MSH3_SCHPO
ID MSH3_SCHPO Reviewed; 993 AA.
AC P26359;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=DNA mismatch repair protein msh3;
DE AltName: Full=Mating-type switching protein swi4;
DE AltName: Full=MutS protein homolog 3;
GN Name=msh3; Synonyms=swi4; ORFNames=SPAC8F11.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=1317550; DOI=10.1093/nar/20.9.2271;
RA Fleck O., Michael H., Heim L.;
RT "The swi4+ gene of Schizosaccharomyces pombe encodes a homologue of
RT mismatch repair enzymes.";
RL Nucleic Acids Res. 20:2271-2278(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=11333218; DOI=10.1093/genetics/158.1.65;
RA Tornier C., Bessone S., Varlet I., Rudolph C., Darmon M., Fleck O.;
RT "Requirement for Msh6, but not for Swi4 (Msh3), in Msh2-dependent repair of
RT base-base mismatches and mononucleotide loops in Schizosaccharomyces
RT pombe.";
RL Genetics 158:65-75(2001).
RN [4]
RP FUNCTION.
RX PubMed=11333219; DOI=10.1093/genetics/158.1.77;
RA Mansour A.A., Tornier C., Lehmann E., Darmon M., Fleck O.;
RT "Control of GT repeat stability in Schizosaccharomyces pombe by mismatch
RT repair factors.";
RL Genetics 158:77-85(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. Msh3 provides substrate-
CC binding and substrate specificity to the complex. When bound, the MutS
CC beta heterodimer bends the DNA helix and shields approximately 20 base
CC pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to
CC 13 nucleotides in size, but can also repair base-base and single
CC insertion-deletion mismatches that occur during replication. After
CC mismatch binding, forms a ternary complex with the MutL alpha
CC heterodimer, which is thought to be responsible for directing the
CC downstream MMR events, including strand discrimination, excision, and
CC resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch
CC repair functions (By similarity). Involved in termination of copy-
CC synthesis during mating-type switching. {ECO:0000250,
CC ECO:0000269|PubMed:11333218, ECO:0000269|PubMed:11333219}.
CC -!- SUBUNIT: Heterodimer consisting of msh2-msh3 (MutS beta). Forms a
CC ternary complex with MutL alpha (mlh1-pms1) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {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; X61306; CAA43603.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB52164.2; -; Genomic_DNA.
DR PIR; S22569; S21964.
DR RefSeq; NP_593952.1; NM_001019379.2.
DR AlphaFoldDB; P26359; -.
DR SMR; P26359; -.
DR STRING; 4896.SPAC8F11.03.1; -.
DR iPTMnet; P26359; -.
DR PaxDb; P26359; -.
DR PRIDE; P26359; -.
DR GeneID; 2543392; -.
DR KEGG; spo:SPAC8F11.03; -.
DR PomBase; SPAC8F11.03; msh3.
DR eggNOG; KOG0218; Eukaryota.
DR HOGENOM; CLU_002472_0_1_1; -.
DR InParanoid; P26359; -.
DR PhylomeDB; P26359; -.
DR Reactome; R-SPO-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR PRO; PR:P26359; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000228; C:nuclear chromosome; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0000406; F:double-strand/single-strand DNA junction binding; ISO:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; NAS:PomBase.
DR GO; GO:0007534; P:gene conversion at mating-type locus; IMP:PomBase.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:PomBase.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
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; SSF55271; SSF55271; 1.
DR PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..993
FT /note="DNA mismatch repair protein msh3"
FT /id="PRO_0000115196"
FT REGION 97..211
FT /note="Mispair-binding domain"
FT /evidence="ECO:0000250"
FT BINDING 759..766
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 499
FT /note="R -> RCTPSEMFHVLK (in Ref. 2; CAB52164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 993 AA; 113362 MW; 44B80E553A59B708 CRC64;
MRGMSYNITH ECDAINILSD NLHEGAISED MVALSGPAIE LLENNVGSSK NSYQEDEGSS
SIDENAPLIS IKRKRRIRTV KSTSNKELVQ RKASKPTKQK SVFTPLEQQY LELKKNYQET
ILAIEVGYKF RFFGKDAKIA SEVLGISCYF EHNFLNASVP SYRIDYHLER LINFGLKVAV
VRQTETAALK STSSSRNTLF DRRVARVLTK GTTLDDSFFR FEQTQHGTLQ ASQFILCVAD
NVDKSKAKSG RVQVGLIAIQ LSSGTTVYDH FQDDFLRSEL QTRLSHFQPC ELIYSNKLSS
ESVALLNHYV STEKTCGRVV RVQHAVQQDV KLALENLQDF FSSKCIMSGS KIIELHMEKV
KSLHSLSIIC LDMAISYLME FSLEDLFVAS NFYQPFDSIS SMVLSKQALE GLELFVNQTD
HTPVGSLFWV LDRTYTRFGQ RMLQRWLQKP LVDKENIIER LDAVEELAFN SNSQVQAIRK
MLYRLPDLEK GLSRIYYQRG FYKAASAFSK NSYSCFKSAL LRRLIQQLPS ISSIIDHFLG
MFDQKEAENN NKVDMFKDID NFDLSEEPND VDYELAQEIR ELKMSILMVR TEMDFHLQEL
RDYLEYPNLE FSIWGNVKFC IEVSKGCKKI PPDWIKLSST RSLFRFHTPK IQSLLIELSS
HEENLTISSE KIYRSFLSRI SEHYNELRNV TTVLGTLDCL ISFARISSQS GYTRPEFSDK
ELLIHESRHP MIELLSDKSF VPNHIHLSSD GVRCLLITGP NMGGKSSFVK QLALSAIMAQ
SGCFVPAKSA LLPIFDSILI RMGSSDNLSV NMSTFMVEML ETKEVLSKAT EKSMVIIDEL
GRGTSTIDGE AISYAVLHYL NQYIKSYLLF VTHFPSLGIL ERRFEGQLRC FHMGYLKSKE
DFETSVSQSI SFLYKLVPGV ASKSYGLNVA RMAGIPFSIL SRATEISENY EKKHRNARKN
VFIRKVAKLL MILNAEEIDF KRLFYDLTAF EEI