MSH3_MOUSE
ID MSH3_MOUSE Reviewed; 1091 AA.
AC P13705;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA mismatch repair protein Msh3;
DE AltName: Full=Protein repair-1;
DE Short=REP-1;
DE AltName: Full=Protein repair-3;
DE Short=REP-3;
GN Name=Msh3; Synonyms=Rep-3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu K., Niu L., Linton J.P., Crouse G.F.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926796; DOI=10.1016/0378-1119(94)90062-0;
RA Liu K., Niu L., Linton J.P., Crouse G.F.;
RT "Characterization of the mouse Rep-3 gene: sequence similarities to
RT bacterial and yeast mismatch-repair proteins.";
RL Gene 147:169-177(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-917.
RX PubMed=2674679; DOI=10.1128/mcb.9.7.3058-3072.1989;
RA Linton J.P., Yen J.-Y.J., Selby E., Chen Z., Chinsky J.M., Liu K.,
RA Kellems R.E., Crouse G.F.;
RT "Dual bidirectional promoters at the mouse dhfr locus: cloning and
RT characterization of two mRNA classes of the divergently transcribed Rep-1
RT gene.";
RL Mol. Cell. Biol. 9:3058-3072(1989).
CC -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC (MMR). Heterodimerizes with MSH2 to form MutS beta which binds to DNA
CC mismatches thereby initiating DNA repair. When bound, the MutS beta
CC heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. MutS beta recognizes large insertion-deletion loops (IDL) up to
CC 13 nucleotides long. After mismatch binding, forms a ternary complex
CC with the MutL alpha heterodimer, which is thought to be responsible for
CC directing the downstream MMR events, including strand discrimination,
CC excision, and resynthesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at
CC least of MSH2, MSH3, MSH6, PMS1 and MLH1. Heterodimer consisting of
CC MSH2-MSH3 (MutS beta). Forms a ternary complex with MutL alpha (MLH1-
CC PMS1). Interacts with EXO1. Interacts with MCM9.
CC {ECO:0000250|UniProtKB:P20585}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
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DR EMBL; M80360; AAA40052.1; -; mRNA.
DR EMBL; L10319; AAB60711.1; -; Genomic_DNA.
DR EMBL; L10295; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10296; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10297; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10298; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10299; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10300; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10301; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10304; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10305; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10306; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10307; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10308; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10309; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10310; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10311; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10312; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10313; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10314; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10315; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10316; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10317; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; L10318; AAB60711.1; JOINED; Genomic_DNA.
DR EMBL; M24919; AAA40051.1; ALT_SEQ; mRNA.
DR PIR; A32495; A32495.
DR RefSeq; NP_034959.2; NM_010829.2.
DR AlphaFoldDB; P13705; -.
DR SMR; P13705; -.
DR BioGRID; 201526; 2.
DR ComplexPortal; CPX-78; DNA mismatch repair MutSbeta complex.
DR STRING; 10090.ENSMUSP00000140002; -.
DR iPTMnet; P13705; -.
DR PhosphoSitePlus; P13705; -.
DR EPD; P13705; -.
DR MaxQB; P13705; -.
DR PaxDb; P13705; -.
DR PeptideAtlas; P13705; -.
DR PRIDE; P13705; -.
DR ProteomicsDB; 291513; -.
DR DNASU; 17686; -.
DR GeneID; 17686; -.
DR KEGG; mmu:17686; -.
DR CTD; 4437; -.
DR MGI; MGI:109519; Msh3.
DR eggNOG; KOG0218; Eukaryota.
DR InParanoid; P13705; -.
DR OrthoDB; 138168at2759; -.
DR PhylomeDB; P13705; -.
DR Reactome; R-MMU-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR BioGRID-ORCS; 17686; 2 hits in 107 CRISPR screens.
DR ChiTaRS; Msh3; mouse.
DR PRO; PR:P13705; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P13705; protein.
DR GO; GO:0032302; C:MutSbeta complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0019237; F:centromeric DNA binding; IDA:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IGI:MGI.
DR GO; GO:0032139; F:dinucleotide insertion or deletion binding; ISO:MGI.
DR GO; GO:0032181; F:dinucleotide repeat insertion binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IGI:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0030983; F:mismatched DNA binding; ISO:MGI.
DR GO; GO:0032142; F:single guanine insertion binding; ISO:MGI.
DR GO; GO:0003697; F:single-stranded DNA binding; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; ISO:MGI.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; ISO:MGI.
DR GO; GO:0006298; P:mismatch repair; IMP:MGI.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; ISO:MGI.
DR GO; GO:0051096; P:positive regulation of helicase activity; ISO:MGI.
DR GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; IMP:MGI.
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; 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; 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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1091
FT /note="DNA mismatch repair protein Msh3"
FT /id="PRO_0000115193"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 850..857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20585"
FT CONFLICT 505..506
FT /note="MV -> IL (in Ref. 2; AAB60711)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="T -> A (in Ref. 2; AAB60711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1091 AA; 123074 MW; 822BF422436FD513 CRC64;
MPRGKSASGG STAAGPGPGR QTVLSRFFRS AGSLRSSASS TEPAEKVTEG DSRKRSLGNG
GPTKKKARKV PEKEEENISV ASHHPEAKKC LRPRIVLKSL EKLKEFCCDS ALPQNRVQTE
ALRERLEVLP RCTDFEDITL QRAKNAVLSE DSKSQANQKD SQFGPCPEVF QKTSDCKPFN
KRSKSVYTPL ELQYLDMKQQ HKDAVLCVEC GYKYRFFGED AEIAARELNI YCHLDHNFMT
ASIPTHRLFV HVRRLVAKGY KVGVVKQTET AALKAIGDNK SSVFSRKLTA LYTKSTLIGE
DVNPLIRLDD SVNIDEVMTD TSTNYLLCIY EEKENIKDKK KGNLSVGVVG VQPATGEVVF
DCFQDSASRL ELETRISSLQ PVELLLPSDL SEPTEMLIQR ATNVSVRDDR IRVERMNNTY
FEYSHAFQTV TEFYAREIVD SQGSQSLSGV INLEKPVICA LAAVIRYLKE FNLEKMLSKP
ESFKQLSSGM EFMRINGTTL RNLEMVQNQT DMKTKGSLLW VLDHTKTSFG RRKLKNWVTQ
PLLKLREINA RLDAVSDVLH SESSVFEQIE NLLRKLPDVE RGLCSIYHKK CSTQEFFLIV
KSLCQLKSEL QALMPAVNSH VQSDLLRALI VELLSPVEHY LKVLNGPAAK VGDKTELFKD
LSDFPLIKKR KNEIQEVIHS IQMRLQEFRK ILKLPSLQYV TVSGQEFMIE IKNSAVSCIP
ADWVKVGSTK AVSRFHPPFI VESYRRLNQL REQLVLDCNA EWLGFLENFG EHYHTLCKAV
DHLATVDCIF SLAKVAKQGN YCRPTLQEEK KIIIKNGRHP MIDVLLGEQD QFVPNSTSLS
DSERVMIITG PNMGGKSSYI KQVTLVTIMA QIGSYVPAEE ATIGIVDGIF TRMGAADNIY
KGRSTFMEQL TDTAEIIRRA SPQSLVILDE LGRGTSTHDG IAIAYATLEY FIRDVKSLTL
FVTHYPPVCE LEKCYPEQVG NYHMGFLVNE DESKQDSGDM EQMPDSVTFL YQITRGIAAR
SYGLNVAKLA DVPREVLQKA AHKSKELEGL VSLRRKRLEC FTDLWMTHSV KDLHTWADKL
EMEEIQTSLP H
