DMC1_MOUSE
ID DMC1_MOUSE Reviewed; 340 AA.
AC Q61880;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Meiotic recombination protein DMC1/LIM15 homolog {ECO:0000305};
GN Name=Dmc1 {ECO:0000312|MGI:MGI:105393}; Synonyms=Dmc1h, Lim15;
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=8581742; DOI=10.1093/dnares/2.3.147;
RA Sato S., Kobayashi T., Hotta Y., Tabata S.;
RT "Characterization of a mouse recA-like gene specifically expressed in
RT testis.";
RL DNA Res. 2:147-150(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv; TISSUE=Testis;
RX PubMed=8602360; DOI=10.1093/nar/24.3.470;
RA Habu T., Taki T., West A., Nishimune Y., Morita T.;
RT "The mouse and human homologs of DMC1, the yeast meiosis-specific
RT homologous recombination gene, have a common unique form of exon-skipped
RT transcript in meiosis.";
RL Nucleic Acids Res. 24:470-477(1996).
RN [3]
RP INTERACTION WITH MND1/PSMC3IP HETERODIMER.
RX PubMed=15834424; DOI=10.1038/nsmb923;
RA Petukhova G.V., Pezza R.J., Vanevski F., Ploquin M., Masson J.-Y.,
RA Camerini-Otero R.D.;
RT "The Hop2 and Mnd1 proteins act in concert with Rad51 and Dmc1 in meiotic
RT recombination.";
RL Nat. Struct. Mol. Biol. 12:449-453(2005).
RN [4]
RP FUNCTION.
RX PubMed=17639081; DOI=10.1101/gad.1562907;
RA Pezza R.J., Voloshin O.N., Vanevski F., Camerini-Otero R.D.;
RT "Hop2/Mnd1 acts on two critical steps in Dmc1-promoted homologous
RT pairing.";
RL Genes Dev. 21:1758-1766(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=21307306; DOI=10.1073/pnas.1016454108;
RA Dray E., Dunlop M.H., Kauppi L., San Filippo J., Wiese C., Tsai M.S.,
RA Begovic S., Schild D., Jasin M., Keeney S., Sung P.;
RT "Molecular basis for enhancement of the meiotic DMC1 recombinase by RAD51
RT associated protein 1 (RAD51AP1).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3560-3565(2011).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=22549958; DOI=10.1101/gad.187559.112;
RA Wojtasz L., Cloutier J.M., Baumann M., Daniel K., Varga J., Fu J.,
RA Anastassiadis K., Stewart A.F., Remenyi A., Turner J.M., Toth A.;
RT "Meiotic DNA double-strand breaks and chromosome asynapsis in mice are
RT monitored by distinct HORMAD2-independent and -dependent mechanisms.";
RL Genes Dev. 26:958-973(2012).
RN [8]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=30760716; DOI=10.1038/s41467-019-08676-2;
RA Zhang J., Fujiwara Y., Yamamoto S., Shibuya H.;
RT "A meiosis-specific BRCA2 binding protein recruits recombinases to DNA
RT double-strand breaks to ensure homologous recombination.";
RL Nat. Commun. 10:722-722(2019).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=30949703; DOI=10.1093/nar/gkz226;
RA Liu H., Huang T., Li M., Li M., Zhang C., Jiang J., Yu X., Yin Y.,
RA Zhang F., Lu G., Luo M.C., Zhang L.R., Li J., Liu K., Chen Z.J.;
RT "SCRE serves as a unique synaptonemal complex fastener and is essential for
RT progression of meiosis prophase I in mice.";
RL Nucleic Acids Res. 47:5670-5683(2019).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=30746471; DOI=10.1126/sciadv.aau9780;
RA Zhang Q., Ji S.Y., Busayavalasa K., Yu C.;
RT "SPO16 binds SHOC1 to promote homologous recombination and crossing-over in
RT meiotic prophase I.";
RL Sci. Adv. 5:eaau9780-eaau9780(2019).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=32463460; DOI=10.1093/nar/gkaa406;
RA Shang Y., Huang T., Liu H., Liu Y., Liang H., Yu X., Li M., Zhai B.,
RA Yang X., Wei Y., Wang G., Chen Z., Wang S., Zhang L.;
RT "MEIOK21: a new component of meiotic recombination bridges required for
RT spermatogenesis.";
RL Nucleic Acids Res. 48:6624-6639(2020).
CC -!- FUNCTION: Participates in meiotic recombination, specifically in
CC homologous strand assimilation, which is required for the resolution of
CC meiotic double-strand breaks. {ECO:0000269|PubMed:17639081}.
CC -!- SUBUNIT: Double stacked ring-shaped homooctamer (By similarity).
CC Interacts with BRCA2 (By similarity). Interacts with the MND1-PSMC3IP
CC heterodimer (PubMed:15834424). Interacts with RAD51AP1; the interaction
CC is direct and stimulates DMC1-mediated homologous recombination (By
CC similarity). {ECO:0000250|UniProtKB:Q14565,
CC ECO:0000269|PubMed:15834424}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21307306}. Chromosome
CC {ECO:0000269|PubMed:21307306, ECO:0000269|PubMed:22549958,
CC ECO:0000269|PubMed:30746471, ECO:0000269|PubMed:30760716,
CC ECO:0000269|PubMed:30949703, ECO:0000269|PubMed:32463460}.
CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:30760716,
CC ECO:0000269|PubMed:8581742}.
CC -!- DEVELOPMENTAL STAGE: In spermatocytes, shows punctate localization
CC along chromosome axes specifically in early meiotic prophase I cells.
CC Foci start to appear from the leptotene stage, reach their greatest
CC number in the zygotene stage, in the early pachytene stage, the DMC1
CC foci mostly disappeared from autosomes and became restricted to the sex
CC chromosomes. {ECO:0000269|PubMed:30760716}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
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DR EMBL; D58419; BAA09590.1; -; mRNA.
DR EMBL; D64107; BAA10969.1; -; mRNA.
DR CCDS; CCDS27644.1; -.
DR PIR; JC4191; JC4191.
DR RefSeq; NP_034189.1; NM_010059.3.
DR AlphaFoldDB; Q61880; -.
DR SMR; Q61880; -.
DR BioGRID; 199244; 1.
DR CORUM; Q61880; -.
DR STRING; 10090.ENSMUSP00000023065; -.
DR iPTMnet; Q61880; -.
DR PhosphoSitePlus; Q61880; -.
DR PaxDb; Q61880; -.
DR PRIDE; Q61880; -.
DR ProteomicsDB; 277345; -.
DR Antibodypedia; 246; 417 antibodies from 34 providers.
DR Ensembl; ENSMUST00000023065; ENSMUSP00000023065; ENSMUSG00000022429.
DR GeneID; 13404; -.
DR KEGG; mmu:13404; -.
DR UCSC; uc007wtu.2; mouse.
DR CTD; 11144; -.
DR MGI; MGI:105393; Dmc1.
DR VEuPathDB; HostDB:ENSMUSG00000022429; -.
DR eggNOG; KOG1434; Eukaryota.
DR GeneTree; ENSGT00760000119398; -.
DR HOGENOM; CLU_041732_0_0_1; -.
DR InParanoid; Q61880; -.
DR OMA; GGINDPD; -.
DR OrthoDB; 877394at2759; -.
DR PhylomeDB; Q61880; -.
DR TreeFam; TF300698; -.
DR BioGRID-ORCS; 13404; 0 hits in 108 CRISPR screens.
DR PRO; PR:Q61880; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61880; protein.
DR Bgee; ENSMUSG00000022429; Expressed in morula and 111 other tissues.
DR ExpressionAtlas; Q61880; baseline and differential.
DR Genevisible; Q61880; MM.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IMP:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR GO; GO:0048477; P:oogenesis; IMP:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0007131; P:reciprocal meiotic recombination; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0042148; P:strand invasion; IBA:GO_Central.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011940; Dmc1.
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; TIGR02238; recomb_DMC1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Chromosome; DNA-binding; Meiosis;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..340
FT /note="Meiotic recombination protein DMC1/LIM15 homolog"
FT /id="PRO_0000122919"
FT BINDING 126..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 230
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 230
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 233
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 236
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 236
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 242
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 242
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 311
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
SQ SEQUENCE 340 AA; 37821 MW; 23EAB08D6E668637 CRC64;
MKEDQVVQEE SGFQDDEESL FQDIDLLQKH GINMADIKKL KSVGICTIKG IQMTTRRALC
NVKGLSEAKV EKIKEAANKL IEPGFLTAFQ YSERRKMVFH ITTGSQEFDK LLGGGIESMA
ITEAFGEFRT GKTQLSHTLC VTAQLPGTGG YSGGKIIFID TENTFRPDRL RDIADRFNVD
HEAVLDNVLY ARAYTSEHQM ELLDYVAAKF HEEAGIFKLL IIDSIMALFR VDFSGRGELA
ERQQKLAQML SRLQKISEEY NVAVFVTNQM TADPGATMTF QADPKKPIGG HILAHASTTR
ISLRKGRGEL RIAKIYDSPE MPENEATFAI TAGGIGDAKE
