MSH3_HUMAN
ID MSH3_HUMAN Reviewed; 1137 AA.
AC P20585; A1L480; A1L482; A6NMM6; Q6PJT5; Q86UQ6; Q92867;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=DNA mismatch repair protein Msh3;
DE Short=hMSH3;
DE AltName: Full=Divergent upstream protein;
DE Short=DUP;
DE AltName: Full=Mismatch repair protein 1;
DE Short=MRP1;
GN Name=MSH3; Synonyms=DUC1, DUG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-79; ARG-949 AND THR-1045.
RX PubMed=2722860; DOI=10.1016/s0021-9258(18)81766-5;
RA Fujii H., Shimada T.;
RT "Isolation and characterization of cDNA clones derived from the divergently
RT transcribed gene in the region upstream from the human dihydrofolate
RT reductase gene.";
RL J. Biol. Chem. 264:10057-10064(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MSH2, AND VARIANTS
RP 57-ALA--ALA-65 DEL; VAL-79 AND ARG-949.
RX PubMed=8942985; DOI=10.1073/pnas.93.24.13629;
RA Acharya S., Wilson T., Gradia S., Kane M.F., Guerrette S., Marsischky G.T.,
RA Kolodner R.D., Fishel R.;
RT "hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:13629-13634(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-79; ARG-949 AND
RP THR-1045.
RA Shimada T., Ikejima M., Watanabe A., Orimo H.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-ALA-ALA-62 INS; VAL-79;
RP LEU-709; ARG-949 AND THR-1045.
RG NIEHS SNPs program;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS 57-ALA--ALA-65 DEL;
RP VAL-79; ARG-949 AND THR-1045.
RC TISSUE=Muscle;
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 [7]
RP POSSIBLE INVOLVEMENT IN ENDMC.
RX PubMed=8782829; DOI=10.1038/ng0996-102;
RA Risinger J.I., Umar A., Boyd J., Berchuck A., Kunkel T.A., Barrett J.C.;
RT "Mutation of MSH3 in endometrial cancer and evidence for its functional
RT role in heteroduplex repair.";
RL Nat. Genet. 14:102-105(1996).
RN [8]
RP INTERACTION WITH EXO1.
RX PubMed=11427529; DOI=10.1074/jbc.m102670200;
RA Schmutte C., Sadoff M.M., Shim K.-S., Acharya S., Fishel R.;
RT "The interaction of DNA mismatch repair proteins with human exonuclease
RT I.";
RL J. Biol. Chem. 276:33011-33018(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1099, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1099, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION IN THE MMR COMPLEX, AND INTERACTION WITH MCM9.
RX PubMed=26300262; DOI=10.1016/j.molcel.2015.07.010;
RA Traver S., Coulombe P., Peiffer I., Hutchins J.R., Kitzmann M.,
RA Latreille D., Mechali M.;
RT "MCM9 Is Required for Mammalian DNA Mismatch Repair.";
RL Mol. Cell 59:831-839(2015).
RN [14]
RP VARIANT ALA-ALA-ALA-62 INS.
RX PubMed=8851770; DOI=10.1007/bf01900603;
RA Nakajima E., Orimo H., Ikejima M., Shimada T.;
RT "Nine-bp repeat polymorphism in exon 1 of the hMSH3 gene.";
RL Jpn. J. Hum. Genet. 40:343-345(1995).
RN [15]
RP VARIANTS VAL-79 AND THR-1045.
RX PubMed=10944853; DOI=10.1007/s100380070031;
RA Orimo H., Nakajima E., Yamamoto M., Ikejima M., Emi M., Shimada T.;
RT "Association between single nucleotide polymorphisms in the hMSH3 gene and
RT sporadic colon cancer with microsatellite instability.";
RL J. Hum. Genet. 45:228-230(2000).
RN [16]
RP INVOLVEMENT IN FAP4.
RX PubMed=27476653; DOI=10.1016/j.ajhg.2016.06.015;
RA Adam R., Spier I., Zhao B., Kloth M., Marquez J., Hinrichsen I., Kirfel J.,
RA Tafazzoli A., Horpaopan S., Uhlhaas S., Stienen D., Friedrichs N.,
RA Altmueller J., Laner A., Holzapfel S., Peters S., Kayser K., Thiele H.,
RA Holinski-Feder E., Marra G., Kristiansen G., Noethen M.M., Buettner R.,
RA Moeslein G., Betz R.C., Brieger A., Lifton R.P., Aretz S.;
RT "Exome Sequencing Identifies Biallelic MSH3 Germline Mutations as a
RT Recessive Subtype of Colorectal Adenomatous Polyposis.";
RL Am. J. Hum. Genet. 99:337-351(2016).
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.
CC -!- SUBUNIT: Component of the DNA mismatch repair (MMR) complex composed at
CC least of MSH2, MSH3, MSH6, PMS1 and MLH1 (PubMed:26300262). Heterodimer
CC consisting of MSH2-MSH3 (MutS beta) (PubMed:8942985). Forms a ternary
CC complex with MutL alpha (MLH1-PMS1). Interacts with EXO1
CC (PubMed:11427529). Interacts with MCM9 (PubMed:26300262).
CC {ECO:0000269|PubMed:11427529, ECO:0000269|PubMed:26300262,
CC ECO:0000269|PubMed:8942985}.
CC -!- INTERACTION:
CC P20585; P40692: MLH1; NbExp=5; IntAct=EBI-1164205, EBI-744248;
CC P20585; P43246: MSH2; NbExp=10; IntAct=EBI-1164205, EBI-355888;
CC P20585; P12004: PCNA; NbExp=6; IntAct=EBI-1164205, EBI-358311;
CC -!- DISEASE: Endometrial cancer (ENDMC) [MIM:608089]: A malignancy of
CC endometrium, the mucous lining of the uterus. Most endometrial cancers
CC are adenocarcinomas, cancers that begin in cells that make and release
CC mucus and other fluids. {ECO:0000305|PubMed:8782829}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Familial adenomatous polyposis 4 (FAP4) [MIM:617100]: A form
CC of familial adenomatous polyposis, a condition characterized by the
CC development of multiple colorectal adenomatous polyps, benign neoplasms
CC derived from glandular epithelium. Some affected individuals may
CC develop colorectal carcinoma. FAP4 inheritance is autosomal recessive.
CC {ECO:0000269|PubMed:27476653}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutS family. MSH3
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11817.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MSH3ID341ch5q11.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/msh3/";
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DR EMBL; J04810; AAB47281.1; -; mRNA.
DR EMBL; U61981; AAB06045.1; -; mRNA.
DR EMBL; D61419; BAD27111.1; -; Genomic_DNA.
DR EMBL; AY275681; AAP13535.1; -; Genomic_DNA.
DR EMBL; AC008434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011817; AAH11817.1; ALT_SEQ; mRNA.
DR EMBL; BC130434; AAI30435.1; -; mRNA.
DR EMBL; BC130436; AAI30437.1; -; mRNA.
DR CCDS; CCDS34195.1; -.
DR PIR; A33507; A33507.
DR RefSeq; NP_002430.3; NM_002439.4.
DR PDB; 3THW; X-ray; 3.09 A; B=219-1134.
DR PDB; 3THX; X-ray; 2.70 A; B=219-1134.
DR PDB; 3THY; X-ray; 2.89 A; B=219-1134.
DR PDB; 3THZ; X-ray; 4.30 A; B=219-1134.
DR PDBsum; 3THW; -.
DR PDBsum; 3THX; -.
DR PDBsum; 3THY; -.
DR PDBsum; 3THZ; -.
DR AlphaFoldDB; P20585; -.
DR SMR; P20585; -.
DR BioGRID; 110574; 91.
DR ComplexPortal; CPX-77; DNA mismatch repair MutSbeta complex.
DR CORUM; P20585; -.
DR DIP; DIP-35127N; -.
DR IntAct; P20585; 23.
DR MINT; P20585; -.
DR STRING; 9606.ENSP00000265081; -.
DR iPTMnet; P20585; -.
DR PhosphoSitePlus; P20585; -.
DR BioMuta; MSH3; -.
DR DMDM; 317373576; -.
DR EPD; P20585; -.
DR jPOST; P20585; -.
DR MassIVE; P20585; -.
DR MaxQB; P20585; -.
DR PaxDb; P20585; -.
DR PeptideAtlas; P20585; -.
DR PRIDE; P20585; -.
DR ProteomicsDB; 53762; -.
DR Antibodypedia; 24651; 293 antibodies from 32 providers.
DR CPTC; P20585; 1 antibody.
DR DNASU; 4437; -.
DR Ensembl; ENST00000265081.7; ENSP00000265081.6; ENSG00000113318.11.
DR GeneID; 4437; -.
DR KEGG; hsa:4437; -.
DR MANE-Select; ENST00000265081.7; ENSP00000265081.6; NM_002439.5; NP_002430.3.
DR UCSC; uc003kgz.5; human.
DR CTD; 4437; -.
DR DisGeNET; 4437; -.
DR GeneCards; MSH3; -.
DR HGNC; HGNC:7326; MSH3.
DR HPA; ENSG00000113318; Low tissue specificity.
DR MalaCards; MSH3; -.
DR MIM; 600887; gene.
DR MIM; 608089; phenotype.
DR MIM; 617100; phenotype.
DR neXtProt; NX_P20585; -.
DR OpenTargets; ENSG00000113318; -.
DR Orphanet; 480536; MSH3-related attenuated familial adenomatous polyposis.
DR PharmGKB; PA31134; -.
DR VEuPathDB; HostDB:ENSG00000113318; -.
DR eggNOG; KOG0218; Eukaryota.
DR GeneTree; ENSGT00550000074949; -.
DR HOGENOM; CLU_002472_0_1_1; -.
DR InParanoid; P20585; -.
DR OMA; LRNVHMK; -.
DR OrthoDB; 138168at2759; -.
DR PhylomeDB; P20585; -.
DR TreeFam; TF300525; -.
DR PathwayCommons; P20585; -.
DR Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
DR Reactome; R-HSA-5632927; Defective Mismatch Repair Associated With MSH3.
DR Reactome; R-HSA-5632928; Defective Mismatch Repair Associated With MSH2.
DR SignaLink; P20585; -.
DR BioGRID-ORCS; 4437; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; MSH3; human.
DR GeneWiki; MSH3; -.
DR GenomeRNAi; 4437; -.
DR Pharos; P20585; Tbio.
DR PRO; PR:P20585; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P20585; protein.
DR Bgee; ENSG00000113318; Expressed in bronchial epithelial cell and 212 other tissues.
DR ExpressionAtlas; P20585; baseline and differential.
DR Genevisible; P20585; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032302; C:MutSbeta complex; IDA:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IDA:BHF-UCL.
DR GO; GO:0043570; P:maintenance of DNA repeat elements; IMP:HGNC-UCL.
DR GO; GO:0006298; P:mismatch repair; IDA:ComplexPortal.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IDA:BHF-UCL.
DR GO; GO:0051096; P:positive regulation of helicase activity; IDA:BHF-UCL.
DR GO; GO:0016447; P:somatic recombination of immunoglobulin gene segments; IBA:GO_Central.
DR Gene3D; 3.30.420.110; -; 1.
DR Gene3D; 3.40.1170.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00612; -.
DR InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1137
FT /note="DNA mismatch repair protein Msh3"
FT /id="PRO_0000115192"
FT REGION 31..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..297
FT /note="Interaction with EXO1"
FT /evidence="ECO:0000269|PubMed:11427529"
FT REGION 201..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 896..903
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1099
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VARIANT 57..65
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8942985"
FT /id="VAR_020934"
FT VARIANT 62
FT /note="A -> AAAA"
FT /evidence="ECO:0000269|PubMed:8851770"
FT /id="VAR_020935"
FT VARIANT 79
FT /note="I -> V (in dbSNP:rs1650697)"
FT /evidence="ECO:0000269|PubMed:10944853,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2722860,
FT ECO:0000269|PubMed:8942985, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_020936"
FT VARIANT 709
FT /note="F -> L (in dbSNP:rs1805354)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_016160"
FT VARIANT 789
FT /note="Y -> F (in dbSNP:rs10067975)"
FT /id="VAR_055251"
FT VARIANT 949
FT /note="Q -> R (in dbSNP:rs184967)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2722860, ECO:0000269|PubMed:8942985,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT /id="VAR_016161"
FT VARIANT 1045
FT /note="A -> T (in dbSNP:rs26279)"
FT /evidence="ECO:0000269|PubMed:10944853,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2722860,
FT ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT /id="VAR_016162"
FT VARIANT 1054
FT /note="T -> A (in dbSNP:rs1805131)"
FT /id="VAR_016163"
FT CONFLICT 61
FT /note="A -> T (in Ref. 6; AAI30435)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="E -> G (in Ref. 1; AAB47281 and 3; BAD27111)"
FT /evidence="ECO:0000305"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 241..245
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:3THW"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 412..421
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 465..475
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 497..512
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 516..519
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 551..553
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 560..564
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 570..581
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 587..601
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 607..613
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 614..617
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 621..629
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 635..661
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 666..672
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 674..678
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 683..686
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 691..696
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 706..708
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 710..737
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 750..757
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 761..763
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 775..781
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 783..814
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 818..841
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 850..854
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 856..862
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 865..870
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 880..884
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 886..888
FT /evidence="ECO:0007829|PDB:3THY"
FT STRAND 891..896
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 900..917
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 922..930
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 933..938
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 952..965
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 971..976
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 977..980
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 983..999
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 1004..1008
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 1012..1016
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 1017..1020
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 1021..1024
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 1025..1033
FT /evidence="ECO:0007829|PDB:3THX"
FT STRAND 1055..1062
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 1066..1069
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 1070..1073
FT /evidence="ECO:0007829|PDB:3THX"
FT TURN 1074..1077
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 1080..1111
FT /evidence="ECO:0007829|PDB:3THX"
FT HELIX 1116..1128
FT /evidence="ECO:0007829|PDB:3THX"
SQ SEQUENCE 1137 AA; 127412 MW; FBAE6B84D3F86032 CRC64;
MSRRKPASGG LAASSSAPAR QAVLSRFFQS TGSLKSTSSS TGAADQVDPG AAAAAAAAAA
AAPPAPPAPA FPPQLPPHIA TEIDRRKKRP LENDGPVKKK VKKVQQKEGG SDLGMSGNSE
PKKCLRTRNV SKSLEKLKEF CCDSALPQSR VQTESLQERF AVLPKCTDFD DISLLHAKNA
VSSEDSKRQI NQKDTTLFDL SQFGSSNTSH ENLQKTASKS ANKRSKSIYT PLELQYIEMK
QQHKDAVLCV ECGYKYRFFG EDAEIAAREL NIYCHLDHNF MTASIPTHRL FVHVRRLVAK
GYKVGVVKQT ETAALKAIGD NRSSLFSRKL TALYTKSTLI GEDVNPLIKL DDAVNVDEIM
TDTSTSYLLC ISENKENVRD KKKGNIFIGI VGVQPATGEV VFDSFQDSAS RSELETRMSS
LQPVELLLPS ALSEQTEALI HRATSVSVQD DRIRVERMDN IYFEYSHAFQ AVTEFYAKDT
VDIKGSQIIS GIVNLEKPVI CSLAAIIKYL KEFNLEKMLS KPENFKQLSS KMEFMTINGT
TLRNLEILQN QTDMKTKGSL LWVLDHTKTS FGRRKLKKWV TQPLLKLREI NARLDAVSEV
LHSESSVFGQ IENHLRKLPD IERGLCSIYH KKCSTQEFFL IVKTLYHLKS EFQAIIPAVN
SHIQSDLLRT VILEIPELLS PVEHYLKILN EQAAKVGDKT ELFKDLSDFP LIKKRKDEIQ
GVIDEIRMHL QEIRKILKNP SAQYVTVSGQ EFMIEIKNSA VSCIPTDWVK VGSTKAVSRF
HSPFIVENYR HLNQLREQLV LDCSAEWLDF LEKFSEHYHS LCKAVHHLAT VDCIFSLAKV
AKQGDYCRPT VQEERKIVIK NGRHPVIDVL LGEQDQYVPN NTDLSEDSER VMIITGPNMG
GKSSYIKQVA LITIMAQIGS YVPAEEATIG IVDGIFTRMG AADNIYKGQS TFMEELTDTA
EIIRKATSQS LVILDELGRG TSTHDGIAIA YATLEYFIRD VKSLTLFVTH YPPVCELEKN
YSHQVGNYHM GFLVSEDESK LDPGAAEQVP DFVTFLYQIT RGIAARSYGL NVAKLADVPG
EILKKAAHKS KELEGLINTK RKRLKYFAKL WTMHNAQDLQ KWTEEFNMEE TQTSLLH
