   DOMAIN          2670..2702
FT                   /note="FATC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT                   ECO:0000255|PROSITE-ProRule:PRU00535"
FT   REGION          2372..2378
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2543..2551
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          2563..2587
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   CONFLICT        152..153
FT                   /note="AS -> GIH (in Ref. 1; BAA92828)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2702 AA;  302366 MW;  DCC88C59F50E23D3 CRC64;
     MAKDDNNLSS LVHELRERVA ASASTPANNL RHSSGDEDAL EIRFRAVIPN LLNTYVVPSL
     GNGREVTAVL KLVGHTARNI PGVFYHGTPS AILPVIARII PFFAEPEFVP GHGVLLETVG
     SLLMLLRSNS RKAYRIFFHD ALQAIQDMQP IASLHSIEPE VCESHIPFRC FCMSFSGIGG
     DLPDANKPRD GDGLVLNLLG ANRWQPFATC ILKLICKCLT EGTLYVQGLI HTSFFKAACS
     LVCCGGADVQ MACFEFATLV GSILTFNILP HVALIQSIIL LLSADEGLPV YRNTIYDSTI
     GRFLTAVYSS CSDAAVKLTA ESLVLVLSHA LQRTKSEELK ASLCSAYVRI VKSCPPCIWK
     IHCLLELLHL PEPCFQLIEC FKAVLIVLGP GCVRVETTKC GSHTSATSDR PVQGINAGKK
     RHIEDESTYK RKRQKVGDDI RRGVYFAPEF ADETDGKDAA SLREMLISTV ESLKPPPAGP
     SLSQTESSIV ALSMLTNAFC FCPWTDMTHR LFNQMYAWIP WIAGQVEETN PIMFDISIYL
     EGIHNLLLVG VDPQYEYTSK GNDLVAIQFL LKLPWTHYML FKTPSSLVKS KCLSVGIWTK
     LGLQDGSDFD IFSWSLSDDF EQVQAVAAIS MPLKVLFSGL GALLHMFPKL EHLLEEKELM
     IKKAIPQSLG FLSCLYGSST TDSEKTACHL LLHEDLKKDE TLNSLLQGFR CSKCDKFIER
     EDEKHFRIIE TPEMVKLKMD HHRDYFNLQS LYFNLLYDES SEETQLACVE VIRRILGHTS
     PDILVRTRSQ WIRCLQYLLV HVNTDVREAF CAQIGIFVQH PIVSCLFLSE DATEKSCERN
     FFNLIEHSLA AAKDLLVIQT LLETTAEVMV AVDVTSELFL ICLFLLIDQL DHPNLIVRIN
     ASKLINRSCY IHVKGGFATL LSTASHIQNE LFDNLSVRLT SRPNVVREFA EAVLGVETEE
     LVRKMVPAVL PKLLVYWQEN AQAANTLNEL AKLIDTDVVP LIVNWLPRVL AFALNQEEDK
     NLLSVLQLYH SQIGSDNQEI FAAALPALLD ELVCFVDIAD TPETDRRLQR LPDAIKKISK
     VLTNAEDLPG FLQNHFVGLL NSIDRKMLHA DDIFLQKQAL KRIKLLIEMM GHYLSTYVPK
     LMVLLMHAIE KDALQSEGLL VLHFFTRKLA DVSPSSIKYV ISQIFAALIP FLEKEKEGPH
     VYLDEVVKIL EELVLKNRDI VKEHICEFPL LPSIPSLGEL NNAIQEARGL MSLKDQLRDI
     VNGMKHENLN VRYMVACELS KLLYNRNEDV AALIAGELVS DMEILSSLIT YLLQGCAEES
     RTTVGQRLKL VCADCLGAIG AIDPAKVRVA SCSRFKIQCS DDDLIFELIH KHLARAFRAA
     QDTIIQDSAA LAIQELLKIA GCEPSLAGNV VVLTPQEHVQ VNVSGSRRCG GNNEVKDRGQ
     KLWDRFSNYV KELIAPCLTS RFQLPNVSDP GSAGPIYRPS MSFRRWLSYW IRKLTAFATG
     SRVSIFAACR GIVRHDMQTA TYLLPYLVLD VVCHGTEAAR LSISEEILSV LDAAASENSG
     VTINSFGVGQ SEVCVQAVFT LLDNLGQWVD DVKQGVALSS SLQSSGGRQV APKSKDQVSN
     STTEQDHLLV QCKYVLELLL AIPKVTLARA SFRCQAYARS LMYLESHVRG KSGSLNPAAE
     KTGIFENADV SSLMGIYSCL DEPDGLSGFA SLSKSLNLQD QLLINKKSGN WADVFTACEQ
     ALQMEPTSVQ RHSDVLNCLL NMCHHQTMVT HVDGLISRVP EYKKTWCTQG VQAAWRLGKW
     DLMDEYLDGA DAEGLLFSSS DSNASFDRDV AKILHAMMKK DQYSVAEGIA ISKQALIAPL
     AAAGMDSYTR AYPFVVKLHL LRELEDFQAV LNGDSYLEKS FSTSDQVFSK AVDNWENRLR
     FTQSSLWTRE PLLAFRRLVF GASGLGAQVG NCWLQYAKLC RLAGHYETAH RAILEAQASG
     APNVHMEKAK LLWITKRSDS AIIELQQSLL NMPEGVVDST VISSINSLLM APPNPEPTVR
     NTQSFKEKKD VAKTLLLYSK WIHHSGQKQK KDVLNLYTQV KELLPWEKGY FHLAKYYDEL
     YVDARKCQQE SSVFSSAGSK KGSVSSNLST EKAGWDYLFK GMYFYAKALH SGHKNLFQAL
     PRLLTLWFDF GTIYKTSGSA GNKELKSTHM KIMSLMRGCL KDLPTYQWLT VLPQLVSRIC
     HQNADTVLMV KNIITSVLHQ FPQQGLWIMA AVSKSTVPAR REAAAEIIQG ARKGFNQSDR
     GHNLFIQFAS LTDHFIKLCF HGGQPRSKVI NIATEFSALK RMMPLDIIMP IQQSLTISLP
     AFHMNNNERH SASVFSGSDL PTISGIADEA EILSSLQRPK KIILLGNDGI EYPFLCKPKD
     DLRKDARMME FTAMINRLLS KYPESRRRKL YIRTFAVAPL TEDCGLVEWV PHTRGLRHIL
     QDIYISCGKF DRQKTNPQIK RIYDQCAVKK EYEMLKTKIL PMFPPVFHKW FLTTFSEPAA
     WFRSRVAYAH TTAVWSMVGH IVGLGDRHGE NILFDSTSGD CVHVDFSCLF DKGLQLEKPE
     LVPFRLTQNM IDGLGITGYE GIFMRVCEIT LTVLRTHRET LMSILETFIH DPLVEWTKSH
     KSSGVEVQNP HAQRAISSIE ARLQGVVVGV PLPVEGQARR LIADAVSLEN LGKMYIWWMP
     WF