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MRE11_CAEEL
ID   MRE11_CAEEL             Reviewed;         728 AA.
AC   Q23255;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Double-strand break repair protein mre-11;
GN   Name=mre-11 {ECO:0000312|WormBase:ZC302.1};
GN   ORFNames=ZC302.1 {ECO:0000312|WormBase:ZC302.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF GLU-95.
RX   PubMed=11238374; DOI=10.1101/gad.864101;
RA   Chin G.M., Villeneuve A.M.;
RT   "C. elegans mre-11 is required for meiotic recombination and DNA repair but
RT   is dispensable for the meiotic G(2) DNA damage checkpoint.";
RL   Genes Dev. 15:522-534(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16628214; DOI=10.1038/sj.emboj.7601102;
RA   Polanowska J., Martin J.S., Garcia-Muse T., Petalcorin M.I.R.,
RA   Boulton S.J.;
RT   "A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA
RT   damage sites.";
RL   EMBO J. 25:2178-2188(2006).
CC   -!- FUNCTION: Involved in DNA double-strand break repair (DSBR)
CC       (PubMed:11238374). Possesses single-strand endonuclease activity and
CC       double-strand-specific 3'-5' exonuclease activity (PubMed:11238374).
CC       Also involved in meiotic DSB processing (PubMed:11238374). In response
CC       to ionizing radiation, probably required for the association between
CC       the brc-1-brd-1 heterodimer and rad-51 and let-70 in order to activate
CC       E3-ubiquitin ligase activity of the heterodimer and induce
CC       ubiquitination at DNA damage sites (PubMed:16628214).
CC       {ECO:0000269|PubMed:11238374, ECO:0000269|PubMed:16628214}.
CC   -!- FUNCTION: Required for meiotic crossing over and chiasma formation.
CC       Pachytene morphology and homolog pairing are normal. Vital in long term
CC       for maintenance of reproductive capacity of subsequent generations.
CC       {ECO:0000269|PubMed:11238374}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P32829};
CC   -!- SUBUNIT: Forms a complex with rad-50. {ECO:0000250|UniProtKB:P32829}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11238374}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in DNA damage
CC       repair defects following ionizing radiation with reduced ubiquitination
CC       at DNA damage sites. {ECO:0000269|PubMed:16628214}.
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family.
CC       {ECO:0000255|RuleBase:RU003447, ECO:0000269|PubMed:11238374}.
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DR   EMBL; Z73978; CAA98292.2; -; Genomic_DNA.
DR   PIR; T27512; T27512.
DR   RefSeq; NP_505736.2; NM_073335.4.
DR   AlphaFoldDB; Q23255; -.
DR   SMR; Q23255; -.
DR   BioGRID; 44517; 17.
DR   IntAct; Q23255; 3.
DR   MINT; Q23255; -.
DR   STRING; 6239.ZC302.1.1; -.
DR   iPTMnet; Q23255; -.
DR   EPD; Q23255; -.
DR   PaxDb; Q23255; -.
DR   PeptideAtlas; Q23255; -.
DR   EnsemblMetazoa; ZC302.1.1; ZC302.1.1; WBGene00003405.
DR   EnsemblMetazoa; ZC302.1.2; ZC302.1.2; WBGene00003405.
DR   GeneID; 179488; -.
DR   KEGG; cel:CELE_ZC302.1; -.
DR   UCSC; ZC302.1.1; c. elegans.
DR   CTD; 179488; -.
DR   WormBase; ZC302.1; CE37459; WBGene00003405; mre-11.
DR   eggNOG; KOG2310; Eukaryota.
DR   GeneTree; ENSGT00390000017288; -.
DR   HOGENOM; CLU_009535_3_0_1; -.
DR   InParanoid; Q23255; -.
DR   OMA; PSREVQH; -.
DR   OrthoDB; 834694at2759; -.
DR   PhylomeDB; Q23255; -.
DR   Reactome; R-CEL-1834949; Cytosolic sensors of pathogen-associated DNA.
DR   Reactome; R-CEL-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-CEL-5685939; HDR through MMEJ (alt-NHEJ).
DR   Reactome; R-CEL-5693548; Sensing of DNA Double Strand Breaks.
DR   Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR   PRO; PR:Q23255; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003405; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0030870; C:Mre11 complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IBA:GO_Central.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
DR   GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
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   1: Evidence at protein level;
KW   DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase; Manganese;
KW   Meiosis; Nuclease; Nucleus; Reference proteome.
FT   CHAIN           1..728
FT                   /note="Double-strand break repair protein mre-11"
FT                   /id="PRO_0000138678"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..636
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         95
FT                   /note="E->K: In mre-11-ME41; defective in meiotic
FT                   chromosome degradation."
FT                   /evidence="ECO:0000269|PubMed:11238374"
SQ   SEQUENCE   728 AA;  81559 MW;  E86C5BEF81216DC9 CRC64;
     MCGSDDSFDD FVPDSQEPAS SRTRNQDHLD DDEVPCSQRP DAANDTMVED LDEGDEPAHD
     ESEDIIKILV ATDIHCGYGE NKANIHMDAV NTFEEVLQIA TEQKVDMILL GGDLFHENNP
     SREVQHRVTQ LLRQYCLNGN PIALEFLSDA SVNFNQSVFG HVNYYDQNLN VGLPIFTIHG
     NHDDLSGKGL TALDLLHESG LVNLFGKHSN IQEFIVSPIL LRKGETRLAL YGIGSQRDDR
     LVRAFKNNSI SFLRPNAGAE DWFNLFVLHQ NRPRRAMHRS TGNFLPESLI PQFFDLLIWG
     HEHECKPDPQ YVASSEAVGD GFYILQPGST VATSLTPEEA LQKNAFLIKI KGRKFASKPI
     PLQTVRPMVC DELLLDKIPP GSRPILKTDR PKHTDGRYID EIAIEAKINE MITTAKAKRR
     PRQPELPLIR LKVIYDGDWL NITPANAKRI GLRYENVVAN AVDMVFIKKN NKPKEGKLQT
     ENEKNITEMA DEMGQVSATN LQTIINDYFI NQPLVDQMTV LKPIGIGRAL EQYSAIEEGG
     LATSANRNFD SCLMHQIDVV RKTLKKMPLP PINDPSDLDK FRDLITKDLY DMKKADSERF
     KNPVADVEME EDEDDPQYYM PPQSTSRTNY ASGSEDEVAN SDEEMGSSIS RHSKQPTTRG
     RGRGARGAGA SRETTRGRSN KVVSTRQIDS DGFEIINDSP SPPPASRSTR GKARGKSAPS
     KKRDLSFF
 
 
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