MRE11_MACFA
ID MRE11_MACFA Reviewed; 707 AA.
AC Q60HE6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Double-strand break repair protein MRE11;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P49959};
DE AltName: Full=Double-strand break repair protein MRE11A;
DE AltName: Full=Meiotic recombination 11 homolog A;
DE Short=MRE11 homolog A;
GN Name=MRE11; Synonyms=MRE11A; ORFNames=QtrA-18006;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex;
RA Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation and characterization of cDNA for macaque neurological disease
RT genes.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the MRN complex, which plays a central role in
CC double-strand break (DSB) repair, DNA recombination, maintenance of
CC telomere integrity and meiosis. The complex possesses single-strand
CC endonuclease activity and double-strand-specific 3'-5' exonuclease
CC activity, which are provided by MRE11. RAD50 may be required to bind
CC DNA ends and hold them in close proximity. This could facilitate
CC searches for short or long regions of sequence homology in the
CC recombining DNA templates, and may also stimulate the activity of DNA
CC ligases and/or restrict the nuclease activity of MRE11 to prevent
CC nucleolytic degradation past a given point. The complex may also be
CC required for DNA damage signaling via activation of the ATM kinase. In
CC telomeres the MRN complex may modulate t-loop formation.
CC {ECO:0000250|UniProtKB:P49959}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Interaction with SAMHD1 stimulates the double-
CC strand-specific 3'-5' exonuclease activity.
CC {ECO:0000250|UniProtKB:P49959}.
CC -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC RAD50/MRE11 associated with a single NBN. As part of the MRN complex,
CC interacts with MCM9; the interaction recruits the complex to DNA repair
CC sites. Component of the BASC complex, at least composed of BRCA1, MSH2,
CC MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN. Found in a complex with
CC TERF2. Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo. Interacts
CC with ATF2. Interacts with EXD2. Interacts with MRNIP. Interacts with
CC SAMHD1; leading to stimulate 3'-5' exonuclease activity. Interacts
CC (when ubiquitinated) with UBQLN4 (via its UBA domain) (By similarity).
CC Interacts with CYREN (via XLF motif) (By similarity).
CC {ECO:0000250|UniProtKB:P49959, ECO:0000250|UniProtKB:Q61216}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49959}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:P49959}. Chromosome
CC {ECO:0000250|UniProtKB:P49959}. Note=Localizes to discrete nuclear foci
CC after treatment with genotoxic agents. {ECO:0000250|UniProtKB:P49959}.
CC -!- PTM: Ubiquitinated following DNA damage. Ubiquitination triggers
CC interaction with UBQLN4, leading to MRE11 removal from chromatin and
CC degradation by the proteasome. {ECO:0000250|UniProtKB:P49959}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000305}.
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DR EMBL; AB125181; BAD51969.1; -; mRNA.
DR AlphaFoldDB; Q60HE6; -.
DR SMR; Q60HE6; -.
DR STRING; 9541.XP_005579432.1; -.
DR PRIDE; Q60HE6; -.
DR eggNOG; KOG2310; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0110025; P:DNA strand resection involved in replication fork processing; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd00840; MPP_Mre11_N; 1.
DR Gene3D; 3.30.110.110; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR003701; Mre11.
DR InterPro; IPR038487; Mre11_capping_dom.
DR InterPro; IPR007281; Mre11_DNA-bd.
DR InterPro; IPR041796; Mre11_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF04152; Mre11_DNA_bind; 1.
DR PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR SMART; SM01347; Mre11_DNA_bind; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR TIGRFAMs; TIGR00583; mre11; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA damage; DNA repair; Endonuclease; Exonuclease;
KW Hydrolase; Isopeptide bond; Manganese; Meiosis; Nuclease; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT CHAIN 2..707
FT /note="Double-strand break repair protein MRE11"
FT /id="PRO_0000138673"
FT REGION 505..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61216"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61216"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT CROSSLNK 416
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49959"
FT CROSSLNK 624
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P49959"
SQ SEQUENCE 707 AA; 80490 MW; CC9F4C10463E881E CRC64;
MSTADALDDE NTFKILVATD IHLGFMEKDA VRGNDTFVTL DEILRLARGN EVDFILLGGD
LFHENKPSRK TLHTCLELLR KYCMGDRPVQ FEILSDQSVN FGFSKFPWVN YQDGNLNISI
PVFSIHGNHD DPTGADALCA LDILSCAGFV NHFGRSMSVE KIDISPVLLQ KGSTKIALYG
LGSIPDERLY RMFVNKKVTM LRPKEDENSW FNLFVIHQNR SKHGSTNFIP EQFLDDFIDL
VIWGHEHECK IAPTKNEQQL FYISQPGSSV VTSLSPGEAV KKHVGLLRIK GRKMNMQKIP
LHTVRQFFME DIVLANHPDI FNPDNPKVTQ AIQSFCLEKI EEMLENAERE RLGNSRQPEK
PLVRLRVDYS GGFEPFSVLR FSQKFVDRVA NPKDIIHFFR HREQKEKTGE EINFGKLITK
PSEGTTLRVE DLVKQYFQTA EKNVQLSLLT ERGMGEAVQE FVDKEEKDAI EELVKYQLEK
TQRFLKERHI DALEDKIDEE VRRFRESRQK NTNEEDDEVR EAMTRARALR SQSEESASAF
SADDLMSIDL AEQMANDSDD SISAATNKGR GRGRGRRGGR GQNSASRGGS QRGRDTGLET
STRSRNSKTA VSASRNMSII DAFKSTRQQP SRNVTTKNYS EVIEVDESDE EEDVFPTTSK
TDQRWSSTSS SKIMSQSQVS KGVDFESSED DDDDPFMNTS SLRRNRR
