ID A0A340WCK4_LIPVE Unreviewed; 3058 AA.
AC A0A340WCK4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Serine-protein kinase ATM {ECO:0000256|RuleBase:RU365027};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU365027};
GN Name=ATM {ECO:0000313|RefSeq:XP_007447277.1,
GN ECO:0000313|RefSeq:XP_007447278.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007447278.1};
RN [1] {ECO:0000313|RefSeq:XP_007447277.1, ECO:0000313|RefSeq:XP_007447278.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon double strand breaks (DSBs), apoptosis and genotoxic
CC stresses such as ionizing ultraviolet A light (UVA), thereby acting as
CC a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-
CC Q. Phosphorylates 'Ser-139' of histone variant H2AX at double strand
CC breaks (DSBs), thereby regulating DNA damage response mechanism. Also
CC plays a role in pre-B cell allelic exclusion, a process leading to
CC expression of a single immunoglobulin heavy chain allele to enforce
CC clonality and monospecific recognition by the B-cell antigen receptor
CC (BCR) expressed on individual B-lymphocytes. After the introduction of
CC DNA breaks by the RAG complex on one immunoglobulin allele, acts by
CC mediating a repositioning of the second allele to pericentromeric
CC heterochromatin, preventing accessibility to the RAG complex and
CC recombination of the second allele. Also involved in signal
CC transduction and cell cycle control. May function as a tumor
CC suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates
CC DYRK2, CHEK2, p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin (NBN),
CC TERF1, RAD9, UBQLN4 and DCLRE1C. May play a role in vesicle and/or
CC protein transport. Could play a role in T-cell development, gonad and
CC neurological function. Binds DNA ends. Plays a role in replication-
CC dependent histone mRNA degradation. Phosphorylation of DYRK2 in nucleus
CC in response to genotoxic stress prevents its MDM2-mediated
CC ubiquitination and subsequent proteasome degradation. Phosphorylates
CC ATF2 which stimulates its function in DNA damage response.
CC Phosphorylates ERCC6 which is essential for its chromatin remodeling
CC activity at DNA double-strand breaks. {ECO:0000256|RuleBase:RU365027}.
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:0000256|ARBA:ARBA00000775,
CC ECO:0000256|RuleBase:RU365027};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000256|RuleBase:RU365027}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365027}.
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 RefSeq; XP_007447277.1; XM_007447215.1.
DR RefSeq; XP_007447278.1; XM_007447216.1.
DR STRING; 118797.A0A340WCK4; -.
DR GeneID; 103070327; -.
DR KEGG; lve:103070327; -.
DR CTD; 472; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU365027};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|RuleBase:RU365027};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU365027};
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 Reference proteome {ECO:0000313|Proteomes:UP000265300};
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 1942..2568
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2688..3001
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3026..3058
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2581..2601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1613..1640
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3058 AA; 350428 MW; 87D3C1A3DE116475 CRC64;
MSLALNDLLI CCRQLEHDRA TERRKEVEKF KRLIQDPETV QHLDQHSDSK QGKYLNWDAV
FRVLQKYIQK ETECLRTAKP NVSTSTQATR QKKMQEISSL VKYFIKCANK RAPRLKCQEL
LNYIMDTVKD SSNGAIYGAD CSNILLKDIL SVRKYWCEIS QQQWTELFSV YFQLYLKPSQ
DINRVLVARI IEAVTKGCCS QTDGLNSKFL DFFSKAIQRA RQEKSSAGLN HILAAFIIFL
KTLAVNFRIR VCELGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYIH HPKGAKTQEK
GAYESTKWKS ILYNVYDLLV SEISHIGSRG KYSSGSRNIA VKENLIELMA DICHQVFNED
TRSLEISQSY TTTQRELGDY NAPCKKRKIE LGWEVIKDHL QKSQNDFNIV PWLQIATQLI
SKYPSSLPNC ELSPLLMILH QLLPQQQHGE RTPYVLRCLM EVALCQGKKS NLESSQKSDL
LKLWIKIWSI TFRGISSEQI QAENFGLLGA IIQGSLVEVD REFWKLFTGS ACRPSCSAVC
CLTLALTICV VPETVKTGME KNIYDVNRNF SLKELIMKWL LFRQLEDDFE GSAQLPPILH
SNFPHLALEK ILVSLTMKNC KAAMNFFQSV PECEQHQKDT EEPSFSEVEE LFLQTTFDKM
DFLTIVKEHT TEKHQSSVGF SVHQNLKQSL DRYLLGLSEQ LLNNYSSETS NSEMLVRCSS
LLVGVLGCYC YVGVIAEEEA YKSELFQKAK SLMQYAGESI TLFKNKTNEE SRIVSLRNMM
HLCTCCLHNC IKHSPNKIAS GFFLRLLTSK LMNDIADICT SLVSIIKKPF DFGEVQSVED
GTDENLMEME DQSSMNLFND YPASSVIDAN ESGESQITIG AMNPLAEEHL SKQDLLFLDM
LKFLCMCVTT AQTNTVSFRA ADIRRKLLML IDSSMLDLTK SLHLHMYLVL LKDLPGEEHP
LPMEDVVELL KPLSNVCSLY RRDQDVCKTI LNHVLHIVTN LCQGNMDAEN TRDAQGQFLT
VIEAFWHLTK EGKCTFSVRM ALVKCLKTLL EADPYSKWAI LNVMGKDFPV NEVFPQFLDD
NHHQVCMLAA QSINRLFQHM KKGGPSTLLK ALPLKLQQAA FENSYLKAQE GMREVSHRAE
NSEILDELCN RKAIFLMMIA VVLYYSPVCE KQALFALCKS VKENGLEPHL IKKVLQKVSE
TFGYRHLEDF MTSHLDYLVL QWLNLEDTEY SLSSFPFTLL NYTNIEDFYR SCYKVLIPHL
VIRSQFDEVK SIANQIQEDW KSLLTDCFPK IIVNILPYFA YEDNTGDSGM AQQRKIATKV
YDMLKDENLL GKQIDHLFIS NLPEIVVELL MTLHEPATSG ASQSTDPCDF SGDLDPAPNP
PHFPSHVIKA TFAYISNCHK TKLKSILEIL SKSPDSYQKI LLAICEQAVE TNNVYKKHRI
LKIYHLFVSL LMNNIKSGLG GAWAFVLRDV IYTLIHYINQ RPSHFMDVSL RSFSLCCDLL
SRVCHTAVTY CKDALESHLH VIVGTLIPLV DDQMEVQEQV LDLLKYLVID NKDNENLYIT
IKLLDPFPDH VVFRDLRITQ QKIKYSRGPF SLLEEINHFL SVNVYDALPL TRLEGLKDLR
RQLEQHKDQM MDLMRASQDN PPDGVMVKLV VSLLQLSKMA VNHTGEREVL EAVGSCLGEV
GPIDFSTIAI QYSKDTSYTK ALELFEDKEL QWTFIMLTYL NNTLVEDCVK VRSAAVTCLK
SILATKTGHS FWEIYKMTND PMLIYLQPFR TSRKKFLEVP RLDKESPLEG LDNTSLWIPQ
SENHDIWLKT LTCAFLNSGG TKSEVLQLLK PMCEVKTDFC QTVLPYLIHD ILIQDTNESW
RNLLSTHIQG FFTNCFRHCS ETSRSTTPAN LDSESEHFFR CHLDKKSQRT MLAVVDYMRR
QKRPSLGTVF DDAFWLELNY LEVAKVAQSC AAHFTALLYA EIYADKKNMD DQEKRSLTFE
EGSQSTTISS LSEKSKEETG ISLQDLLLEI YRSIGEPDSL YGCGGGKILQ PLTRLRTYEH
EAMWGKALVT YDLETAISSS TRQAGIIQAL QNLGLCHILS VYLRGLDHEN KEWCAELQEL
HYQVAWRNMQ WDHCISVNKG IEGTSYHESL YNALQSLRDG EFSTFYESLK YARVKEVEEL
CKGSLESVYS LYPTLSRLQA IGELENIGEL FSRSITDRQP SEVYLKWWKH SQLLKDSDFS
FQEPIMALRT VILEILMEKE MENSQRECLK DILTKHLVEL SVLARTFKNT QLPERAIFQI
KQYNSASCGV SEWQLEEAQV FWAKKEQSLA LSILKQMIKK LGASCTENDP NLKLIYTECL
RVCGTWLAET CLENPAVIMQ TYLEKAVEVA GNYDGESNDG LRNGKMKAFL SLARFSDTQY
QRIENYMKSS EFENKQALLK RAKEEVGLLR EHKIQTNRYT VKVQRELELD ECALHALKED
RKRFLCKAVE NYINCLLSGE GHDTWIFRLC SLWLENSGVS EVNGMMKRDG MKIPSYKFLP
LMYQLAARMG TKMMGGLGFH EVLNNLISRI SMDHPHHTLF IILALANANK DEFLTKPEAA
RRSRITKNAP KQSSQLDEDR TEAANKIIRT IRSRRPQMVR SVEALCDAYI ILANLDATQW
KTQRKGISIP ADQPIIKLKN LEDVVVPTME IKVDPTGEYG NLVTIQSFKA EFRLAGGLNL
PKIIDCLGSD GKERRQLVKG RDDLRQDAVM QQVFQMCNTL LQRNTETRKR KLTICTYKVV
PLSQRSGVLE WCTGTVPIGE FLVNNESGAH KRYRPKDFSA YQCQKKMMDV QKKSFEEKYE
TFMEICQNFQ PVFRYFCMEK FLDPAVWFEK RLAYTRSVAT SSIVGYILGL GDRHVQNILI
NEQSAELVHI DLGVAFEQGK ILPTPETVPF RLTRDIVDGM GITGVEGVFR RCCEKTMEVM
RNSQETLLTI VEVLLYDPLF DWTMNPLKAL YLQQRPEDES ELHSTPNADD QECKRNLSDI
DHSFNKVAER VLMRLQEKLK GVEEGTVLSV GGQVNLLIQQ AMDPKNLSRL FPGWKAWV
//