RAD51_RABIT
ID RAD51_RABIT Reviewed; 339 AA.
AC O77507;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA repair protein RAD51 homolog 1;
GN Name=RAD51;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=9634474; DOI=10.1007/s002510050410;
RA Schiaffella E., Fuschiotti P., Bensinger S.J., Mage R.G.;
RT "High RAD51 mRNA levels in young rabbit appendix. A role in B-cell gene
RT conversion?";
RL Immunogenetics 48:108-115(1998).
CC -!- FUNCTION: Plays an important role in homologous strand exchange, a key
CC step in DNA repair through homologous recombination (HR). Binds to
CC single-stranded DNA in an ATP-dependent manner to form nucleoprotein
CC filaments which are essential for the homology search and strand
CC exchange. Catalyzes the recognition of homology and strand exchange
CC between homologous DNA partners to form a joint molecule between a
CC processed DNA break and the repair template. Recruited to resolve
CC stalled replication forks during replication stress. Part of a PALB2-
CC scaffolded HR complex containing BRCA2 and RAD51C and which is thought
CC to play a role in DNA repair by HR. Plays a role in regulating
CC mitochondrial DNA copy number under conditions of oxidative stress in
CC the presence of RAD51C and XRCC3. Also involved in interstrand cross-
CC link repair. {ECO:0000250|UniProtKB:Q06609}.
CC -!- SUBUNIT: Forms linear homooligomers, giving rise to a RAD51
CC nucleoprotein filament, which is essential for strand-pairing reactions
CC during DNA recombination. Interacts with BRCA1 and either directly or
CC indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts
CC with the BCDX2 subcomplex RAD51C:RAD51B. Component of the homologous
CC recombination repair (HR) complex composed of ERCC5/XPG, BRCA2, PALB2,
CC DSS1 and RAD51. Interacts directly with PALB2 which may serve as a
CC scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and
CC XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and
CC this may require prior phosphorylation of CHEK1. Interacts with the
CC MND1-PSMC3IP heterodimer. Found in a complex, at least composed of BLM,
CC RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts
CC with SPIDR; the interaction is direct and recruits RAD51 to DNA damage
CC sites. Interacts with FIGNL1 (via N-terminal one-half region); the
CC interaction is direct. Interacts with RAD51AP1 (via C-terminal region);
CC the interaction is direct. Interacts with NABP2, RPA1, PALB2 and RAD51.
CC Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5.
CC Interacts with hyperphosphorylated RPA2; this interaction is necessary
CC for efficient recruitment to chromatin in response to DNA damage.
CC Interacts with SWSAP1; involved in homologous recombination repair.
CC Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere
CC with the formation of the RAD51-DNA homologous recombination structure.
CC Interacts with POLQ; POLQ acts as an inhibitor of homology-
CC recombination repair (HR) pathway by limiting RAD51 accumulation at
CC resected ends. Interacts with FBH1. Interacts with POLN. Interacts with
CC RFWD3. Interacts with the MCM8-MCM9 complex; the interaction recruits
CC RAD51 to DNA damage sites (By similarity). Component of a multiprotein
CC complex with MEIOB and SPATA22. Interacts with the complex
CC BRME1:HSF2BP:BRCA2 (By similarity). Interacts with HELQ; stimulating
CC HELQ DNA helicase activity and ability to unwing DNA. Interacts with
CC MMS22L; the interaction is direct and promotes recruitment of RAD51 to
CC sites of DNA damage. Interacts with the ATAD5 RFC-like complex. Within
CC the ATAD5 RFC-like complex, interacts with ATAD5 (via N-terminus); the
CC interaction is direct and enhanced under replication stress. Interacts
CC with WDR48; the interaction is enhanced under replication stress (By
CC similarity). {ECO:0000250|UniProtKB:Q06609,
CC ECO:0000250|UniProtKB:Q08297}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q06609}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q06609}. Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q06609}. Chromosome
CC {ECO:0000250|UniProtKB:Q06609}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q06609}.
CC Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon
CC induction of DNA damage. DNA damage induces an increase in nuclear
CC levels. Together with FIGNL1, redistributed in discrete nuclear DNA
CC damage-induced foci after ionizing radiation (IR) or camptothecin (CPT)
CC treatment. Accumulated at sites of DNA damage in a SPIDR-dependent
CC manner. Recruited at sites of DNA damage in a MCM9-MCM8-dependent
CC manner. Colocalizes with ERCC5/XPG to nuclear foci in S phase (By
CC similarity). {ECO:0000250|UniProtKB:Q06609}.
CC -!- PTM: Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex,
CC regulating RAD51 subcellular location and preventing its association
CC with DNA. Ubiquitinated by RFWD3 in response to DNA damage:
CC ubiquitination leads to degradation by the proteasome, promoting
CC homologous recombination. {ECO:0000250|UniProtKB:Q06609}.
CC -!- PTM: Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance
CC association with chromatin at sites of DNA damage and promote DNA
CC repair by homologous recombination. Phosphorylation by ABL1 inhibits
CC function. {ECO:0000250|UniProtKB:Q06609}.
CC -!- SIMILARITY: Belongs to the RecA family. RAD51 subfamily. {ECO:0000305}.
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DR EMBL; AF017729; AAC28561.1; -; mRNA.
DR RefSeq; NP_001075493.1; NM_001082024.1.
DR AlphaFoldDB; O77507; -.
DR BMRB; O77507; -.
DR SMR; O77507; -.
DR STRING; 9986.ENSOCUP00000014527; -.
DR GeneID; 100008661; -.
DR KEGG; ocu:100008661; -.
DR CTD; 5888; -.
DR eggNOG; KOG1433; Eukaryota.
DR InParanoid; O77507; -.
DR OrthoDB; 877394at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0072757; P:cellular response to camptothecin; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0000730; P:DNA recombinase assembly; ISS:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IEA:InterPro.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011941; DNA_recomb/repair_Rad51.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02239; recomb_RAD51; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT CHAIN 2..339
FT /note="DNA repair protein RAD51 homolog 1"
FT /id="PRO_0000122934"
FT DOMAIN 48..77
FT /note="HhH"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..257
FT /note="Interaction with PALB2"
FT /evidence="ECO:0000250"
FT MOTIF 245..260
FT /note="Nuclear export signal; masked by the interaction
FT with BRCA2"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT BINDING 127..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT MOD_RES 54
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT MOD_RES 309
FT /note="Phosphothreonine; by CHEK1"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q06609"
SQ SEQUENCE 339 AA; 37028 MW; 0B7A2C6621FAF84D CRC64;
MAMQMQLEAN ADTSVEEESF GPQPVSRLEQ CGINANDVKK LEEAGFHTEE AVAYAPKKEL
INIKGISEAK ADKILTEAAK LVPMGFTTAT EFHQRRSEII QITTGSKELD KLLQGGIETG
SITEMFGEFR TGKTQICHTL AVTCQLPIDR GGGEGKAMYI DTEGTFRPER LLAVAERYGL
SGSDVLDNVA YARGFNTDHQ TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA
RQMHLARFLR MLLRLADEFG VTVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
