ID A0A2U3VZR5_ODORO Unreviewed; 3054 AA.
AC A0A2U3VZR5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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_004401109.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004401109.1};
RN [1] {ECO:0000313|RefSeq:XP_004401109.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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_004401109.1; XM_004401052.1.
DR STRING; 9708.A0A2U3VZR5; -.
DR GeneID; 101378264; -.
DR KEGG; oro:101378264; -.
DR CTD; 472; -.
DR InParanoid; A0A2U3VZR5; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000245340; 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 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:UP000245340};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU365027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365027}.
FT DOMAIN 1938..2564
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2684..2996
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3022..3054
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2974..2995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3054 AA; 349202 MW; 2B2EB3728041AD83 CRC64;
MSLALNDLLI CCRQLEHDRA TERRKEVEKF KRLIRDPETV QHLDRHSDSK QSKYLNWDAV
FRFLQKYVQK ETECLRTAKP SVSASTQATR QKKMQEISSL VKYFIKCANK RAPRLKCQEL
LNYIMDTVKD SFNGAVYGAD CSNILLKDIL SVRKYWCEIS QQQWLELFSV YFSLYLKPEQ
DINRVLVARI IHAVTKGCCS QTDGLNSKFL DFFSKAIQHA RQEKSSAGLN HILAAFITFL
KTLAVNFRIR VCQLGDEILP TLLYIWTQHR LNDSLKEVII ELFQLQIYVH HPKGAKTQEK
GAYESSKWKS ILYNLYDLLI NEISHIGSRG KYSSGSRNVA VKENLIELMA DICHQIFNED
TRSLEISQSY TTTQREFNDY SAPCKKKKIE LGWEVIKDHL QKSQSDFDLV PWLQITTQLI
SKYPSSLPNY ELSPLLMILY QLLPQHRHGE RTPYVLRCLT EVALCQGKKS NLEGSQKSDL
LKFWIKIWSL TFRGISSEQI QAENFGLLGA IIQGSLIEVD REFWKLFTGS ACRPSCPAVC
CLTLAMTICV VPETVKTGGE QSTCEVNRSC SLKELMMKWL LLSQLEDNFE DCTELPPVLH
SNFPHLAVEK ILVSLTMKNC KAAMNFLQTV PGCEQHQKDQ EEPSFSEVEE LFLQTTFDKM
DFLTTVKECA VEKHQATVGF SVHQNLKQSL DLCLLGLSEQ LLNNYSSETT NAEMLIRCSS
LLVGVLGCYC YVGVIAEEEA YRSELFQKAK SLMQCAGESI TLFKNKTSEE SRFASLRNMM
NLCTSCLCNC TKPSPNKIAS RFFLRLLTSK LMNDIADICR SLASFIRKPF DFREVESGED
DPDENMMEVE DHSSMNLFSD SGASEAGMSG DGQSTFGAMN PLAEEHLSKQ DLLFLDMLKF
LCVCVTTAQT GPVSFRAADI RRKLLMLIDT SMLDPTKSLH LHMYLVLLKE LPGEEYPLPM
EEVVELLKPL SNVCSLYRRD QDVCKTVLNH FVPVVRNLCQ GDMDAENTRD AQGQFLTVIG
AFWHLAKEGK CTFSVRMALV KCLKTLLETD PYSKWAILNV MGKDFPVNEV FPHFLADNHH
QVGMLAAESI NRLFQDMKYR GSSTLLKALP LKLQQTAFEN AYLKAQEGTR EVSHRAENPE
FLDETYNRKS VLLMTIAVIL CCSPVCEKQA LFALCKSVKE NGLEPRLVKK VLEKVSETFG
YRRLEDFMAS HLDYLVLEWL NLQDTEHSLY SFPFILLNYT NVEDFYRSCY KVLIPHLVIR
SRFDEVKSIA NQIDEDWKSL LTHCFPKILV NILPYFAYEG TGDSGMAQQR ETATKVYDML
KDEDLLGKQI DHLFLTNLPE IVVELLMTLH EPATSGASQS TDLCDFSGDL DPAPNPPHFP
SHVIKATFAY ISNCHKTKLK SILEILSKSP DSYQKILLAI CEQAAETNNV YKKHRILKIY
HLFVTLLLKD ITSALGGAWA FVLRDVIYTL IHYINKRPSR FMDVSLRSFS LCCDLLSRVC
HTAVTYCKDA LENHLHVIVG TLIPLVDDQM EVQEQVLDLL KYLVIDNKDN ENLYMTIKLL
DPFPDHDVFK DLRITQQKIK YSKGPFSLLE EINHFLSVSV YDALPLTRLE GLKDLCRQLA
QHKDQMVDLM RASQDNPQDG IMVKLIVSLL QLCKMAVNHT GEREVLEAVG SCLGEVGPVD
FSTIAIQHGR DTSSTKAPEL FEDKELQWTF TALTYLNNTL VEDCVKVRSA AVTCLKSILA
TKTGHSFWEI YKTTPDPMLI YLQPFRTSKK KFLEVPRPDK ESPLEGLDDM SLWIPQSENH
DIWIKRLTCA FLDSGGTKSE ILQLLKPMCE VKTDFCQTVL PYLIHDILLQ DTDESWRNLL
SAHIQGFFTN CFRHSLPTSR STTPANLDSE SEHLFRCCVD KKSQRTMLAV VDYMRRQKRP
SLGTVFDDAF WLELNYLEVA KVAQSCAAHF TALLYAEIYA DKKSMEDQDK RSLTFEEASQ
STAISSLSEK SKEETGISLQ DLLLEIYRSI GEPDSLYGCG GGKLLQPLTR LRTYEHEAMW
GKALVTYDLE TAISSATRQA GIIQALQNLG LCHILSVYLK GLDHENKEWC AELQELHYQA
AWRNMQWGHC PSVNKGIEGT SYHESLYNAL QSLRDREFST FYESLRYARV KEVEELCKGS
LESVYSLYPT LSRLQAIGEL ENIGELFSRS GTDRQPSEVY TKWRKHSQLL KDSDFSFQEP
IMALRTVILE ILMEKEMENS QRECFRDILT KHLVELSILA RTVENTQLPE RAIFQIKQYN
PASCGVSEWQ LEEAQVFWAK KEQSLALSIL KQMIKKLDAS CAENDPDLRL TYAECLRVCG
TWLAETCLEN PAVIMQTYLE KAVEVARNYD GESSDELRNG KMKAFLSLAR FSDTQYQRIE
NYMKSSEFEN KQALLKRAKE EVGLLREHKI QTNRYTVKVQ RELELDECAL RALKEDRKRF
LCKAVENYIS CLLSGEGHDM WIFRLCSLWL ENSGVSEVNG MMKTDGMKIP SYKFLPLMYQ
LAARMGTKMM GGLGFHEVLN NLISRISMDH PHHTLFIILA LANANKDEFL TKPEAARRNR
IIKNAPKQSS PLDEDRTEAA NRIIHTIRSR RPQMVRSVEA LCDAYIILAN LDAAQWKTQR
KGINIPADQP ITKLKNLEDV VVPTMEIKVD PTGEYRNLVT IQSFKAEFRL AGGLNLPKII
DCLGSDGKER RQLVKGRDDL RQDAVMQQVF QMCNKLLQRN TETRKRKLTI CTYKVVPLSQ
RSGVLEWCTG TVPIGEFLVN NENGAHKRYR PRDFSAVHCQ KKMMDVQKKS FEEKYKTFMD
VCQKFQPVFR YFCMEKFLDP AVWFEKRLAY TRSVATSSIV GYILGLGDRH VQNILINEQS
AELVHIDLGV AFEQGKILPT PETVPFRLTR DIVDGMGITG VEGVFRRCCE KTMEVMRSSQ
ETLLTIVEVL LYDPLFDWTM NPLKALYLQQ RPEDDTELHS TPSGEDPECK RNLSDTDQSF
NKVAERVLMR LQEKLKGVEE GTVLSVGGQV NLLIQQAMDP KNLSRLFPGW KAWV
//
