MSH6_ARATH
ID MSH6_ARATH Reviewed; 1324 AA.
AC O04716;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA mismatch repair protein MSH6;
DE Short=AtMSH6;
DE AltName: Full=MutS protein homolog 6;
GN Name=MSH6; Synonyms=AGAA.3, MSH6-1; OrderedLocusNames=At4g02070;
GN ORFNames=T10M13.8;
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].
RC STRAIN=cv. Landsberg erecta;
RA Till S., Granat S., Parnell L., Kaplan N., Hoffman J., Lodhi M.,
RA Johnson A.F., Dedhia N., Martienssen R., McCombie W.R.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 FUNCTION, AND INTERACTION WITH MSH2.
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 [6]
RP FUNCTION, AND INTERACTION WITH MSH2.
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 [7]
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 the heterodimer MutS alpha (MSH2-MSH6 heterodimer) which
CC binds to DNA mismatches thereby initiating DNA repair. MutS alpha
CC recognizes single base mismatches and trinucleotide insertion-deletion
CC loops (IDL) in the DNA. Is involved in a UV-B-induced DNA damage
CC response pathway. {ECO:0000269|PubMed:10852942,
CC ECO:0000269|PubMed:14530450, ECO:0000269|PubMed:21307385}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH6 (MutS alpha).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O04716-1; Sequence=Displayed;
CC -!- INDUCTION: By UV-B. {ECO:0000269|PubMed:21307385}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB57798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF001535; AAB57798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ245967; CAB53337.1; -; Genomic_DNA.
DR EMBL; AF001308; AAC78699.1; -; Genomic_DNA.
DR EMBL; AL161493; CAB80700.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82119.1; -; Genomic_DNA.
DR PIR; T01508; T01508.
DR RefSeq; NP_192116.1; NM_116438.2. [O04716-1]
DR AlphaFoldDB; O04716; -.
DR SMR; O04716; -.
DR BioGRID; 13436; 1.
DR STRING; 3702.AT4G02070.1; -.
DR iPTMnet; O04716; -.
DR PaxDb; O04716; -.
DR PRIDE; O04716; -.
DR ProteomicsDB; 250778; -. [O04716-1]
DR EnsemblPlants; AT4G02070.1; AT4G02070.1; AT4G02070. [O04716-1]
DR GeneID; 828147; -.
DR Gramene; AT4G02070.1; AT4G02070.1; AT4G02070. [O04716-1]
DR KEGG; ath:AT4G02070; -.
DR Araport; AT4G02070; -.
DR TAIR; locus:2132233; AT4G02070.
DR eggNOG; KOG0217; Eukaryota.
DR InParanoid; O04716; -.
DR OMA; SGGQRQW; -.
DR OrthoDB; 138168at2759; -.
DR PhylomeDB; O04716; -.
DR PRO; PR:O04716; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O04716; baseline and differential.
DR Genevisible; O04716; AT.
DR GO; GO:0032301; C:MutSalpha complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; ISS: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; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR InterPro; IPR017261; DNA_mismatch_repair_MutS/MSH.
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; IPR036678; MutS_con_dom_sf.
DR InterPro; IPR045076; MutS_family.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002999; Tudor.
DR PANTHER; PTHR11361; PTHR11361; 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; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR SMART; SM00534; MUTSac; 1.
DR SMART; SM00533; MUTSd; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF48334; SSF48334; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53150; SSF53150; 1.
DR SUPFAM; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1324
FT /note="DNA mismatch repair protein MSH6"
FT /id="PRO_0000115210"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..259
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1083..1090
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1324 AA; 146797 MW; 787A340272CF979C CRC64;
MAPSRRQISG RSPLVNQQRQ ITSFFGKSAS SSSSPSPSPS PSLSNKKTPK SNNPNPKSPS
PSPSPPKKTP KLNPNPSSNL PARSPSPGPD TPSPVQSKFK KPLLVIGQTP SPPQSVVITY
GDEVVGKQVR VYWPLDKKWY DGSVTFYDKG EGKHVVEYED GEEESLDLGK EKTEWVVGEK
SGDRFNRLKR GASALRKVVT DSDDDVEMGN VEEDKSDGDD SSDEDWGKNV GKEVCESEED
DVELVDENEM DEEELVEEKD EETSKVNRVS KTDSRKRKTS EVTKSGGEKK SKTDTGTILK
GFKASVVEPA KKIGQADRVV KGLEDNVLDG DALARFGARD SEKFRFLGVD RRDAKRRRPT
DENYDPRTLY LPPDFVKKLT GGQRQWWEFK AKHMDKVVFF KMGKFYELFE MDAHVGAKEL
DIQYMKGEQP HCGFPEKNFS VNIEKLVRKG YRVLVVEQTE TPDQLEQRRK ETGSKDKVVK
REVCAVVTKG TLTDGEMLLT NPDASYLMAL TEGGESLTNP TAEHNFGVCL VDVATQKIIL
GQFKDDQDCS ALSCLLSEMR PVEIIKPAKV LSYATERTIV RQTRNPLVNN LVPLSEFWDS
EKTIYEVGII YKRINCQPSS AYSSEGKILG DGSSFLPKML SELATEDKNG SLALSALGGA
IYYLRQAFLD ESLLRFAKFE SLPYCDFSNV NEKQHMVLDA AALENLEIFE NSRNGGYSGT
LYAQLNQCIT ASGKRLLKTW LARPLYNTEL IKERQDAVAI LRGENLPYSL EFRKSLSRLP
DMERLIARMF SSIEASGRNG DKVVLYEDTA KKQVQEFIST LRGCETMAEA CSSLRAILKH
DTSRRLLHLL TPGQSLPNIS SSIKYFKDAF DWVEAHNSGR VIPHEGADEE YDCACKTVEE
FESSLKKHLK EQRKLLGDAS INYVTVGKDE YLLEVPESLS GSVPHDYELC SSKKGVSRYW
TPTIKKLLKE LSQAKSEKES ALKSISQRLI GRFCEHQEKW RQLVSATAEL DVLISLAFAS
DSYEGVRCRP VISGSTSDGV PHLSATGLGH PVLRGDSLGR GSFVPNNVKI GGAEKASFIL
LTGPNMGGKS TLLRQVCLAV ILAQIGADVP AETFEVSPVD KICVRMGAKD HIMAGQSTFL
TELSETAVML TSATRNSLVV LDELGRGTAT SDGQAIAESV LEHFIEKVQC RGFFSTHYHR
LSVDYQTNPK VSLCHMACQI GEGIGGVEEV TFLYRLTPGA CPKSYGVNVA RLAGLPDYVL
QRAVIKSQEF EALYGKNHRK TDHKLAAMIK QIISSVASDS DYSASKDSLC ELHSMANTFL
RLTN
