ID ATM_CAEEL Reviewed; 2378 AA.
AC Q9N3Q4; V6CJ63; V6CKB4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 27-MAR-2024, entry version 162.
DE RecName: Full=Serine/threonine-protein kinase ATM {ECO:0000250|UniProtKB:Q13315};
DE EC=2.7.11.1;
GN Name=atm-1; ORFNames=Y48G1BL.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=16824923; DOI=10.1016/j.cub.2006.05.047;
RA van Haaften G., Romeijn R., Pothof J., Koole W., Mullenders L.H.,
RA Pastink A., Plasterk R.H., Tijsterman M.;
RT "Identification of conserved pathways of DNA-damage response and radiation
RT protection by genome-wide RNAi.";
RL Curr. Biol. 16:1344-1350(2006).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17347667; DOI=10.1038/sj.cdd.4402115;
RA Stergiou L., Doukoumetzidis K., Sendoel A., Hengartner M.O.;
RT "The nucleotide excision repair pathway is required for UV-C-induced
RT apoptosis in Caenorhabditis elegans.";
RL Cell Death Differ. 14:1129-1138(2007).
RN [4]
RP REVISION OF GENE MODEL, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22350747; DOI=10.1007/s00438-012-0681-0;
RA Jones M.R., Huang J.C., Chua S.Y., Baillie D.L., Rose A.M.;
RT "The atm-1 gene is required for genome stability in Caenorhabditis
RT elegans.";
RL Mol. Genet. Genomics 287:325-335(2012).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling in the presence of DNA double strand breaks (DSBs) and other
CC forms of DNA damage induced by ionizing radiation and other genotoxic
CC stresses such as UV. Plays a role in maintaining genome stability.
CC {ECO:0000269|PubMed:16824923, ECO:0000269|PubMed:17347667,
CC ECO:0000269|PubMed:22350747}.
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 Evidence={ECO:0000250|UniProtKB:Q13315};
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; Evidence={ECO:0000250|UniProtKB:Q13315};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13315}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9N3Q4-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9N3Q4-2; Sequence=VSP_055333;
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to ionizing radiation with
CC reduced survival compared to wild-type animals. Loss of induction of
CC apoptosis following UV-C or ionizing radiation treatment but no effect
CC on apoptotic response induced by X-ray exposure. Low brood size,
CC reduced viability and sterility, appearance of a high-incidence-of-
CC males (Him) phenotype, and reduced chromosome number due to chromosome
CC fusions. {ECO:0000269|PubMed:17347667, ECO:0000269|PubMed:22350747}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000255}.
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DR EMBL; FO081620; CDK13475.1; -; Genomic_DNA.
DR EMBL; FO081456; CDK13475.1; JOINED; Genomic_DNA.
DR EMBL; FO081488; CDK13475.1; JOINED; Genomic_DNA.
DR EMBL; FO081620; CDK13476.1; -; Genomic_DNA.
DR EMBL; FO081488; CDK13476.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001293214.1; NM_001306285.1. [Q9N3Q4-1]
DR RefSeq; NP_001293215.1; NM_001306286.1. [Q9N3Q4-2]
DR AlphaFoldDB; Q9N3Q4; -.
DR SMR; Q9N3Q4; -.
DR STRING; 6239.Y48G1BL.2a.1; -.
DR EPD; Q9N3Q4; -.
DR PaxDb; 6239-Y48G1BL-2; -.
DR EnsemblMetazoa; Y48G1BL.2a.1; Y48G1BL.2a.1; WBGene00000227. [Q9N3Q4-1]
DR EnsemblMetazoa; Y48G1BL.2b.1; Y48G1BL.2b.1; WBGene00000227. [Q9N3Q4-2]
DR GeneID; 3565793; -.
DR KEGG; cel:CELE_Y48G1BL.2; -.
DR UCSC; Y48G1BL.2; c. elegans. [Q9N3Q4-1]
DR AGR; WB:WBGene00000227; -.
DR WormBase; Y48G1BL.2a; CE49304; WBGene00000227; atm-1. [Q9N3Q4-1]
DR WormBase; Y48G1BL.2b; CE49311; WBGene00000227; atm-1. [Q9N3Q4-2]
DR eggNOG; KOG0892; Eukaryota.
DR InParanoid; Q9N3Q4; -.
DR OMA; ATIPNMV; -.
DR OrthoDB; 8448at2759; -.
DR PRO; PR:Q9N3Q4; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000227; Expressed in embryo and 3 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:UniProtKB.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR038980; ATM_plant.
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; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Cell cycle; DNA damage; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2378
FT /note="Serine/threonine-protein kinase ATM"
FT /id="PRO_0000396514"
FT DOMAIN 1415..1937
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2044..2366
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2346..2378
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2050..2056
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2218..2226
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2238..2263
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT VAR_SEQ 1..677
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_055333"
SQ SEQUENCE 2378 AA; 273957 MW; BB646EBBB3B1D8E2 CRC64;
MSVTQLKNLK HAIAQLLEWD GTKTARKKIV DEVVLLYHAL GAEALSEDNQ EIYDLYDLSA
RIFNLAKKEI EEANQQFEKE RKKGTRRSEK PVPTPLFELS IQHLKRCCQQ GIDHNQVPWI
AYCLKLLEFP ITITEKSIEN EISNVLLLSS NASQLHWAEH AHLSSLWKWI WSRVETADIG
ALAMRNYMEL AANLLENVDY VVFEKSPIDL MAKVMGTLKK SVEMGNPKEY WCHYRKFSVV
HILSYIVHRW GLEARDFILR EIFELTGSLS NLISVAHKDG EQSKKCIMRL IDDLVKLAMI
ETVHGHRTMN EVTRGNIQKL VKTGIQESLK SAHRNFSRSS TFSISEECVR YLTRWLLAER
RLEQPSAAMN ESFELTGDSS SKKKDDATFD SLIDLSFGST ISGKHKLNAW NGVMQILNEL
LKSRRLELQV TEKIVTILWE KRKSYTTEPL RTVFCSILST VVCQADVRFG HRKVPTIDSI
LKYSLSLMPN VASLPSAAAL TETIVRFRTV SREGLRNTWD TVSRTSSGSF EVVRLISALI
SVTEFDENSR FANDERVRSW SFRKDIIEWV LLDPNAHSHK LLYQLCQYHP TYCYESEASS
SDDSLLQTLK LCKLACSPAP PSAPKALRPL EASIEEIVRY VHDKLKSILA TEITLPAFVL
CHEFALKYPD RSYEFNKMYK KLYQIMEDQE EDEFLQSARH FSKWPQNLTL PIQKQTINCM
AVFFEANLDN QLVDLCQWSD RRKVLVEMLA ELAATRSEIR DKLQKSMPFN KFVKECIMEN
RGDLYEMTKR FEKYSFLLSI RNLIVTRMII TNEAARLLGD GETISETDIF IIEKRTLSTC
IRNVSEGKEL SGYTLDPYTV AANVHNVHFD HINVEIYLEL LKKSPFFAQN IVRHLLRQNG
KEAEEETWHL HATVLKIVMK DEKLLAVCVA TIPNMVRYLK VYQIHFSPKS NAAKFLHLDM
ESISHCQSYL RKPTKSSNLI TAANFLTLFG CEKRTWKRPI LRFWSIFKQQ PAMCCEKLLI
FAEECVELGL NHRIACLLRA LTTSEFCRKA LCDEYLKIAF QLTYRSIFLI LSKNECRPEI
VELCDDMNLR YDLLQHQIKH VAAHHLEHFE RFETKIAFSV EKFLKSGIDG IDFEDLGLVE
FYKQLNENLT EDAIRSNEAR NIYIVDILST IWLQLPSIRP QILPILARFK HISPAWTNFP
QPPHISTNEK SFLQHLRFHL YLKMMNISKS MTQGEYATCI MMLLTSYDSS HFVADLIEKK
QLGKLKLQQR RNVLCILSRL LKDQAVMGDE DETIIDPILF KAITKASAVF EDTAACIVPF
LFKICVDFKG KYDKCVINLL GCLKGVNAED EIVVRCLAEC VDSIGLNVIA RYERLNIETH
SEFGVKWFFK LSRLFLKHGF TTHSFAIANI LFDRLSARKR NTMMIDRTSL DRIDRSQELI
NLLVEIYVAE GNSVALSSLP PAVQNRPDVR QVMNKSSKEW LKLLSSNQMD SWELTIVQWM
CGIQFNAITG DKYLNSILRC NFNEYTKKID SPLKFVYFQL FHLSTSTLEI EEAISSMPLA
PTIDQMRLMI IANATASFEP QSVEEHVVRA VRELRETSNR RKSGGNVKGI NEKTTRMVKL
AEMLTENKAY DAAINLLDTW EHECLQWTSV AAESIDIDLI RICKQHVTCR SGDPRMADIN
LRTMHPRVPV MSDLAIAEWS LALSKITIEY RNDMEEGIRI LEFGCKHLQN KDSVETRLKV
LLKLHSVCIG QLSKLEEYRE TRTYRMKQQA VTAFEQQIQN SCRTSLARGN SGDEWTKKTV
QRVRKEHQFE KNDLEKVDNS LNSAARKAVS SGFDALLCIS QLEDDDEAIR ASSLIIFPLI
DVIYKYETDV GVIALLKEHT KSKLPSKLWI SATSHIASKC FSIEKSQITR HLSQILCHLI
YDYPYHVLHT ILMYDDEKNA SKVKGFLKTI FDARADQRDS SKLKEIVITI REAHQAYREI
AMLDVRGNVR IQRVEINGKT MYRWPHDLKI FKCKLRQLPI PTISQKIGCP GDYSTTDLIT
WKRWKDVFTI ADGISTPKIW EIEGSDGKWY KTVWKKDDVR QDVLVEQMFD VTNNMLEKAM
LRTYNVVPLD TECGVIEFCG GTVSLKEVMC GVTREGGLHR EFNSEEVSAS KVSSMMRQVQ
TESTETRRQV FVEICQQYSP VFRHFFYTNF STAQIWRQKI INYRQSLATW SIVCYIVGLG
DRHASNILFD QKLCTFVHID LGMILEYSKR TLPVPEQVPF RITRDVLDPI LIEGIENGQL
AEECTQIMEK LKENGKVILG VASALLRETM TNFREAEQAA GRPSYISEMA IGRLREKLRG
TDDGVTAQSS NLQIRRLLRE ATSADNLSRM FCGWMPFL
//
