ID   MSH6_MOUSE              Reviewed;        1358 AA.
AC   P54276; O54710; Q6GTK8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=DNA mismatch repair protein Msh6 {ECO:0000303|PubMed:9390556};
DE   AltName: Full=G/T mismatch-binding protein {ECO:0000303|PubMed:8812455};
DE            Short=GTBP {ECO:0000250|UniProtKB:P52701};
DE            Short=GTMBP {ECO:0000303|PubMed:8812455};
DE   AltName: Full=MutS protein homolog 6 {ECO:0000250|UniProtKB:P52701};
DE   AltName: Full=MutS-alpha 160 kDa subunit;
DE            Short=p160 {ECO:0000250|UniProtKB:P52701};
GN   Name=Msh6 {ECO:0000312|MGI:MGI:1343961}; Synonyms=Gtmbp;
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].
RX   PubMed=8812455; DOI=10.1006/geno.1996.0464;
RA   Corradi A., Croci L., Stayton C.L., Gulisano M., Boncinelli E.,
RA   Consalez G.G.;
RT   "cDNA sequence, map, and expression of the murine homolog of GTBP, a DNA
RT   mismatch repair gene.";
RL   Genomics 36:288-295(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RX   PubMed=9390556; DOI=10.1016/s0092-8674(00)80433-x;
RA   Edelmann W., Yang K., Umar A., Heyer J., Lau K., Fan K., Liedtke W.,
RA   Cohen P., Kane M.K., Lipford J.R., Yu N., Crouse G.F., Pollard J.W.,
RA   Kunkel T., Lipkin M., Kolodner R., Kucherlapati R.;
RT   "Mutation in the mismatch repair gene Msh6 causes cancer susceptibility.";
RL   Cell 91:467-477(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 375-425 AND 1001-1050.
RA   Donohue P.J., Feng S.L.Y., Alberts G.F., Guo Y., Peifley K.A., Hsu D.K.W.,
RA   Winkles J.A.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-252; SER-254;
RP   SER-256 AND SER-261, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Component of the post-replicative DNA mismatch repair system
CC       (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA
CC       mismatches thereby initiating DNA repair. When bound, MutS alpha bends
CC       the DNA helix and shields approximately 20 base pairs, and recognizes
CC       single base mismatches and dinucleotide insertion-deletion loops (IDL)
CC       in the DNA. After mismatch binding, forms a ternary complex with the
CC       MutL alpha heterodimer, which is thought to be responsible for
CC       directing the downstream MMR events, including strand discrimination,
CC       excision, and resynthesis. ATP binding and hydrolysis play a pivotal
CC       role in mismatch repair functions. The ATPase activity associated with
CC       MutS alpha regulates binding similar to a molecular switch: mismatched
CC       DNA provokes ADP-->ATP exchange, resulting in a discernible
CC       conformational transition that converts MutS alpha into a sliding clamp
CC       capable of hydrolysis-independent diffusion along the DNA backbone.
CC       This transition is crucial for mismatch repair. MutS alpha may also
CC       play a role in DNA homologous recombination repair. Recruited on
CC       chromatin in G1 and early S phase via its PWWP domain that specifically
CC       binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early
CC       recruitment to chromatin to be replicated allowing a quick
CC       identification of mismatch repair to initiate the DNA mismatch repair
CC       reaction (By similarity). {ECO:0000250|UniProtKB:P52701}.
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-MSH6 (MutS alpha). Forms a ternary complex with MutL alpha (MLH1-
CC       PMS1). Interacts with MCM9. Part of the BRCA1-associated genome
CC       surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1,
CC       ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This
CC       association could be a dynamic process changing throughout the cell
CC       cycle and within subnuclear domains. {ECO:0000250|UniProtKB:P52701}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P52701}.
CC       Chromosome {ECO:0000250|UniProtKB:P52701}. Note=Associates with
CC       H3K36me3 via its PWWP domain. {ECO:0000250|UniProtKB:P52701}.
CC   -!- DOMAIN: The PWWP domain specifically recognizes and binds trimethylated
CC       'Lys-36' of histone H3 (H3K36me3). {ECO:0000250|UniProtKB:P52701}.
CC   -!- PTM: Phosphorylated by PRKCZ, which may prevent MutS alpha degradation
CC       by the ubiquitin-proteasome pathway. {ECO:0000250|UniProtKB:P52701}.
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family.
CC       {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; U42190; AAC53034.1; -; mRNA.
DR   EMBL; AF031087; AAB88445.1; -; Genomic_DNA.
DR   EMBL; AF031085; AAB88445.1; JOINED; Genomic_DNA.
DR   EMBL; AF031086; AAB88445.1; JOINED; Genomic_DNA.
DR   EMBL; BC051160; AAH51160.1; -; mRNA.
DR   EMBL; BC051634; AAH51634.1; -; mRNA.
DR   EMBL; U61388; AAB39930.1; -; mRNA.
DR   EMBL; U61389; AAB39931.1; -; mRNA.
DR   CCDS; CCDS29021.1; -.
DR   RefSeq; NP_034960.1; NM_010830.2.
DR   AlphaFoldDB; P54276; -.
DR   SMR; P54276; -.
DR   BioGRID; 201528; 20.
DR   ComplexPortal; CPX-81; DNA mismatch repair MutSalpha complex.
DR   CORUM; P54276; -.
DR   IntAct; P54276; 5.
DR   MINT; P54276; -.
DR   STRING; 10090.ENSMUSP00000005503; -.
DR   GlyGen; P54276; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P54276; -.
DR   PhosphoSitePlus; P54276; -.
DR   SwissPalm; P54276; -.
DR   EPD; P54276; -.
DR   jPOST; P54276; -.
DR   MaxQB; P54276; -.
DR   PaxDb; 10090-ENSMUSP00000005503; -.
DR   PeptideAtlas; P54276; -.
DR   ProteomicsDB; 290100; -.
DR   Pumba; P54276; -.
DR   Antibodypedia; 3963; 953 antibodies from 45 providers.
DR   DNASU; 17688; -.
DR   Ensembl; ENSMUST00000005503.5; ENSMUSP00000005503.4; ENSMUSG00000005370.5.
DR   GeneID; 17688; -.
DR   KEGG; mmu:17688; -.
DR   UCSC; uc008dvd.2; mouse.
DR   AGR; MGI:1343961; -.
DR   CTD; 2956; -.
DR   MGI; MGI:1343961; Msh6.
DR   VEuPathDB; HostDB:ENSMUSG00000005370; -.
DR   eggNOG; KOG0217; Eukaryota.
DR   GeneTree; ENSGT00550000075024; -.
DR   HOGENOM; CLU_002472_1_3_1; -.
DR   InParanoid; P54276; -.
DR   OMA; TPMMAQY; -.
DR   OrthoDB; 168255at2759; -.
DR   PhylomeDB; P54276; -.
DR   TreeFam; TF105842; -.
DR   Reactome; R-MMU-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
DR   BioGRID-ORCS; 17688; 1 hit in 120 CRISPR screens.
DR   ChiTaRS; Msh6; mouse.
DR   PRO; PR:P54276; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P54276; Protein.
DR   Bgee; ENSMUSG00000005370; Expressed in animal zygote and 252 other cell types or tissues.
DR   ExpressionAtlas; P54276; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0032301; C:MutSalpha complex; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003684; F:damaged DNA binding; IMP:MGI.
DR   GO; GO:0003677; F:DNA binding; IMP:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0000400; F:four-way junction DNA binding; IEA:Ensembl.
DR   GO; GO:0032137; F:guanine/thymine mispair binding; IDA:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0030983; F:mismatched DNA binding; ISS:UniProtKB.
DR   GO; GO:0032405; F:MutLalpha complex binding; IEA:Ensembl.
DR   GO; GO:0032357; F:oxidized purine DNA binding; IEA:Ensembl.
DR   GO; GO:0032142; F:single guanine insertion binding; IEA:Ensembl.
DR   GO; GO:0032143; F:single thymine insertion binding; IEA:Ensembl.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR   GO; GO:0045190; P:isotype switching; IMP:MGI.
DR   GO; GO:0006298; P:mismatch repair; IMP:MGI.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IMP:MGI.
DR   GO; GO:0009411; P:response to UV; IMP:MGI.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:MGI.
DR   GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   CDD; cd05837; PWWP_MSH6; 1.
DR   Gene3D; 1.10.1420.10; -; 2.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 3.40.1170.10; DNA repair protein MutS, domain I; 1.
DR   Gene3D; 3.30.420.110; MutS, connector domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR000313; PWWP_dom.
DR   PANTHER; PTHR11361:SF148; DNA MISMATCH REPAIR PROTEIN MSH6; 1.
DR   PANTHER; PTHR11361; DNA MISMATCH REPAIR PROTEIN MUTS FAMILY MEMBER; 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   Pfam; PF00855; PWWP; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF55271; DNA repair protein MutS, domain I; 1.
DR   SUPFAM; SSF48334; DNA repair protein MutS, domain III; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   Genevisible; P54276; MM.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1358
FT                   /note="DNA mismatch repair protein Msh6"
FT                   /id="PRO_0000115208"
FT   DOMAIN          92..154
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1132..1139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         38
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         40
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         67
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         269
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         275
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         487
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         503
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         827
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         932
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   MOD_RES         1007
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P52701"
FT   CONFLICT        65..66
FT                   /note="EA -> DG (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374..375
FT                   /note="PE -> QK (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        754
FT                   /note="T -> N (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        800
FT                   /note="D -> Y (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1227
FT                   /note="N -> S (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1329
FT                   /note="Q -> R (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1333
FT                   /note="E -> G (in Ref. 1; AAC53034)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1358 AA;  151084 MW;  979D289BC69E6047 CRC64;
     MSRQSTLYSF FPKSPALGDT KKAAAEASRQ GAAASGASAS RGGDAAWSEA EPGSRSAAVS
     ASSPEAKDLN GGLRRASSSA QAVPPSSCDF SPGDLVWAKM EGYPWWPCLV YNHPFDGTFI
     RKKGKSVRVH VQFFDDSPTR GWVSKRMLKP YTGSKSKEAQ KGGHFYSSKS EILRAMQRAD
     EALSKDTAER LQLAVCDEPS EPEEEEETEV HEAYLSDKSE EDNYNESEEE AQPSVQGPRR
     SSRQVKKRRV ISDSESDIGG SDVEFKPDTK QEGSSDDASS GVGDSDSEDL GTFGKGAPKR
     KRAMVAQGGL RRKSLKKETG SAKRATPILS ETKSTLSAFS APQNSESQTH VSGGGNDSSG
     PTVWYHETLE WLKPEKRRDE HRRRPDHPEF NPTTLYVPEE FLNSCTPGMR KWWQLKSQNF
     DLVIFYKVGK FYELYHMDAV IGVSELGLIF MKGNWAHSGF PEIAFGRFSD SLVQKGYKVA
     RVEQTETPEM MEARCRKMAH VSKFDRVVRR EICRIITKGT QTYSVLDGDP SENYSRYLLS
     LKEKEEETSG HTRVYGVCFV DTSLGKFFIG QFSDDRHCSR FRTLVAHYPP VQILFEKGNL
     STETKTVLKG SLSSCLQEGL IPGSQFWDAT KTLRTLLEGG YFTGNGDSST VLPLVLKGMT
     SESDSVGLTP GEESELALSA LGGIVFYLKK CLIDQELLSM ANFEEYFPLD SDTVSTVKPG
     AVFTKASQRM VLDAVTLNNL EIFLNGTNGS TEGTLLERLD TCHTPFGKRL LKQWLCAPLC
     SPSAISDRLD AVEDLMAVPD KVTEVADLLK KLPDLERLLS KIHNVGSPLK SQNHPDSRAI
     MYEETTYSKK KIIDFLSALE GFKVMCKVSG LLEEVAGGFT SKTLKQVVTL QSKSPKGRFP
     DLTAELQRWD TAFDHEKARK TGLITPKAGF DSDYDQALAD IRENEQSLLE YLDKQRSRLG
     CKSIVYWGIG RNRYQLEIPE NFATRNLPEE YELKSTKKGC KRYWTKTIEK KLANLINAEE
     RRDTSLKDCM RRLFCNFDKN HKDWQSAVEC IAVLDVLLCL ANYSQGGDGP MCRPEIVLPG
     EDTHPFLEFK GSRHPCITKT FFGDDFIPND ILIGCEEEAE EHGKAYCVLV TGPNMGGKST
     LIRQAGLLAV MAQLGCYVPA EKCRLTPVDR VFTRLGASDR IMSGESTFFV ELSETASILR
     HATAHSLVLV DELGRGTATF DGTAIANAVV KELAETIKCR TLFSTHYHSL VEDYSKSVCV
     RLGHMACMVE NECEDPSQET ITFLYKFIKG ACPKSYGFNA ARLANLPEEV IQKGHRKARE
     FERMNQSLQL FREVCLATEK PTINGEAIHR LLALINGL
//