DMC1_ARATH
ID DMC1_ARATH Reviewed; 344 AA.
AC Q39009; P93001; Q4V3A9; Q9LIL0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Meiotic recombination protein DMC1 homolog {ECO:0000305};
DE Short=AtDMC1 {ECO:0000303|PubMed:17785529};
GN Name=DMC1 {ECO:0000303|PubMed:9520262}; Synonyms=LIM15;
GN OrderedLocusNames=At3g22880; ORFNames=F5N5.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7584052; DOI=10.1093/dnares/2.2.89;
RA Sato S., Hotta Y., Tabata S.;
RT "Structural analysis of a recA-like gene in the genome of Arabidopsis
RT thaliana.";
RL DNA Res. 2:89-93(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9025299; DOI=10.1046/j.1365-313x.1997.11010001.x;
RA Klimyuk V.I., Jones J.D.G.;
RT "AtDMC1, the Arabidopsis homologue of the yeast DMC1 gene:
RT characterization, transposon-induced allelic variation and meiosis-
RT associated expression.";
RL Plant J. 11:1-14(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=9520262; DOI=10.1007/s004380050649;
RA Doutriaux M.P., Couteau F., Bergounioux C., White C.;
RT "Isolation and characterisation of the RAD51 and DMC1 homologs from
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 257:283-291(1998).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10488231; DOI=10.2307/3871042;
RA Couteau F., Belzile F., Horlow C., Grandjean O., Vezon D., Doutriaux M.P.;
RT "Random chromosome segregation without meiotic arrest in both male and
RT female meiocytes of a dmc1 mutant of Arabidopsis.";
RL Plant Cell 11:1623-1634(1999).
RN [8]
RP INTERACTION WITH BRCA2A AND BRCA2B.
RX PubMed=16415210; DOI=10.1104/pp.105.075838;
RA Dray E., Siaud N., Dubois E., Doutriaux M.P.;
RT "Interaction between Arabidopsis Brca2 and its partners Rad51, Dmc1, and
RT Dss1.";
RL Plant Physiol. 140:1059-1069(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17785529; DOI=10.1101/gad.439007;
RA Sanchez-Moran E., Santos J.-L., Jones G.H., Franklin F.C.;
RT "ASY1 mediates AtDMC1-dependent interhomolog recombination during meiosis
RT in Arabidopsis.";
RL Genes Dev. 21:2220-2233(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23300481; DOI=10.1371/journal.pgen.1003165;
RA Crismani W., Portemer V., Froger N., Chelysheva L., Horlow C.,
RA Vrielynck N., Mercier R.;
RT "MCM8 is required for a pathway of meiotic double-strand break repair
RT independent of DMC1 in Arabidopsis thaliana.";
RL PLoS Genet. 9:E1003165-E1003165(2013).
CC -!- FUNCTION: May participate in meiotic recombination, specifically in
CC homologous strand assimilation, which is required for the resolution of
CC meiotic double-strand breaks (PubMed:10488231, PubMed:23300481).
CC Mediates interhomolog recombination during meiosis (PubMed:17785529).
CC {ECO:0000269|PubMed:10488231, ECO:0000269|PubMed:17785529,
CC ECO:0000269|PubMed:23300481}.
CC -!- SUBUNIT: Double stacked ring-shaped homooctamer (By similarity).
CC Interacts with BRCA2A and BRCA2B (PubMed:16415210).
CC {ECO:0000250|UniProtKB:Q14565, ECO:0000269|PubMed:16415210}.
CC -!- INTERACTION:
CC Q39009; Q9ZNV8: AHP2; NbExp=2; IntAct=EBI-307715, EBI-1100687;
CC Q39009; Q7Y1C5: BRCA2A; NbExp=4; IntAct=EBI-307715, EBI-307680;
CC Q39009; Q7Y1C4: BRCA2B; NbExp=6; IntAct=EBI-307715, EBI-307707;
CC Q39009; Q8GYD2: MND1; NbExp=2; IntAct=EBI-307715, EBI-1554720;
CC Q39009; P94102: RAD51; NbExp=4; IntAct=EBI-307715, EBI-307687;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17785529}.
CC -!- TISSUE SPECIFICITY: Expressed in mitotic and/or meiotic tissues.
CC Expressed in roots, leaves and anthers and carpels of young fower buds.
CC {ECO:0000269|PubMed:9520262}.
CC -!- DEVELOPMENTAL STAGE: Cell cycle regulated, peaking at the S phase. It
CC is also expressed at high levels in exponentially growing cells in
CC suspension cultures. {ECO:0000269|PubMed:9520262}.
CC -!- DISRUPTION PHENOTYPE: Strongly reduced fertility and seed numbers due
CC to defects in male and female gametogenesis.
CC {ECO:0000269|PubMed:10488231, ECO:0000269|PubMed:23300481}.
CC -!- SIMILARITY: Belongs to the RecA family. DMC1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08255.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB03033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D45415; BAA08255.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U76670; AAC49617.1; -; Genomic_DNA.
DR EMBL; AP001300; BAB03033.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76687.1; -; Genomic_DNA.
DR EMBL; BT023447; AAY56438.1; -; mRNA.
DR PIR; JC4092; JC4092.
DR RefSeq; NP_188928.2; NM_113188.3.
DR AlphaFoldDB; Q39009; -.
DR SMR; Q39009; -.
DR BioGRID; 7192; 8.
DR IntAct; Q39009; 7.
DR STRING; 3702.AT3G22880.1; -.
DR PaxDb; Q39009; -.
DR PRIDE; Q39009; -.
DR ProteomicsDB; 222219; -.
DR EnsemblPlants; AT3G22880.1; AT3G22880.1; AT3G22880.
DR GeneID; 821860; -.
DR Gramene; AT3G22880.1; AT3G22880.1; AT3G22880.
DR KEGG; ath:AT3G22880; -.
DR Araport; AT3G22880; -.
DR TAIR; locus:2084558; AT3G22880.
DR eggNOG; KOG1434; Eukaryota.
DR HOGENOM; CLU_041732_0_1_1; -.
DR OMA; GGINDPD; -.
DR OrthoDB; 877394at2759; -.
DR PhylomeDB; Q39009; -.
DR PRO; PR:Q39009; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39009; baseline and differential.
DR Genevisible; Q39009; AT.
DR GO; GO:0000794; C:condensed nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000150; F:DNA strand exchange activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051026; P:chiasma assembly; IMP:TAIR.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; IDA:TAIR.
DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; TAS:TAIR.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
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; DNA-binding; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..344
FT /note="Meiotic recombination protein DMC1 homolog"
FT /id="PRO_0000122920"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 235
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 235
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 238
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 241
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 241
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 247
FT /ligand="dsDNA"
FT /ligand_id="ChEBI:CHEBI:4705"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 247
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT BINDING 315
FT /ligand="ssDNA"
FT /ligand_id="ChEBI:CHEBI:9160"
FT /evidence="ECO:0000250|UniProtKB:Q14565"
FT CONFLICT 104
FT /note="S -> L (in Ref. 1; BAA08255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37513 MW; E0A97D320A41387D CRC64;
MMASLKAEET SQMQLVEREE NDEDEDLFEM IDKLIAQGIN AGDVKKLQEA GIHTCNGLMM
HTKKNLTGIK GLSEAKVDKI CEAAEKIVNF GYMTGSDALI KRKSVVKITT GCQALDDLLG
GGIETSAITE AFGEFRSGKT QLAHTLCVTT QLPTNMKGGN GKVAYIDTEG TFRPDRIVPI
AERFGMDPGA VLDNIIYARA YTYEHQYNLL LGLAAKMSEE PFRILIVDSI IALFRVDFTG
RGELADRQQK LAQMLSRLIK IAEEFNVAVY MTNQVIADPG GGMFISDPKK PAGGHVLAHA
ATIRLLFRKG KGDTRVCKVY DAPNLAEAEA SFQITQGGIA DAKD
