RAD54_MOUSE
ID RAD54_MOUSE Reviewed; 747 AA.
AC P70270; Q8BSR5; Q8C2C4; Q8K3D4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=DNA repair and recombination protein RAD54-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q7ZV09};
DE AltName: Full=RAD54 homolog;
DE Short=mHR54;
DE Short=mRAD54;
GN Name=Rad54l; Synonyms=Rad54;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8805304; DOI=10.1016/s0960-9822(02)00606-1;
RA Kanaar R., Troelstra C., Swagemakers S.M.A., Essers J., Smit B.,
RA Franssen J.-H., Pastink A., Bezzubova O.Y., Buerstedde J.-M., Clever B.,
RA Heyer W.-D., Hoeijmakers J.H.J.;
RT "Human and mouse homologs of the Saccharomyces cerevisiae RAD54 DNA repair
RT gene: evidence for functional conservation.";
RL Curr. Biol. 6:828-838(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=9108475; DOI=10.1016/s0092-8674(00)80199-3;
RA Essers J., Hendriks R.W., Swagemakers S.M.A., Troelstra C., de Wit J.,
RA Bootsma D., Hoeijmakers J.H.J., Kanaar R.;
RT "Disruption of mouse RAD54 reduces ionizing radiation resistance and
RT homologous recombination.";
RL Cell 89:195-204(1997).
RN [5]
RP FUNCTION.
RX PubMed=10209103; DOI=10.1016/s0960-9822(99)80142-0;
RA Tan T.L.R., Essers J., Citterio E., Swagemakers S.M.A., de Wit J.,
RA Benson F.E., Hoeijmakers J.H.J., Kanaar R.;
RT "Mouse Rad54 affects DNA conformation and DNA-damage-induced Rad51 foci
RT formation.";
RL Curr. Biol. 9:325-328(1999).
RN [6]
RP FUNCTION.
RX PubMed=10757799; DOI=10.1128/mcb.20.9.3147-3156.2000;
RA Dronkert M.L.G., Beverloo H.B., Johnson R.D., Hoeijmakers J.H.J., Jasin M.,
RA Kanaar R.;
RT "Mouse RAD54 affects DNA double-strand break repair and sister chromatid
RT exchange.";
RL Mol. Cell. Biol. 20:3147-3156(2000).
RN [7]
RP FUNCTION.
RX PubMed=12218123; DOI=10.4049/jimmunol.169.6.3069;
RA D'Avirro N., Truong D., Luong M., Kanaar R., Selsing E.;
RT "Gene conversion-like sequence transfers between transgenic antibody V
RT genes are independent of RAD54.";
RL J. Immunol. 169:3069-3075(2002).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION, AND FUNCTION.
RX PubMed=12531026; DOI=10.1016/s1568-7864(02)00110-6;
RA Essers J., Hendriks R.W., Wesoly J., Beerens C.E.M.T., Smit B.,
RA Hoeijmakers J.H.J., Wyman C., Dronkert M.L.G., Kanaar R.;
RT "Analysis of mouse Rad54 expression and its implications for homologous
RT recombination.";
RL DNA Repair 1:779-793(2002).
RN [9]
RP FUNCTION.
RX PubMed=12548566; DOI=10.1002/immu.200310009;
RA Bross L., Wesoly J., Buerstedde J.-M., Kanaar R., Jacobs H.;
RT "Somatic hypermutation does not require Rad54 and Rad54B-mediated
RT homologous recombination.";
RL Eur. J. Immunol. 33:352-357(2003).
RN [10]
RP FUNCTION.
RX PubMed=12897131; DOI=10.1128/mcb.23.16.5572-5580.2003;
RA Jaco I., Munoz P., Goytisolo F., Wesoly J., Bailey S., Taccioli G.,
RA Blasco M.A.;
RT "Role of mammalian Rad54 in telomere length maintenance.";
RL Mol. Cell. Biol. 23:5572-5580(2003).
RN [11]
RP FUNCTION.
RX PubMed=15175260; DOI=10.1101/gad.1204304;
RA Mills K.D., Ferguson D.O., Essers J., Eckersdorff M., Kanaar R., Alt F.W.;
RT "Rad54 and DNA ligase IV cooperate to maintain mammalian chromatid
RT stability.";
RL Genes Dev. 18:1283-1292(2004).
CC -!- FUNCTION: Plays an essential role in homologous recombination (HR)
CC which is a major pathway for repairing DNA double-strand breaks (DSBs),
CC single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication
CC forks. Acts as a molecular motor during the homology search and guides
CC RAD51 ssDNA along a donor dsDNA thereby changing the homology search
CC from the diffusion-based mechanism to a motor-guided mechanism. Plays
CC also an essential role in RAD51-mediated synaptic complex formation
CC which consists of three strands encased in a protein filament formed
CC once homology is recognized. Once DNA strand exchange occured,
CC dissociates RAD51 from nucleoprotein filaments formed on dsDNA (By
CC similarity). Deficiency also resulted in an increased frequency of end-
CC to-end chromosome fusions involving telomeres compared to the controls,
CC suggesting a putative role in telomere capping. Non-homologous end
CC joining (NHEJ) and homologous recombination (HR) represent the two
CC major pathways of DNA double-strand break (DSB) repair in eukaryotic
CC cells. LIG4 and RAD54L cooperate to support cellular proliferation,
CC repair spontaneous DSBs, and prevent chromosome and single chromatid
CC aberrations (PubMed:10209103, PubMed:10757799, PubMed:12218123,
CC PubMed:12531026, PubMed:12548566, PubMed:12897131, PubMed:15175260,
CC PubMed:9108475). {ECO:0000250|UniProtKB:P32863,
CC ECO:0000269|PubMed:10209103, ECO:0000269|PubMed:10757799,
CC ECO:0000269|PubMed:12218123, ECO:0000269|PubMed:12531026,
CC ECO:0000269|PubMed:12548566, ECO:0000269|PubMed:12897131,
CC ECO:0000269|PubMed:15175260, ECO:0000269|PubMed:9108475}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P32863};
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts (via N-terminus) with
CC RAD51 (By similarity). Interacts with NAP1L1 (By similarity). Interacts
CC with BRD9; this interaction orchestrates RAD51-RAD54 complex formation
CC (By similarity). {ECO:0000250|UniProtKB:P32863,
CC ECO:0000250|UniProtKB:Q7ZV09}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Hardly detectable in most tissues. Dramatically
CC increased in thymus, spleen and testis. {ECO:0000269|PubMed:8805304}.
CC -!- PTM: Acetylated. Acetylation promotes interaction with BRD9, and
CC subsequently with RAD54, which is essential for homologous
CC recombination (HR). {ECO:0000250|UniProtKB:Q92698}.
CC -!- PTM: Phosphorylated. Phosphorylation at Ser-572 by NEK1 specifically in
CC G2 phase allows efficient removal of RAD51 filaments from DNA.
CC {ECO:0000250|UniProtKB:Q92698}.
CC -!- MISCELLANEOUS: The nucleus of a mouse embryonic stem (ES) cell contains
CC on average 2.4 x 10(5) molecules.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; X97796; CAA66380.1; -; mRNA.
DR EMBL; AK088876; BAC40627.1; -; mRNA.
DR EMBL; BC021643; AAH21643.1; -; mRNA.
DR CCDS; CCDS18504.1; -.
DR RefSeq; NP_001116430.1; NM_001122958.1.
DR RefSeq; NP_001116431.1; NM_001122959.1.
DR RefSeq; NP_033041.3; NM_009015.3.
DR RefSeq; XP_006502940.1; XM_006502877.3.
DR RefSeq; XP_006502941.1; XM_006502878.3.
DR AlphaFoldDB; P70270; -.
DR SMR; P70270; -.
DR BioGRID; 202569; 9.
DR IntAct; P70270; 6.
DR STRING; 10090.ENSMUSP00000099765; -.
DR iPTMnet; P70270; -.
DR PhosphoSitePlus; P70270; -.
DR EPD; P70270; -.
DR MaxQB; P70270; -.
DR PaxDb; P70270; -.
DR PeptideAtlas; P70270; -.
DR PRIDE; P70270; -.
DR ProteomicsDB; 300346; -.
DR Antibodypedia; 18708; 266 antibodies from 31 providers.
DR DNASU; 19366; -.
DR Ensembl; ENSMUST00000102704; ENSMUSP00000099765; ENSMUSG00000028702.
DR Ensembl; ENSMUST00000102705; ENSMUSP00000099766; ENSMUSG00000028702.
DR GeneID; 19366; -.
DR KEGG; mmu:19366; -.
DR UCSC; uc008ugb.2; mouse.
DR CTD; 8438; -.
DR MGI; MGI:894697; Rad54l.
DR VEuPathDB; HostDB:ENSMUSG00000028702; -.
DR eggNOG; KOG0390; Eukaryota.
DR GeneTree; ENSGT00940000156897; -.
DR HOGENOM; CLU_000315_10_5_1; -.
DR InParanoid; P70270; -.
DR OMA; YTEHERM; -.
DR OrthoDB; 93727at2759; -.
DR PhylomeDB; P70270; -.
DR TreeFam; TF101224; -.
DR BioGRID-ORCS; 19366; 14 hits in 109 CRISPR screens.
DR ChiTaRS; Rad54l; mouse.
DR PRO; PR:P70270; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P70270; protein.
DR Bgee; ENSMUSG00000028702; Expressed in presomitic mesoderm and 162 other tissues.
DR Genevisible; P70270; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0015616; F:DNA translocase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IGI:MGI.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:MGI.
DR GO; GO:0006302; P:double-strand break repair; IGI:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:MGI.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..747
FT /note="DNA repair and recombination protein RAD54-like"
FT /id="PRO_0000074338"
FT DOMAIN 170..345
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 500..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..9
FT /note="Required for chromatin remodeling, strand pairing
FT activities and coupling of ATPase activity"
FT /evidence="ECO:0000250"
FT MOTIF 296..299
FT /note="DEGH box"
FT COMPBIAS 9..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92698"
FT MOD_RES 515
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92698"
FT MOD_RES 572
FT /note="Phosphoserine; by NEK1"
FT /evidence="ECO:0000250|UniProtKB:Q92698"
FT CONFLICT 103
FT /note="A -> V (in Ref. 3; AAH21643)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="I -> V (in Ref. 1; CAA66380)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="I -> V (in Ref. 2; BAC40627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 84694 MW; A08DFFCB95BF8A50 CRC64;
MRRSLAPSQL ARRKPEDRSS DDEDWQPGTV TPKKRKSSSE TQVQECFLSP FRKPLTQLLN
RPPCLDSSQH EAFIRSILSK PFKVPIPNYQ GPLGSRALGL KRAGVRRALH DPLEEGALVL
YEPPPLSAHD QLKLDKEKLP VHVVVDPILS KVLRPHQREG VKFLWECVTS RRIPGSHGCI
MADEMGLGKT LQCITLMWTL LRQSPECKPE IEKAVVVSPS SLVKNWYNEV EKWLGGRIQP
LAIDGGSKDE IDRKLEGFMN QRGARVPSPI LIISYETFRL HVGVLKKGNV GLVICDEGHR
LKNSENQTYQ ALDSLNTSRR VLISGTPIQN DLLEYFSLVH FVNSGILGTA HEFKKHFELP
ILKSRDAAAS EADRQRGEER LRELIGIVNR CLIRRTSDIL SKYLPVKIEQ VVCCRLTPLQ
TELYKRFLRQ AKPEEELREG KMSVSSLSSI TSLKKLCNHP ALIYDKCVAE EDGFEGTLGI
FPPGYNSKAV EPQLSGKMLV LDYILAVTRS RSSDKVVLVS NYTQTLDLFE KLCRVRRYLY
VRLDGTMSIK KRAKVVERFN SPSSPDFVFM LSSKAGGCGL NLIGANRLVM FDPDWNPAND
EQAMARVWRD GQKKICYIYR LLSAGTIEEK IFQRQSHKKA LSSCVVDEEQ DVERHFSLGE
LKELFTLDEA SLSDTHDRLH CRRCVNNRQV WPPPDGSDCT SDLAQWNHST DKRGLQDEVL
QAAWDASSTA ITFVFHQRSH EEQRGLH
