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Database: UniProt
Entry: A0A340WCK4_LIPVE
LinkDB: A0A340WCK4_LIPVE
Original site: A0A340WCK4_LIPVE 
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
//
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