Double-strand break repair protein MRE11 (EC 3.1.-.-) (Double-strand break repair protein MRE11A) (Meiotic recombination 11 homolog 1) (MRE11 homolog 1) (Meiotic recombination 11 homolog A) (MRE11 homolog A)

 MRE11_RAT               Reviewed;         706 AA.
 Q9JIM0;
 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
 01-OCT-2000, sequence version 1.
 23-FEB-2022, entry version 145.
 RecName: Full=Double-strand break repair protein MRE11;
          EC=3.1.-.- {ECO:0000250|UniProtKB:P49959};
 AltName: Full=Double-strand break repair protein MRE11A;
 AltName: Full=Meiotic recombination 11 homolog 1;
          Short=MRE11 homolog 1;
 AltName: Full=Meiotic recombination 11 homolog A;
          Short=MRE11 homolog A;
 Name=Mre11; Synonyms=Mre11a;
 Rattus norvegicus (Rat).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
 Murinae; Rattus.
 NCBI_TaxID=10116;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=10908350; DOI=10.1093/nar/28.15.2882;
 Lanson N.A. Jr., Egeland D.B., Royals B.A., Claycomb W.C.;
 "The MRE11-NBS1-RAD50 pathway is perturbed in SV40 large T antigen-
 immortalized AT-1, AT-2 and HL-1 cardiomyocytes.";
 Nucleic Acids Res. 28:2882-2892(2000).
 [2]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, AND IDENTIFICATION BY
 MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=22673903; DOI=10.1038/ncomms1871;
 Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
 Olsen J.V.;
 "Quantitative maps of protein phosphorylation sites across 14 different rat
 organs and tissues.";
 Nat. Commun. 3:876-876(2012).
 -!- FUNCTION: Component of the MRN complex, which plays a central role in
     double-strand break (DSB) repair, DNA recombination, maintenance of
     telomere integrity and meiosis. The complex possesses single-strand
     endonuclease activity and double-strand-specific 3'-5' exonuclease
     activity, which are provided by MRE11. RAD50 may be required to bind
     DNA ends and hold them in close proximity. This could facilitate
     searches for short or long regions of sequence homology in the
     recombining DNA templates, and may also stimulate the activity of DNA
     ligases and/or restrict the nuclease activity of MRE11 to prevent
     nucleolytic degradation past a given point. The complex may also be
     required for DNA damage signaling via activation of the ATM kinase. In
     telomeres the MRN complex may modulate t-loop formation.
     {ECO:0000250|UniProtKB:P49959}.
 -!- COFACTOR:
     Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
 -!- ACTIVITY REGULATION: Interaction with SAMHD1 stimulates the double-
     strand-specific 3'-5' exonuclease activity.
     {ECO:0000250|UniProtKB:P49959}.
 -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
     RAD50/MRE11 associated with a single NBN. As part of the MRN complex,
     interacts with MCM9; the interaction recruits the complex to DNA repair
     sites. Component of the BASC complex, at least composed of BRCA1, MSH2,
     MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN. Found in a complex with
     TERF2. Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo. Interacts
     with ATF2. Interacts with EXD2. Interacts with MRNIP. Interacts with
     SAMHD1; leading to stimulate 3'-5' exonuclease activity. Interacts
     (when ubiquitinated) with UBQLN4 (via its UBA domain) (By similarity).
     Interacts with CYREN (via XLF motif) (By similarity).
     {ECO:0000250|UniProtKB:P49959, ECO:0000250|UniProtKB:Q61216}.
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49959}.
     Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Chromosome
     {ECO:0000250|UniProtKB:P49959}. Note=Localizes to discrete nuclear foci
     after treatment with genotoxic agents. {ECO:0000250|UniProtKB:P49959}.
 -!- PTM: Ubiquitinated following DNA damage. Ubiquitination triggers
     interaction with UBQLN4, leading to MRE11 removal from chromatin and
     degradation by the proteasome. {ECO:0000250|UniProtKB:P49959}.
 -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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 EMBL; AF218574; AAF91227.1; -; mRNA.
 RefSeq; NP_071615.1; NM_022279.1.
 SMR; Q9JIM0; -.
 STRING; 10116.ENSRNOP00000012940; -.
 iPTMnet; Q9JIM0; -.
 PhosphoSitePlus; Q9JIM0; -.
 jPOST; Q9JIM0; -.
 PaxDb; Q9JIM0; -.
 GeneID; 64046; -.
 KEGG; rno:64046; -.
 UCSC; RGD:69263; rat.
 CTD; 4361; -.
 RGD; 69263; Mre11a.
 eggNOG; KOG2310; Eukaryota.
 InParanoid; Q9JIM0; -.
 OrthoDB; 834694at2759; -.
 PhylomeDB; Q9JIM0; -.
 Reactome; R-RNO-1834949; Cytosolic sensors of pathogen-associated DNA.
 Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
 Reactome; R-RNO-5685938; HDR through Single Strand Annealing (SSA).
 Reactome; R-RNO-5685939; HDR through MMEJ (alt-NHEJ).
 Reactome; R-RNO-5685942; HDR through Homologous Recombination (HRR).
 Reactome; R-RNO-5693548; Sensing of DNA Double Strand Breaks.
 Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
 Reactome; R-RNO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
 Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
 Reactome; R-RNO-5693579; Homologous DNA Pairing and Strand Exchange.
 Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
 Reactome; R-RNO-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
 Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
 Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
 PRO; PR:Q9JIM0; -.
 Proteomes; UP000002494; Unplaced.
 GO; GO:0000785; C:chromatin; IDA:RGD.
 GO; GO:0000781; C:chromosome, telomeric region; ISO:RGD.
 GO; GO:0000794; C:condensed nuclear chromosome; IDA:RGD.
 GO; GO:0005737; C:cytoplasm; ISO:RGD.
 GO; GO:0030870; C:Mre11 complex; ISO:RGD.
 GO; GO:0005654; C:nucleoplasm; IDA:RGD.
 GO; GO:0005634; C:nucleus; IDA:RGD.
 GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO; GO:0016605; C:PML body; ISO:RGD.
 GO; GO:0005657; C:replication fork; ISS:UniProtKB.
 GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
 GO; GO:0008408; F:3'-5' exonuclease activity; ISO:RGD.
 GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
 GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
 GO; GO:0004520; F:endodeoxyribonuclease activity; ISO:RGD.
 GO; GO:0042802; F:identical protein binding; ISO:RGD.
 GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
 GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
 GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; ISO:RGD.
 GO; GO:0008283; P:cell population proliferation; ISO:RGD.
 GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
 GO; GO:0051276; P:chromosome organization; ISO:RGD.
 GO; GO:0032508; P:DNA duplex unwinding; ISO:RGD.
 GO; GO:0110025; P:DNA strand resection involved in replication fork processing; ISS:UniProtKB.
 GO; GO:0006302; P:double-strand break repair; ISO:RGD.
 GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
 GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:RGD.
 GO; GO:0007507; P:heart development; IEP:RGD.
 GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:RGD.
 GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
 GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IBA:GO_Central.
 GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:RGD.
 GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; ISO:RGD.
 GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
 GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:RGD.
 GO; GO:0033674; P:positive regulation of kinase activity; ISO:RGD.
 GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:RGD.
 GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:RGD.
 GO; GO:0007062; P:sister chromatid cohesion; ISO:RGD.
 GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
 GO; GO:0031860; P:telomeric 3' overhang formation; ISO:RGD.
 CDD; cd00840; MPP_Mre11_N; 1.
 Gene3D; 3.30.110.110; -; 1.
 Gene3D; 3.60.21.10; -; 1.
 InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
 InterPro; IPR029052; Metallo-depent_PP-like.
 InterPro; IPR003701; Mre11.
 InterPro; IPR038487; Mre11_capping_dom.
 InterPro; IPR007281; Mre11_DNA-bd.
 InterPro; IPR041796; Mre11_N.
 Pfam; PF00149; Metallophos; 1.
 Pfam; PF04152; Mre11_DNA_bind; 1.
 PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
 SMART; SM01347; Mre11_DNA_bind; 1.
 SUPFAM; SSF56300; SSF56300; 1.
 TIGRFAMs; TIGR00583; mre11; 1.
 1: Evidence at protein level;
 Acetylation; Chromosome; DNA damage; DNA repair; Endonuclease; Exonuclease;
 Hydrolase; Isopeptide bond; Manganese; Meiosis; Nuclease; Nucleus;
 Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
 INIT_MET        1
                 /note="Removed"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 CHAIN           2..706
                 /note="Double-strand break repair protein MRE11"
                 /id="PRO_0000138675"
 REGION          505..706
                 /note="Disordered"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 COMPBIAS        505..528
                 /note="Basic and acidic residues"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 COMPBIAS        529..549
                 /note="Polar residues"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 COMPBIAS        584..641
                 /note="Polar residues"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 COMPBIAS        658..681
                 /note="Polar residues"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 ACT_SITE        129
                 /note="Proton donor"
                 /evidence="ECO:0000250"
 MOD_RES         2
                 /note="N-acetylserine"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 MOD_RES         2
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q61216"
 MOD_RES         275
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 MOD_RES         618
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 MOD_RES         640
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q61216"
 MOD_RES         648
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 MOD_RES         676
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 MOD_RES         686
                 /note="Phosphoserine"
                 /evidence="ECO:0007744|PubMed:22673903"
 MOD_RES         699
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 CROSSLNK        416
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in SUMO2)"
                 /evidence="ECO:0000250|UniProtKB:P49959"
 SEQUENCE   706 AA;  80122 MW;  0183A41BC015FDA0 CRC64;
 MSPTDPLDDE DTFKILVATD IHLGFMEKDA VRGNDTFVTF DEILRLALEN EVDFILLGGD
 LFHENKPSRK TLHSCLELLR KYCMGDRPVQ FEIISDQSVN FGFSKFPWVN YRDGNLNISI
 PVFSIHGNHD DPTGADALCA LDVLSCAGFV NHFGRSMSVE KVDISPVLLQ KGSTKLALYG
 LGSIPDERLY RMFVNKKVTM LRPKEDENSW FNLFVIHQNR SKHGSTNFIP EQFLDDFIDL
 VIWGHEHECK IGPTRNEQQL FYVSQPGSSV VTALSPGETV KKHVGLLRVK GRKMNMQKLP
 LRTVRQFFME DVVLANHPSL FNPDNPKVTQ AIQSFCLEKI EEMLDSAERE RLGNPQQPEK
 PLIRLRVDYS GGFEPFNVLR FSQKFVDRVA NPKDVIHFFR HREQKGKTGE EINFGKLIIK
 PASEGTTLRV EDLVKQYFQT AEKNVQLSLL TERGMGEAVQ EFVDKEEKDA IEELVKYQLE
 KTQRFLKERH IDALEDKIDE EVRRFRESRQ RNTNEEDDEV REAMSRARAL RSQSENAASA
 FSADDLSFDI TEQTADDSDD SQSAVPSRGR GRGRGRRGGR GQSTAPRGGS QRGRDTGLGI
 STRGRSSKAT ASTSRNMSII DAFRSTRQQP SRNVATKNYS ETIEVDESDD DDSFPTSSRA
 DQRWSGTAPS KRMSQSQTAK GVDFESDEDD DDDPFMSGSC PRRNRR

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