MSH3_YEAST
ID MSH3_YEAST Reviewed; 1018 AA.
AC P25336; D6VR92;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DNA mismatch repair protein MSH3;
DE AltName: Full=Mismatch-binding protein;
DE Short=MBP;
DE AltName: Full=MutS protein homolog 3;
GN Name=MSH3; OrderedLocusNames=YCR092C; ORFNames=YCR1152, YCR92C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8510668; DOI=10.1007/bf00281607;
RA New L., Liu K., Crouse G.F.;
RT "The yeast gene MSH3 defines a new class of eukaryotic MutS homologues.";
RL Mol. Gen. Genet. 239:97-108(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1803822; DOI=10.1002/yea.320070910;
RA Valle G., Bergantino E., Lanfranchi G., Carignani G.;
RT "The sequence of a 6.3 kb segment of yeast chromosome III reveals an open
RT reading frame coding for a putative mismatch binding protein.";
RL Yeast 7:981-988(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP DNA-BINDING SPECIFICITY, AND INTERACTION WITH MSH2.
RX PubMed=8805366; DOI=10.1016/s0960-9822(02)70686-6;
RA Habraken Y., Sung P., Prakash L., Prakash S.;
RT "Binding of insertion/deletion DNA mismatches by the heterodimer of yeast
RT mismatch repair proteins MSH2 and MSH3.";
RL Curr. Biol. 6:1185-1187(1996).
RN [6]
RP FUNCTION, AND INTERACTION WITH MSH2.
RX PubMed=8600025; DOI=10.1101/gad.10.4.407;
RA Marsischky G.T., Filosi N., Kane M.F., Kolodner R.D.;
RT "Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent
RT mismatch repair.";
RL Genes Dev. 10:407-420(1996).
RN [7]
RP INTERACTION WITH POL30.
RX PubMed=8910404; DOI=10.1074/jbc.271.45.27987;
RA Johnson R.E., Kovvali G.K., Guzder S.N., Amin N.S., Holm C., Habraken Y.,
RA Sung P., Prakash L., Prakash S.;
RT "Evidence for involvement of yeast proliferating cell nuclear antigen in
RT DNA mismatch repair.";
RL J. Biol. Chem. 271:27987-27990(1996).
RN [8]
RP FUNCTION, DNA-BINDING SPECIFICITY, AND COMPLEX FORMATION WITH MLH1-PMS1.
RX PubMed=9368761; DOI=10.1016/s0960-9822(06)00337-x;
RA Habraken Y., Sung P., Prakash L., Prakash S.;
RT "Enhancement of MSH2-MSH3-mediated mismatch recognition by the yeast MLH1-
RT PMS1 complex.";
RL Curr. Biol. 7:790-793(1997).
RN [9]
RP FUNCTION IN MMR.
RX PubMed=9111357; DOI=10.1128/mcb.17.5.2851;
RA Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D.;
RT "Microsatellite instability in yeast: dependence on repeat unit size and
RT DNA mismatch repair genes.";
RL Mol. Cell. Biol. 17:2851-2858(1997).
RN [10]
RP FUNCTION IN NHTR.
RX PubMed=9256462; DOI=10.1073/pnas.94.17.9214;
RA Sugawara N., Paques F., Colaiacovo M., Haber J.E.;
RT "Role of Saccharomyces cerevisiae Msh2 and Msh3 repair proteins in double-
RT strand break-induced recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9214-9219(1997).
RN [11]
RP FUNCTION.
RX PubMed=9770499; DOI=10.1073/pnas.95.21.12404;
RA Flores-Rozas H., Kolodner R.D.;
RT "The Saccharomyces cerevisiae MLH3 gene functions in MSH3-dependent
RT suppression of frameshift mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12404-12409(1998).
RN [12]
RP MUTAGENESIS OF GLY-796.
RX PubMed=10523644; DOI=10.1128/mcb.19.11.7558;
RA Studamire B., Price G., Sugawara N., Haber J.E., Alani E.;
RT "Separation-of-function mutations in Saccharomyces cerevisiae MSH2 that
RT confer mismatch repair defects but do not affect nonhomologous-tail removal
RT during recombination.";
RL Mol. Cell. Biol. 19:7558-7567(1999).
RN [13]
RP MUTAGENESIS OF GLN-4 AND 10-PHE-PHE-11.
RX PubMed=11005803; DOI=10.1074/jbc.c000513200;
RA Clark A.B., Valle F., Drotschmann K., Gary R.K., Kunkel T.A.;
RT "Functional interaction of proliferating cell nuclear antigen with MSH2-
RT MSH6 and MSH2-MSH3 complexes.";
RL J. Biol. Chem. 275:36498-36501(2000).
RN [14]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP FUNCTION.
RX PubMed=16702432; DOI=10.1534/genetics.106.055616;
RA Stone J.E., Petes T.D.;
RT "Analysis of the proteins involved in the in vivo repair of base-base
RT mismatches and four-base loops formed during meiotic recombination in the
RT yeast Saccharomyces cerevisiae.";
RL Genetics 173:1223-1239(2006).
RN [18]
RP FUNCTION IN NHTR, AND DNA-BINDING.
RX PubMed=16781730; DOI=10.1016/j.jmb.2006.05.032;
RA Surtees J.A., Alani E.;
RT "Mismatch repair factor MSH2-MSH3 binds and alters the conformation of
RT branched DNA structures predicted to form during genetic recombination.";
RL J. Mol. Biol. 360:523-536(2006).
RN [19]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF LYS-158; LYS-160; PRO-203;
RP GLN-226 AND ARG-247.
RX PubMed=17157869; DOI=10.1016/j.jmb.2006.10.099;
RA Lee S.D., Surtees J.A., Alani E.;
RT "Saccharomyces cerevisiae MSH2-MSH3 and MSH2-MSH6 complexes display
RT distinct requirements for DNA binding domain I in mismatch recognition.";
RL J. Mol. Biol. 366:53-66(2007).
RN [20]
RP FUNCTION, AND IDENTIFICATION OF INITIATION SITE.
RX PubMed=17636021; DOI=10.1128/mcb.00855-07;
RA Harrington J.M., Kolodner R.D.;
RT "Saccharomyces cerevisiae Msh2-Msh3 acts in repair of base-base mispairs.";
RL Mol. Cell. Biol. 27:6546-6554(2007).
RN [21]
RP FUNCTION.
RX PubMed=17573527; DOI=10.1073/pnas.0704148104;
RA Shell S.S., Putnam C.D., Kolodner R.D.;
RT "Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-
RT binding domain combines properties of both proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10956-10961(2007).
RN [22]
RP INTERACTION WITH SAW1.
RX PubMed=18471978; DOI=10.1016/j.molcel.2008.02.028;
RA Li F., Dong J., Pan X., Oum J.-H., Boeke J.D., Lee S.E.;
RT "Microarray-based genetic screen defines SAW1, a gene required for
RT Rad1/Rad10-dependent processing of recombination intermediates.";
RL Mol. Cell 30:325-335(2008).
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 either the MutL alpha or
CC MutL beta heterodimer, which is thought to be responsible for directing
CC the downstream MMR events, including strand discrimination, excision,
CC and resynthesis. MutS beta also has a role in regulation of
CC heteroduplex formation during mitotic and meiotic recombination. MutS
CC beta binds to DNA flap structures predicted to form during
CC recombination, and is required for 3' non-homologous tail removal
CC (NHTR). MutS beta-binding alters the DNA conformation of its substrate
CC at the ds/ssDNA junction and may facilitate its recognition and/or
CC cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10
CC endonuclease. ATP binding and hydrolysis play a pivotal role in MMR and
CC NHTR. {ECO:0000269|PubMed:16702432, ECO:0000269|PubMed:16781730,
CC ECO:0000269|PubMed:17157869, ECO:0000269|PubMed:17573527,
CC ECO:0000269|PubMed:17636021, ECO:0000269|PubMed:8600025,
CC ECO:0000269|PubMed:9111357, ECO:0000269|PubMed:9256462,
CC ECO:0000269|PubMed:9368761, ECO:0000269|PubMed:9770499}.
CC -!- SUBUNIT: Heterodimer consisting of MSH2-MSH3 (MutS beta). Forms a
CC ternary complex with either MutL alpha (MLH1-PMS1) or MutL beta (MLH1-
CC MLH3). MutS beta interacts with proliferating cell nuclear antigen
CC (PCNA/POL30). Interacts with SAW1. {ECO:0000269|PubMed:18471978,
CC ECO:0000269|PubMed:8600025, ECO:0000269|PubMed:8805366,
CC ECO:0000269|PubMed:8910404}.
CC -!- INTERACTION:
CC P25336; P25847: MSH2; NbExp=3; IntAct=EBI-11362, EBI-11352;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The PIP box serves as a PCNA(POL30)-recognition and -binding
CC motif.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34803.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA42247.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA46116.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X64954; CAA46116.1; ALT_INIT; Genomic_DNA.
DR EMBL; M96250; AAA34803.1; ALT_INIT; Genomic_DNA.
DR EMBL; X59720; CAA42247.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006937; DAA07561.1; -; Genomic_DNA.
DR PIR; S19508; S19508.
DR RefSeq; NP_010016.2; NM_001178798.1.
DR AlphaFoldDB; P25336; -.
DR SMR; P25336; -.
DR BioGRID; 31064; 97.
DR ComplexPortal; CPX-1036; DNA mismatch repair MutSbeta complex.
DR DIP; DIP-2422N; -.
DR ELM; P25336; -.
DR IntAct; P25336; 36.
DR MINT; P25336; -.
DR STRING; 4932.YCR092C; -.
DR MaxQB; P25336; -.
DR PaxDb; P25336; -.
DR PRIDE; P25336; -.
DR EnsemblFungi; YCR092C_mRNA; YCR092C; YCR092C.
DR GeneID; 850454; -.
DR KEGG; sce:YCR092C; -.
DR SGD; S000000688; MSH3.
DR VEuPathDB; FungiDB:YCR092C; -.
DR eggNOG; KOG0218; Eukaryota.
DR GeneTree; ENSGT00550000074949; -.
DR HOGENOM; CLU_002472_3_1_1; -.
DR InParanoid; P25336; -.
DR OMA; LRNVHMK; -.
DR BioCyc; YEAST:G3O-29386-MON; -.
DR Reactome; R-SCE-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR PRO; PR:P25336; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25336; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032302; C:MutSbeta complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
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:0032135; F:DNA insertion or deletion binding; IDA:SGD.
DR GO; GO:0000406; F:double-strand/single-strand DNA junction binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IMP:SGD.
DR GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
DR GO; GO:0006298; P:mismatch repair; IDA:ComplexPortal.
DR GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR GO; GO:0000735; P:removal of nonhomologous ends; IMP:SGD.
DR GO; GO:0043111; P:replication fork arrest; IMP:SGD.
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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1018
FT /note="DNA mismatch repair protein MSH3"
FT /id="PRO_0000115195"
FT REGION 21..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..256
FT /note="Mispair-binding domain"
FT MOTIF 4..11
FT /note="PIP box"
FT COMPBIAS 44..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 791..798
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 4
FT /note="Q->A: Partially functional in a mismatch repair
FT assay; when associated with 10-AA-11."
FT /evidence="ECO:0000269|PubMed:11005803"
FT MUTAGEN 10..11
FT /note="FF->AA: Partially functional in a mismatch repair
FT assay; when associated with A-4."
FT /evidence="ECO:0000269|PubMed:11005803"
FT MUTAGEN 158
FT /note="K->A: Alters DNA-binding activity and impairs MSH2-
FT MSH3-mediated DNA mismatch repair; when associated with
FT ALA-160."
FT /evidence="ECO:0000269|PubMed:17157869"
FT MUTAGEN 160
FT /note="K->A: Alters DNA-binding activity and impairs MSH2-
FT MSH3-mediated DNA mismatch repair; when associated with
FT ALA-158."
FT /evidence="ECO:0000269|PubMed:17157869"
FT MUTAGEN 203
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:17157869"
FT MUTAGEN 226
FT /note="Q->A: No effect."
FT /evidence="ECO:0000269|PubMed:17157869"
FT MUTAGEN 247
FT /note="R->A: Impairs MSH2-MSH3-mediated DNA mismatch
FT repair."
FT /evidence="ECO:0000269|PubMed:17157869"
FT MUTAGEN 796
FT /note="G->D: Defective in MMR and in NHTR."
FT /evidence="ECO:0000269|PubMed:10523644"
SQ SEQUENCE 1018 AA; 116534 MW; 1AD91C2E2F2856EF CRC64;
MAGQPTISRF FKKAVKSELT HKQEQEVAVG NGAGSESICL DTDEEDNLSS VASTTVTNDS
FPLKGSVSSK NSKNSEKTSG TSTTFNDIDF AKKLDRIMKR RSDENVEAED DEEEGEEDFV
KKKARKSPTA KLTPLDKQVK DLKMHHRDKV LVIRVGYKYK CFAEDAVTVS RILHIKLVPG
KLTIDESNPQ DCNHRQFAYC SFPDVRLNVH LERLVHHNLK VAVVEQAETS AIKKHDPGAS
KSSVFERKIS NVFTKATFGV NSTFVLRGKR ILGDTNSIWA LSRDVHQGKV AKYSLISVNL
NNGEVVYDEF EEPNLADEKL QIRIKYLQPI EVLVNTDDLP LHVAKFFKDI SCPLIHKQEY
DLEDHVVQAI KVMNEKIQLS PSLIRLVSKL YSHMVEYNNE QVMLIPSIYS PFASKIHMLL
DPNSLQSLDI FTHDGGKGSL FWLLDHTRTS FGLRMLREWI LKPLVDVHQI EERLDAIECI
TSEINNSIFF ESLNQMLNHT PDLLRTLNRI MYGTTSRKEV YFYLKQITSF VDHFKMHQSY
LSEHFKSSDG RIGKQSPLLF RLFSELNELL STTQLPHFLT MINVSAVMEK NSDKQVMDFF
NLNNYDCSEG IIKIQRESES VRSQLKEELA EIRKYLKRPY LNFRDEVDYL IEVKNSQIKD
LPDDWIKVNN TKMVSRFTTP RTQKLTQKLE YYKDLLIRES ELQYKEFLNK ITAEYTELRK
ITLNLAQYDC ILSLAATSCN VNYVRPTFVN GQQAIIAKNA RNPIIESLDV HYVPNDIMMS
PENGKINIIT GPNMGGKSSY IRQVALLTIM AQIGSFVPAE EIRLSIFENV LTRIGAHDDI
INGDSTFKVE MLDILHILKN CNKRSLLLLD EVGRGTGTHD GIAISYALIK YFSELSDCPL
ILFTTHFPML GEIKSPLIRN YHMDYVEEQK TGEDWMSVIF LYKLKKGLTY NSYGMNVAKL
ARLDKDIINR AFSISEELRK ESINEDALKL FSSLKRILKS DNITATDKLA KLLSLDIH
