ID A0A8C7HIH2_ONCKI Unreviewed; 3003 AA.
AC A0A8C7HIH2;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU365027};
GN Name=ATM {ECO:0000313|Ensembl:ENSOKIP00005058199.1};
GN Synonyms=atm {ECO:0000313|Ensembl:ENSOKIP00005058199.1};
OS Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8019 {ECO:0000313|Ensembl:ENSOKIP00005058199.1, ECO:0000313|Proteomes:UP000694557};
RN [1] {ECO:0000313|Ensembl:ENSOKIP00005058199.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOKIP00005058199.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:0000256|ARBA:ARBA00048977};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000256|ARBA:ARBA00048977};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899,
CC ECO:0000256|RuleBase:RU365027};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasmic vesicle
CC {ECO:0000256|ARBA:ARBA00004541}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
CC Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000256|ARBA:ARBA00010769, ECO:0000256|RuleBase:RU365027}.
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DR Ensembl; ENSOKIT00005061867.1; ENSOKIP00005058199.1; ENSOKIG00005024860.1.
DR GeneTree; ENSGT00670000098061; -.
DR Proteomes; UP000694557; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-ARBA.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:1901701; P:cellular response to oxygen-containing compound; IEA:UniProtKB-ARBA.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:UniProtKB-ARBA.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-ARBA.
DR GO; GO:0007127; P:meiosis I; IEA:UniProtKB-ARBA.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IEA:UniProtKB-ARBA.
DR GO; GO:0010557; P:positive regulation of macromolecule biosynthetic process; IEA:UniProtKB-ARBA.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IEA:UniProtKB-ARBA.
DR GO; GO:1904358; P:positive regulation of telomere maintenance via telomere lengthening; IEA:UniProtKB-ARBA.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:UniProtKB-ARBA.
DR GO; GO:0010506; P:regulation of autophagy; IEA:UniProtKB-ARBA.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-ARBA.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; IEA:UniProtKB-ARBA.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:UniProtKB-ARBA.
DR CDD; cd05171; PIKKc_ATM; 1.
DR FunFam; 1.10.1070.11:FF:000011; Serine-protein kinase ATM; 1.
DR FunFam; 3.30.1010.10:FF:000015; Serine-protein kinase ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 1.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR021668; TAN.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF11640; TAN; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01342; TAN; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365027};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU365027};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU365027};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365027};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000694557};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1904..2521
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2634..2949
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2971..3003
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 3003 AA; 338884 MW; 61C48E3758FA4ECE CRC64;
MSLVLHELLV CCRGLENDKA TERKKEADRF RQLIRSPDTV KELDHISGTR AAKSSKQLTW
NAVFRFLQKY LQKETELLQS GKANVSATTQ ANRQKKMQEI SSLVKYFIRC ANKRGPRLNC
GELLNHVMEV LRSSFSCLAY GEDYSSILLK NILSVRKYWC DITQQQWHNL LDLYCGLFTG
SSKAINRVLV SRIIHTAVQG CCLQTEGFSH TLFSFFSRAL LNARQERHLA VVEHLVSALN
VFLRSAAMNC RMRVCRLGEE LLPSVLYVWT QMRPSTTLKE EIVEFFNLQL CVHHPKGSKT
QDTGAYAEDW VKWQSLLYNL YDALVSEISQ IGSRGKYATG SRHIAVKENL MELTAEICHQ
LFSEDCNFQM LEVTQAHLRA TQRGSPHGTP SKRRRIDLGW EVLRDHLQPH HSDFDVIPWL
QITSVLTSKY PSMVPGQELV PLLSVLCQLL GEQRRGDRGP YVLRCLREVA RCQATHPERA
QSYRAELGRL WGRVWALALR GVSSPQTEAL SLALLSTILQ GAFIPIDREL WKLFSGSACK
PSDAAALCLA QALLKCPVLK SLGTGWDHAG AVEGVGPPSL KENIISWLLM NEQSEEAEES
SRPHPVICRW AVYHWAYIAF LFTLLVLSKS NQILLVTCAK YNRCRPYAVM QEQAQVEVKG
SLSEIESMYL QFSFDEMPSN PMAKVMVSSA GTQLTVVPSL KHKLEQGLLS VADHLLNCYS
PDSQTTPPEC LVRCSSLLTG VLAGYVSTGL LTEEEACHSQ LFLKAKALVQ DFSEYISNVK
VKMAEDGTMT TLRSVMRLCT QCVNRGVKIF PARLLTELAE ICKLLVSHGE GLADDNQTRH
CPPCISRNQP VTRWSFKYSY LLLDAKSLLA EEHLAQQDLA ILASLEFLSL CVSAEFIHGL
SFKPVEVRRR LLLMLEQIDC TKPLHLNMYL VLLKKLPAED TSLAAEEFDS LLRPLADLCS
LYRQDQEVCA AVLLGLLPSI RSLGRTQDQH NDMRHVQGAL IQVVSGFWSA PKTGKCTAIV
KVALIHCLLA LLEADPCCKW AVLTLREEEL PVSVILPSHL SDSHHHVRML AAMTVERLVF
TDRTLSHQKM LPLKCQQTAF ENVYLKAQEG MRLQNSSPED LSDETFNRKA TLLKSLSVVL
CCSPVCEKQS LFALFQSYKE NNIEEPLIKK VLGSVSRALG YRSVEGFVSS HLDYLVAEWL
GQHGYTLESF PYTLLNHATL KDFYSSSYQV LIPHLVFLDD FKQVKSISTL LGKDWKKLLA
NCFPKIMVNI LPYFAMSGQD AQVARQREKA HRVYDLLKDS NCLGKPQIDS LIHSNLSDIV
VELLMTLYEG AATEEGGRGD LRRFIGELDP APNPPYFSSY VIKATLDYLS SCHSANLKSL
VAILSKTPIS IQRILLAVCQ KAAETINAYE RHRILLMYHL FVSLLLKEVK DGLGGAWAFV
LRDIIYTLIH HINSRLGVNL DEVSSRSFSL CCDLLTSVCR TAVQFCDDAV ESHLQVIVGT
LTAQVTTQLA ISQQVLSLLK FLVVESQDKL KSAIQKLEPF PDRPEFRELR AVQHTLKYST
GKFTLRQEIA HFLSVASCDS LPLTRLEGLK DLRRQLHNNK SQIRPLLRES DPAESVLVLL
VLNLLQLCKL AANHPGGRDI LEAAGSCLGE LGPVDFSTIA LLHGKDQLNA RAVSLFPSVE
PQWLYITLNC INNALTHHCI EVRQAAVQSL KGILATQAGA DFWEIHKDNR DPMLAYLNPF
RSTKKKEVSL VARERLESQD LWVPEAGGHK AWLKMLCMVL LDSGGVRSEA LLLSRPLCLV
KTDFCHRVLP LIIHDILLGD SDGSWRKLLS THIQDFFTSC FSRARASSRS TTPLLSDSES
DISDQGLLDK ASLRTMLSVI NYLRQQQRPL GSDRFVDAFL NYLEVARAAQ SCSAHFTALL
YSEIYVDKIK TNMEENHRIT FDESSQNFTI SSLTEESVKD TGISLQDLLI EVYRSIGEPD
SLYGCEGGKM TSALTRIRTY EHEAMWGKAL TSYDLHSNLP DGTRQVGIVE GLQNIGLSSI
LATYLRGLES EGVEWGAELR ELRFQAAWRN MQWDCDLSER VPESVFCSLQ ALRDKEFSTF
DQTLKYARGN EVEELCKGSL EAVSSLYPAL RNLQRISELE SIRQLFSKPL TDVGLAEVCS
HWQQHSQLLV DSDFTLVEPI LALRSVAQET LISQERDPEK NKYLSTVLTS HLMELCQLAR
AAGNTQLAER AVFQMKQHGG GGGRGSTASS WQLEEAQVFW AKGEQGLALG LLRQMIHTLE
DILHHFKDKL VNVNPALVPV FTECLRLCGN WLAETCLESP GVILEKYLER VKLRTQAFLS
LARFSDAQYQ GIDNYMKSSE FENKQALLEK AKEEVDLMRE RKVGKNRYTV KVQRELELDE
RALSNLQADR RRFLCKAVEN YIHCLEQGEE HDTWVFRLAS LWLENADVKT VNDMMKGGVN
RIPSYKFLPL MYQLAARMGT KMSATVAEDV GFYGVLNELI CLSCLEHPHH TLFIILALVN
ANKDESFSRS RLSKSTPRHS SQLDLERSEV AQGIMKKIRK KRAQMIRGIE VLCDAYITLA
YMDASRHKTE KTILIPSDQP IMQIKNLDDV IIPTMEIKVD PSGKYDNLVT IKSFKPHFHL
AGGVNLPKII DCVGSDGKIR RQLVKGQDDL RQDAVMQQVF HMCSMLLQRN TETRKRKLNI
RRYKVVPFSQ RSGVLEWCSG TVPIGDFLID PQKGAHTRFC PQDWTSITCR KKMMESQRLG
SGGKTQAFSE VCQNFRPVFR YFCMERFLDP AVWLEKRLAY TRSVATSSIV GYIVGLGDRH
IQNILIDEQT AELVHIDLGV AFEQGKILPT PETVPFRLSR DIVDGMGITG VEGVFRRCCE
KTMEVMRCSQ EALLTIVEVL LYDPLFDWTM NPLKAFYLQQ QHDEQAELQS TPSVEDQRGR
IQFSDSQSFN KVAERVLLRL QEKLKGVEDG RVLSVGGQVN LLIQQAMDPN NLSRLFPGWQ
AWV
//