MSH3_ARATH
ID MSH3_ARATH Reviewed; 1081 AA.
AC O65607; O81818;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE Short=AtMSH3;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=At4g25540; ORFNames=M7J2.90;
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 [MRNA].
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 [2]
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 [3]
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 [4]
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).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Forms the heterodimer MutS beta (MSH2-MSH3 heterodimer) which
CC binds to DNA mismatches thereby initiating DNA repair. MutS beta
CC recognizes single base mismatches and trinucleotide insertion-deletion
CC loops (IDL) in the DNA. {ECO:0000269|PubMed:10852942}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18172.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ007791; CAA07684.1; -; mRNA.
DR EMBL; AL022197; CAA18172.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85075.1; -; Genomic_DNA.
DR PIR; T05793; T05793.
DR PIR; T51613; T51613.
DR RefSeq; NP_194284.2; NM_118686.3.
DR AlphaFoldDB; O65607; -.
DR SMR; O65607; -.
DR BioGRID; 13946; 1.
DR STRING; 3702.AT4G25540.1; -.
DR iPTMnet; O65607; -.
DR PaxDb; O65607; -.
DR PRIDE; O65607; -.
DR ProteomicsDB; 238914; -.
DR EnsemblPlants; AT4G25540.1; AT4G25540.1; AT4G25540.
DR GeneID; 828659; -.
DR Gramene; AT4G25540.1; AT4G25540.1; AT4G25540.
DR KEGG; ath:AT4G25540; -.
DR Araport; AT4G25540; -.
DR TAIR; locus:2131829; AT4G25540.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_2_1; -.
DR InParanoid; O65607; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR PhylomeDB; O65607; -.
DR PRO; PR:O65607; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65607; baseline and differential.
DR Genevisible; O65607; AT.
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; IDA:TAIR.
DR GO; GO:0006298; P:mismatch repair; ISS:TAIR.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
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 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 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 ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1081
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000115194"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 817..824
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1081 AA; 119366 MW; 42A4F2BA92DAD288 CRC64;
MGKQKQQTIS RFFAPKPKSP THEPNPVAES STPPPKISAT VSFSPSKRKL LSDHLAAASP
KKPKLSPHTQ NPVPDPNLHQ RFLQRFLEPS PEEYVPETSS SRKYTPLEQQ VVELKSKYPD
VVLMVEVGYR YRFFGEDAEI AARVLGIYAH MDHNFMTASV PTFRLNFHVR RLVNAGYKIG
VVKQTETAAI KSHGANRTGP FFRGLSALYT KATLEAAEDI SGGCGGEEGF GSQSNFLVCV
VDERVKSETL GCGIEMSFDV RVGVVGVEIS TGEVVYEEFN DNFMRSGLEA VILSLSPAEL
LLGQPLSQQT EKFLVAHAGP TSNVRVERAS LDCFSNGNAV DEVISLCEKI SAGNLEDDKE
MKLEAAEKGM SCLTVHTIMN MPHLTVQALA LTFCHLKQFG FERILYQGAS FRSLSSNTEM
TLSANTLQQL EVVKNNSDGS ESGSLFHNMN HTLTVYGSRL LRHWVTHPLC DRNLISARLD
AVSEISACMG SHSSSQLSSE LVEEGSERAI VSPEFYLVLS SVLTAMSRSS DIQRGITRIF
HRTAKATEFI AVMEAILLAG KQIQRLGIKQ DSEMRSMQSA TVRSTLLRKL ISVISSPVVV
DNAGKLLSAL NKEAAVRGDL LDILITSSDQ FPELAEARQA VLVIREKLDS SIASFRKKLA
IRNLEFLQVS GITHLIELPV DSKVPMNWVK VNSTKKTIRY HPPEIVAGLD ELALATEHLA
IVNRASWDSF LKSFSRYYTD FKAAVQALAA LDCLHSLSTL SRNKNYVRPE FVDDCEPVEI
NIQSGRHPVL ETILQDNFVP NDTILHAEGE YCQIITGPNM GGKSCYIRQV ALISIMAQVG
SFVPASFAKL HVLDGVFTRM GASDSIQHGR STFLEELSEA SHIIRTCSSR SLVILDELGR
GTSTHDGVAI AYATLQHLLA EKRCLVLFVT HYPEIAEISN GFPGSVGTYH VSYLTLQKDK
GSYDHDDVTY LYKLVRGLCS RSFGFKVAQL AQIPPSCIRR AISMAAKLEA EVRARERNTR
MGEPEGHEEP RGAEESISAL GDLFADLKFA LSEEDPWKAF EFLKHAWKIA GKIRLKPTCS
F
