MSH2_ARATH
ID MSH2_ARATH Reviewed; 937 AA.
AC O24617; Q9SQ60; Q9ZR93;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=DNA mismatch repair protein MSH2;
DE Short=AtMSH2;
DE AltName: Full=MutS protein homolog 2;
GN Name=MSH2; OrderedLocusNames=At3g18524; ORFNames=MYF24.25;
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 / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9342879; DOI=10.1104/pp.115.2.833;
RA Culligan K.M., Hays J.B.;
RT "DNA mismatch repair in plants. An Arabidopsis thaliana gene that predicts
RT a protein belonging to the MSH2 subfamily of eukaryotic MutS homologs.";
RL Plant Physiol. 115:833-839(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=10517319; DOI=10.1007/pl00008640;
RA Ade J., Belzile F., Philippe H., Doutriaux M.P.;
RT "Four mismatch repair paralogues coexist in Arabidopsis thaliana: AtMSH2,
RT AtMSH3, AtMSH6-1 and AtMSH6-2.";
RL Mol. Gen. Genet. 262:239-249(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 665-781.
RA Cerovic G., Radman M.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH MSH3; MSH6 AND MSH7.
RX PubMed=10852942; DOI=10.2307/3871224;
RA Culligan K.M., Hays J.B.;
RT "Arabidopsis MutS homologs-AtMSH2, AtMSH3, AtMSH6, and a novel AtMSH7-form
RT three distinct protein heterodimers with different specificities for
RT mismatched DNA.";
RL Plant Cell 12:991-1002(2000).
RN [8]
RP FUNCTION.
RX PubMed=11550901; DOI=10.1139/gen-44-4-651;
RA Ade J., Haffani Y., Beizile F.J.;
RT "Functional analysis of the Arabidopsis thaliana mismatch repair gene
RT MSH2.";
RL Genome 44:651-657(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12970498; DOI=10.1104/pp.103.023952;
RA Leonard J.M., Bollmann S.R., Hays J.B.;
RT "Reduction of stability of arabidopsis genomic and transgenic DNA-repeat
RT sequences (microsatellites) by inactivation of AtMSH2 mismatch-repair
RT function.";
RL Plant Physiol. 133:328-338(2003).
RN [10]
RP FUNCTION, AND INTERACTION WITH MSH6 AND MSH7.
RX PubMed=14530450; DOI=10.1093/nar/gkg780;
RA Wu S.Y., Culligan K., Lamers M., Hays J.;
RT "Dissimilar mispair-recognition spectra of Arabidopsis DNA-mismatch-repair
RT proteins MSH2*MSH6 (MutSalpha) and MSH2*MSH7 (MutSgamma).";
RL Nucleic Acids Res. 31:6027-6034(2003).
RN [11]
RP FUNCTION.
RX PubMed=16311517; DOI=10.1038/sj.embor.7400577;
RA Emmanuel E., Yehuda E., Melamed-Bessudo C., Avivi-Ragolsky N., Levy A.A.;
RT "The role of AtMSH2 in homologous recombination in Arabidopsis thaliana.";
RL EMBO Rep. 7:100-105(2006).
RN [12]
RP FUNCTION.
RX PubMed=16507082; DOI=10.1111/j.1365-313x.2006.02657.x;
RA Li L., Jean M., Belzile F.;
RT "The impact of sequence divergence and DNA mismatch repair on homeologous
RT recombination in Arabidopsis.";
RL Plant J. 45:908-916(2006).
RN [13]
RP FUNCTION.
RX PubMed=17294256; DOI=10.1007/s11103-006-9128-5;
RA Lafleuriel J., Degroote F., Depeiges A., Picard G.;
RT "Impact of the loss of AtMSH2 on double-strand break-induced recombination
RT between highly diverged homeologous sequences in Arabidopsis thaliana
RT germinal tissues.";
RL Plant Mol. Biol. 63:833-846(2007).
RN [14]
RP FUNCTION, AND INDUCTION BY UV-B.
RX PubMed=21307385; DOI=10.1093/jxb/err001;
RA Lario L.D., Ramirez-Parra E., Gutierrez C., Casati P., Spampinato C.P.;
RT "Regulation of plant MSH2 and MSH6 genes in the UV-B-induced DNA damage
RT response.";
RL J. Exp. Bot. 62:2925-2937(2011).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Forms three different heterodimers: MutS alpha (MSH2-MSH6
CC heterodimer), MutS beta (MSH2-MSH3 heterodimer) and MutS gamma (MSH2-
CC MSH7 heterodimer) which binds to DNA mismatches thereby initiating DNA
CC repair. MutS alpha and MutS beta recognize single base mismatches and
CC trinucleotide insertion-deletion loops (IDL) in the DNA. MutS gamma
CC recognizes specifically the T/G single base mismatch. Plays a role in
CC DNA homologous recombination repair and has a broad range of anti-
CC recombination effects. Can suppress recombination between divergent
CC direct repeats in somatic cells and possesses an anti-recombination
CC meiotic effect. Is involved in a UV-B-induced DNA damage response
CC pathway. {ECO:0000269|PubMed:10852942, ECO:0000269|PubMed:11550901,
CC ECO:0000269|PubMed:12970498, ECO:0000269|PubMed:14530450,
CC ECO:0000269|PubMed:16311517, ECO:0000269|PubMed:16507082,
CC ECO:0000269|PubMed:17294256, ECO:0000269|PubMed:21307385}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH6 (MutS alpha), MSH2-MSH3
CC (MutS beta) and MSH2-MSH7 (MutS gamma).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- INDUCTION: By UV-B. {ECO:0000269|PubMed:21307385}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:12970498}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
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DR EMBL; AF026549; AAB81282.1; -; mRNA.
DR EMBL; AF109243; AAD04176.1; -; Genomic_DNA.
DR EMBL; AF002706; AAB82649.1; -; mRNA.
DR EMBL; AF003005; AAB82650.1; -; Genomic_DNA.
DR EMBL; AB026658; BAB01119.1; -; Genomic_DNA.
DR EMBL; AP001303; BAB01119.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE76112.1; -; Genomic_DNA.
DR EMBL; U87911; AAD00647.1; -; mRNA.
DR RefSeq; NP_566804.3; NM_113607.4.
DR AlphaFoldDB; O24617; -.
DR SMR; O24617; -.
DR BioGRID; 6716; 6.
DR STRING; 3702.AT3G18524.1; -.
DR PaxDb; O24617; -.
DR PRIDE; O24617; -.
DR ProteomicsDB; 239001; -.
DR EnsemblPlants; AT3G18524.1; AT3G18524.1; AT3G18524.
DR GeneID; 821383; -.
DR Gramene; AT3G18524.1; AT3G18524.1; AT3G18524.
DR KEGG; ath:AT3G18524; -.
DR Araport; AT3G18524; -.
DR TAIR; locus:2095097; AT3G18524.
DR eggNOG; KOG0219; Eukaryota.
DR HOGENOM; CLU_002472_10_0_1; -.
DR InParanoid; O24617; -.
DR OMA; LFRIYQV; -.
DR OrthoDB; 138168at2759; -.
DR PhylomeDB; O24617; -.
DR PRO; PR:O24617; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O24617; baseline and differential.
DR Genevisible; O24617; AT.
DR GO; GO:0032301; C:MutSalpha complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0003684; F:damaged DNA binding; IDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IDA:TAIR.
DR GO; GO:0006298; P:mismatch repair; IMP:TAIR.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0045128; P:negative regulation of reciprocal meiotic recombination; IMP:TAIR.
DR GO; GO:0006290; P:pyrimidine dimer repair; IMP:TAIR.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR011184; DNA_mismatch_repair_Msh2.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR InterPro; IPR036187; DNA_mismatch_repair_MutS_sf.
DR InterPro; IPR007860; DNA_mmatch_repair_MutS_con_dom.
DR InterPro; IPR032642; Msh2.
DR InterPro; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11361; PTHR11361; 1.
DR PANTHER; PTHR11361:SF35; PTHR11361:SF35; 1.
DR Pfam; PF01624; MutS_I; 1.
DR Pfam; PF05188; MutS_II; 1.
DR Pfam; PF05192; MutS_III; 1.
DR Pfam; PF05190; MutS_IV; 1.
DR Pfam; PF00488; MutS_V; 1.
DR PIRSF; PIRSF005813; MSH2; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..937
FT /note="DNA mismatch repair protein MSH2"
FT /id="PRO_0000115187"
FT REGION 861..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 666..673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VARIANT 404
FT /note="T -> A (in strain: cv. Landsberg erecta)"
FT VARIANT 468
FT /note="S -> N (in strain: cv. Landsberg erecta)"
FT VARIANT 624
FT /note="S -> L (in strain: cv. Landsberg erecta)"
FT VARIANT 737
FT /note="S -> T (in strain: cv. Landsberg erecta)"
FT VARIANT 902
FT /note="I -> M (in strain: cv. Landsberg erecta)"
FT CONFLICT 781
FT /note="F -> Y (in Ref. 6; AAD00647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 937 AA; 105503 MW; BDE4D207FCF7C9B4 CRC64;
MEGNFEEQNK LPELKLDAKQ AQGFLSFYKT LPNDTRAVRF FDRKDYYTAH GENSVFIAKT
YYHTTTALRQ LGSGSNALSS VSISRNMFET IARDLLLERN DHTVELYEGS GSNWRLVKTG
SPGNIGSFED VLFANNEMQD TPVVVSIFPS FHDGRCVIGM AYVDLTRRVL GLAEFLDDSR
FTNLESSLIA LGAKECIFPA ESGKSNECKS LYDSLERCAV MITERKKHEF KGRDLDSDLK
RLVKGNIEPV RDLVSGFDLA TPALGALLSF SELLSNEDNY GNFTIRRYDI GGFMRLDSAA
MRALNVMESK TDANKNFSLF GLMNRTCTAG MGKRLLHMWL KQPLVDLNEI KTRLDIVQCF
VEEAGLRQDL RQHLKRISDV ERLLRSLERR RGGLQHIIKL YQSTIRLPFI KTAMQQYTGE
FASLISERYL KKLEALSDQD HLGKFIDLVE CSVDLDQLEN GEYMISSSYD TKLASLKDQK
ELLEQQIHEL HKKTAIELDL QVDKALKLDK AAQFGHVFRI TKKEEPKIRK KLTTQFIVLE
TRKDGVKFTN TKLKKLGDQY QSVVDDYRSC QKELVDRVVE TVTSFSEVFE DLAGLLSEMD
VLLSFADLAA SCPTPYCRPE ITSSDAGDIV LEGSRHPCVE AQDWVNFIPN DCRLMRGKSW
FQIVTGPNMG GKSTFIRQVG VIVLMAQVGS FVPCDKASIS IRDCIFARVG AGDCQLRGVS
TFMQEMLETA SILKGASDKS LIIIDELGRG TSTYDGFGLA WAICEHLVQV KRAPTLFATH
FHELTALAQA NSEVSGNTVG VANFHVSAHI DTESRKLTML YKVEPGACDQ SFGIHVAEFA
NFPESVVALA REKAAELEDF SPSSMIINNE ESGKRKSRED DPDEVSRGAE RAHKFLKEFA
AIPLDKMELK DSLQRVREMK DELEKDAADC HWLRQFL
