PMS1_ARATH
ID PMS1_ARATH Reviewed; 923 AA.
AC Q941I6; O81287; Q8GY98;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DNA mismatch repair protein PMS1;
DE AltName: Full=Postmeiotic segregation protein 1;
DE AltName: Full=Protein POSTMEIOTIC SEGREGATION 1;
GN Name=PMS1; OrderedLocusNames=At4g02460; ORFNames=T14P8.6;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RX AGRICOLA=IND43639031; DOI=10.1016/j.plantsci.2004.04.012;
RA Alou A.H., Jean M., Domingue O., Belzile F.J.;
RT "Structure and expression of AtPMS1, the Arabidopsis ortholog of the yeast
RT DNA repair gene PMS1.";
RL Plant Sci. 167:447-456(2004).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP MUTAGENESIS OF 108-PHE-ARG-109, AND FUNCTION.
RX PubMed=15604748; DOI=10.1007/s11103-004-3472-0;
RA Alou A.H., Azaiez A., Jean M., Belzile F.J.;
RT "Involvement of the Arabidopsis thaliana AtPMS1 gene in somatic repeat
RT instability.";
RL Plant Mol. Biol. 56:339-349(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19115045; DOI=10.1007/s11103-008-9447-9;
RA Li L., Dion E., Richard G., Domingue O., Jean M., Belzile F.J.;
RT "The Arabidopsis DNA mismatch repair gene PMS1 restricts somatic
RT recombination between homeologous sequences.";
RL Plant Mol. Biol. 69:675-684(2009).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=20571910; DOI=10.1007/s11033-010-0203-2;
RA Galles C., Gomez R.L., Spampinato C.P.;
RT "PMS1 from Arabidopsis thaliana: optimization of protein overexpression in
RT Escherichia coli.";
RL Mol. Biol. Rep. 38:1063-1070(2011).
RN [8]
RP FUNCTION.
RX PubMed=23184005; DOI=10.1007/s11033-012-2269-5;
RA Galles C., Spampinato C.P.;
RT "Yeast mutator phenotype enforced by Arabidopsis PMS1 expression.";
RL Mol. Biol. Rep. 40:2107-2114(2013).
CC -!- FUNCTION: Required for DNA mismatch repair (MMR), correcting base-base
CC mismatches and insertion-deletion loops (IDLs) resulting from DNA
CC replication, DNA damage or from recombination events between non-
CC identical sequences during meiosis. Component of the MutLalpha
CC heterodimer that forms a ternary complex with the MutS heterodimers,
CC which initially recognize the DNA mismatches. This complex is thought
CC to be responsible for directing the downsteam MMR events, including
CC strand discrimination, excision, and resynthesis. Plays a major role in
CC maintaining the genetic stability of simple sequence repeats and in the
CC repair of heteroduplex sites present in meiotic recombination
CC intermediates. Does not seem to be required for homologous somatic
CC recombination. {ECO:0000269|PubMed:15604748,
CC ECO:0000269|PubMed:19115045, ECO:0000269|PubMed:23184005}.
CC -!- SUBUNIT: Heterodimer of MLH1 and PMS1, called MutLalpha, which is the
CC major MMR MutL activity correcting base-base mismatches as well as
CC IDLs. The heterodimer binds double strand DNA independently of a
CC mismatch with positive cooperativity and has more than one DNA binding
CC site. Forms a ternary complex with either the MSH2-MSH6 (MutSalpha) or
CC the MSH2-MSH3 heterodimer (MutSbeta), which recognize and bind to
CC mismatch DNA. Ternary complex formation is promoted by ATP binding.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q941I6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q941I6-2; Sequence=VSP_046044, VSP_046045, VSP_046046;
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in mature leaves.
CC Detected in rapidly dividing tissues. {ECO:0000269|PubMed:20571910,
CC ECO:0000269|Ref.1}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility. Increased homeologous
CC recombination frequency. {ECO:0000269|PubMed:19115045}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site and an intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC19275.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80739.1; 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; AY047228; AAL01156.1; -; mRNA.
DR EMBL; AF069298; AAC19275.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161494; CAB80739.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82175.1; -; Genomic_DNA.
DR EMBL; AK117777; BAC42424.1; -; mRNA.
DR PIR; T01304; T01304.
DR RefSeq; NP_567236.1; NM_116479.4. [Q941I6-1]
DR AlphaFoldDB; Q941I6; -.
DR SMR; Q941I6; -.
DR STRING; 3702.AT4G02460.1; -.
DR iPTMnet; Q941I6; -.
DR PaxDb; Q941I6; -.
DR PRIDE; Q941I6; -.
DR ProteomicsDB; 226211; -. [Q941I6-1]
DR EnsemblPlants; AT4G02460.1; AT4G02460.1; AT4G02460. [Q941I6-1]
DR GeneID; 827997; -.
DR Gramene; AT4G02460.1; AT4G02460.1; AT4G02460. [Q941I6-1]
DR KEGG; ath:AT4G02460; -.
DR Araport; AT4G02460; -.
DR TAIR; locus:2133274; AT4G02460.
DR eggNOG; KOG1978; Eukaryota.
DR HOGENOM; CLU_004131_0_2_1; -.
DR InParanoid; Q941I6; -.
DR OMA; HIPRPSK; -.
DR OrthoDB; 735423at2759; -.
DR PhylomeDB; Q941I6; -.
DR PRO; PR:Q941I6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q941I6; baseline and differential.
DR Genevisible; Q941I6; AT.
DR GO; GO:0032300; C:mismatch repair complex; IBA:GO_Central.
DR GO; GO:0032389; C:MutLalpha complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IMP:TAIR.
DR GO; GO:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0006298; P:mismatch repair; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0048316; P:seed development; IMP:TAIR.
DR Gene3D; 3.30.1370.100; -; 1.
DR Gene3D; 3.30.1540.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR014762; DNA_mismatch_repair_CS.
DR InterPro; IPR002099; DNA_mismatch_repair_N.
DR InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR038973; MutL/Mlh/Pms.
DR InterPro; IPR014790; MutL_C.
DR InterPro; IPR042120; MutL_C_dimsub.
DR InterPro; IPR042121; MutL_C_regsub.
DR InterPro; IPR037198; MutL_C_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10073; PTHR10073; 1.
DR Pfam; PF01119; DNA_mis_repair; 1.
DR Pfam; PF08676; MutL_C; 1.
DR SMART; SM01340; DNA_mis_repair; 1.
DR SMART; SM00853; MutL_C; 1.
DR SUPFAM; SSF118116; SSF118116; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00585; mutl; 1.
DR PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..923
FT /note="DNA mismatch repair protein PMS1"
FT /id="PRO_0000421835"
FT REGION 543..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 288
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_046044"
FT VAR_SEQ 730..734
FT /note="HAADE -> SSSLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_046045"
FT VAR_SEQ 735..923
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_046046"
FT MUTAGEN 108..109
FT /note="FR->AF: Defective in MMR activity. Increase in
FT microsatellite instability."
FT /evidence="ECO:0000269|PubMed:15604748"
SQ SEQUENCE 923 AA; 102684 MW; 178ACAA4B982F8FB CRC64;
MQGDSSPSPT TTSSPLIRPI NRNVIHRICS GQVILDLSSA VKELVENSLD AGATSIEINL
RDYGEDYFQV IDNGCGISPT NFKVLALKHH TSKLEDFTDL LNLTTYGFRG EALSSLCALG
NLTVETRTKN EPVATLLTFD HSGLLTAEKK TARQIGTTVT VRKLFSNLPV RSKEFKRNIR
KEYGKLVSLL NAYALIAKGV RFVCSNTTGK NPKSVVLNTQ GRGSLKDNII TVFGISTFTS
LQPVSICVSE DCRVEGFLSK PGQGTGRNLA DRQYFFINGR PVDMPKVSKL VNELYKDTSS
RKYPVTILDF IVPGGACDLN VTPDKRKVFF SDETSVIGSL REGLNEIYSS SNASYIVNRF
EENSEQPDKA GVSSFQKKSN LLSEGIVLDV SSKTRLGEAI EKENPSLREV EIDNSSPMEK
FKFEIKACGT KKGEGSLSVH DVTHLDKTPS KGLPQLNVTE KVTDASKDLS SRSSFAQSTL
NTFVTMGKRK HENISTILSE TPVLRNQTSS YRVEKSKFEV RALASRCLVE GDQLDDMVIS
KEDMTPSERD SELGNRISPG TQADNVERHE REHEKPIRFE EPTSDNTLTK GDVERVSEDN
PRCSQPLRSV ATVLDSPAQS TGPKMFSTLE FSFQNLRTRR LERLSRLQST GYVSKCMNTP
QPKKCFAAAT LELSQPDDEE RKARALAAAT SELERLFRKE DFRRMQVLGQ FNLGFIIAKL
ERDLFIVDQH AADEKFNFEH LARSTVLNQQ PLLQPLNLEL SPEEEVTVLM HMDIIRENGF
LLEENPSAPP GKHFRLRAIP YSKNITFGVE DLKDLISTLG DNHGECSVAS SYKTSKTDSI
CPSRVRAMLA SRACRSSVMI GDPLRKNEMQ KIVEHLADLE SPWNCPHGRP TMRHLVDLTT
LLTLPDDDNV NDDDDDDATI SLA
