MXI1_HUMAN
ID MXI1_HUMAN Reviewed; 228 AA.
AC P50539; B1ANN7; D3DR25; D3DRA9; Q15887; Q6FHW2; Q96E53;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Max-interacting protein 1;
DE Short=Max interactor 1;
DE AltName: Full=Class C basic helix-loop-helix protein 11;
DE Short=bHLHc11;
GN Name=MXI1; Synonyms=BHLHC11;
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] (ISOFORM 1).
RX PubMed=8425219; DOI=10.1016/0092-8674(93)90662-a;
RA Zervos A.S., Gyuris J., Brent R.;
RT "Mxi1, a protein that specifically interacts with Max to bind Myc-Max
RT recognition sites.";
RL Cell 72:223-232(1993).
RN [2]
RP ERRATUM OF PUBMED:8425219.
RA Zervos A.S., Gyuris J., Brent R.;
RL Cell 79:388-388(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8838813; DOI=10.1006/geno.1996.0144;
RA Wechsler D.S., Shelly C.A., Dang C.V.;
RT "Genomic organization of human MXI1, a putative tumor suppressor gene.";
RL Genomics 32:466-470(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8918230; DOI=10.1016/0378-1119(96)00206-5;
RA Shimizu E., Shirasawa H., Kodama K., Sato T., Shimizu B.;
RT "Expression, regulation and polymorphism of the mxi1 genes.";
RL Gene 176:45-48(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Hippocampus, and Lung;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 216-228.
RX PubMed=7789959; DOI=10.1007/bf00209493;
RA Albarosa R., Didonato S., Finocchiaro G.;
RT "Redefinition of the coding sequence of the MXI1 gene and identification of
RT a polymorphic repeat in the 3' non-coding region that allows the detection
RT of loss of heterozygosity of chromosome 10q25 in glioblastomas.";
RL Hum. Genet. 95:709-711(1995).
RN [11]
RP VARIANT PROSTATE CANCER ALA-152.
RX PubMed=7773287; DOI=10.1038/ng0395-249;
RA Eagle L.R., Yin X., Brothman A.R., Williams B.J., Atkin N.B.,
RA Prochownik E.V.;
RT "Mutation of the MXI1 gene in prostate cancer.";
RL Nat. Genet. 9:249-255(1995).
CC -!- FUNCTION: Transcriptional repressor. MXI1 binds with MAX to form a
CC sequence-specific DNA-binding protein complex which recognizes the core
CC sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional
CC activity by competing for MAX.
CC -!- SUBUNIT: Interacts with SMC3 (By similarity). Efficient DNA binding
CC requires dimerization with another bHLH protein. Binds DNA as a
CC heterodimer with MAX. Interacts with RNF17 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P50539; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-752241, EBI-739580;
CC P50539; Q53RC5: DKFZp547I014; NbExp=3; IntAct=EBI-752241, EBI-10212065;
CC P50539; O75356: ENTPD5; NbExp=3; IntAct=EBI-752241, EBI-7416931;
CC P50539; P61244: MAX; NbExp=6; IntAct=EBI-752241, EBI-751711;
CC P50539; P61244-2: MAX; NbExp=3; IntAct=EBI-752241, EBI-10218525;
CC P50539-3; Q13137: CALCOCO2; NbExp=6; IntAct=EBI-10211940, EBI-739580;
CC P50539-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10211940, EBI-3867333;
CC P50539-3; O95967: EFEMP2; NbExp=3; IntAct=EBI-10211940, EBI-743414;
CC P50539-3; Q15323: KRT31; NbExp=3; IntAct=EBI-10211940, EBI-948001;
CC P50539-3; Q6A162: KRT40; NbExp=3; IntAct=EBI-10211940, EBI-10171697;
CC P50539-3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10211940, EBI-11959885;
CC P50539-3; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-10211940, EBI-11749135;
CC P50539-3; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-10211940, EBI-10172150;
CC P50539-3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10211940, EBI-10172290;
CC P50539-3; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-10211940, EBI-10171774;
CC P50539-3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10211940, EBI-10172052;
CC P50539-3; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-10211940, EBI-11987425;
CC P50539-3; Q99750: MDFI; NbExp=3; IntAct=EBI-10211940, EBI-724076;
CC P50539-3; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10211940, EBI-945833;
CC P50539-3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10211940, EBI-22310682;
CC P50539-3; Q5VY43: PEAR1; NbExp=3; IntAct=EBI-10211940, EBI-1249608;
CC P50539-3; Q8N720: ZNF655; NbExp=3; IntAct=EBI-10211940, EBI-625509;
CC P50539-4; Q6A162: KRT40; NbExp=3; IntAct=EBI-16436111, EBI-10171697;
CC P50539-4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-16436111, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P50539-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50539-2; Sequence=VSP_012825;
CC Name=3;
CC IsoId=P50539-3; Sequence=VSP_037943;
CC Name=4;
CC IsoId=P50539-4; Sequence=VSP_012825, VSP_043170;
CC -!- TISSUE SPECIFICITY: High levels found in the brain, heart and lung
CC while lower levels are seen in the liver, kidney and skeletal muscle.
CC -!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in
CC tissues of the prostate. Most prostate cancers are adenocarcinomas that
CC develop in the acini of the prostatic ducts. Other rare histopathologic
CC types of prostate cancer that occur in approximately 5% of patients
CC include small cell carcinoma, mucinous carcinoma, prostatic ductal
CC carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal
CC cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell
CC carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:7773287}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MXI1ID209.html";
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DR EMBL; L07648; AAA75508.1; -; mRNA.
DR EMBL; U32515; AAC50446.1; -; Genomic_DNA.
DR EMBL; U32512; AAC50446.1; JOINED; Genomic_DNA.
DR EMBL; U32513; AAC50446.1; JOINED; Genomic_DNA.
DR EMBL; U32514; AAC50446.1; JOINED; Genomic_DNA.
DR EMBL; D63940; BAA09972.1; -; mRNA.
DR EMBL; BT007069; AAP35732.1; -; mRNA.
DR EMBL; CR536576; CAG38813.1; -; mRNA.
DR EMBL; AL360182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49565.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49567.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49568.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49569.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49570.1; -; Genomic_DNA.
DR EMBL; BC012907; AAH12907.1; -; mRNA.
DR EMBL; BC035128; AAH35128.2; -; mRNA.
DR EMBL; S78470; AAD14282.1; -; Genomic_DNA.
DR CCDS; CCDS31284.1; -. [P50539-4]
DR CCDS; CCDS7563.1; -. [P50539-3]
DR CCDS; CCDS7564.2; -. [P50539-1]
DR PIR; A45182; A45182.
DR RefSeq; NP_001008541.1; NM_001008541.1. [P50539-4]
DR RefSeq; NP_005953.4; NM_005962.4. [P50539-1]
DR RefSeq; NP_569157.2; NM_130439.3. [P50539-3]
DR AlphaFoldDB; P50539; -.
DR SMR; P50539; -.
DR BioGRID; 110686; 47.
DR CORUM; P50539; -.
DR DIP; DIP-205N; -.
DR ELM; P50539; -.
DR IntAct; P50539; 26.
DR MINT; P50539; -.
DR STRING; 9606.ENSP00000331152; -.
DR iPTMnet; P50539; -.
DR PhosphoSitePlus; P50539; -.
DR BioMuta; MXI1; -.
DR DMDM; 116242666; -.
DR EPD; P50539; -.
DR jPOST; P50539; -.
DR MassIVE; P50539; -.
DR MaxQB; P50539; -.
DR PaxDb; P50539; -.
DR PeptideAtlas; P50539; -.
DR PRIDE; P50539; -.
DR ProteomicsDB; 56235; -. [P50539-1]
DR ProteomicsDB; 56236; -. [P50539-2]
DR ProteomicsDB; 56237; -. [P50539-3]
DR ProteomicsDB; 56238; -. [P50539-4]
DR Antibodypedia; 18346; 253 antibodies from 30 providers.
DR DNASU; 4601; -.
DR Ensembl; ENST00000239007.11; ENSP00000239007.7; ENSG00000119950.21. [P50539-1]
DR Ensembl; ENST00000332674.9; ENSP00000331152.5; ENSG00000119950.21. [P50539-3]
DR Ensembl; ENST00000361248.8; ENSP00000354606.4; ENSG00000119950.21. [P50539-4]
DR Ensembl; ENST00000369612.1; ENSP00000358625.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000650644.1; ENSP00000498900.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000650696.1; ENSP00000499158.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000650810.1; ENSP00000498390.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000650843.1; ENSP00000498547.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000650900.1; ENSP00000499209.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000650952.1; ENSP00000499161.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651004.1; ENSP00000498396.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651167.1; ENSP00000498764.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651467.1; ENSP00000499128.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651495.1; ENSP00000498536.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651516.1; ENSP00000498873.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651613.1; ENSP00000498554.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651811.1; ENSP00000498472.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651848.1; ENSP00000498238.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000651866.1; ENSP00000498306.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000652028.1; ENSP00000498928.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000652463.1; ENSP00000499087.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000652506.1; ENSP00000498573.1; ENSG00000119950.21. [P50539-2]
DR Ensembl; ENST00000652604.1; ENSP00000498971.1; ENSG00000119950.21. [P50539-4]
DR GeneID; 4601; -.
DR KEGG; hsa:4601; -.
DR MANE-Select; ENST00000332674.9; ENSP00000331152.5; NM_130439.3; NP_569157.2. [P50539-3]
DR UCSC; uc001kyy.3; human. [P50539-1]
DR CTD; 4601; -.
DR DisGeNET; 4601; -.
DR GeneCards; MXI1; -.
DR HGNC; HGNC:7534; MXI1.
DR HPA; ENSG00000119950; Low tissue specificity.
DR MalaCards; MXI1; -.
DR MIM; 176807; phenotype.
DR MIM; 600020; gene.
DR neXtProt; NX_P50539; -.
DR OpenTargets; ENSG00000119950; -.
DR PharmGKB; PA31335; -.
DR VEuPathDB; HostDB:ENSG00000119950; -.
DR eggNOG; KOG2483; Eukaryota.
DR GeneTree; ENSGT00940000155809; -.
DR HOGENOM; CLU_082604_0_0_1; -.
DR InParanoid; P50539; -.
DR OMA; VEMINIQ; -.
DR OrthoDB; 1311585at2759; -.
DR PhylomeDB; P50539; -.
DR TreeFam; TF315654; -.
DR PathwayCommons; P50539; -.
DR SignaLink; P50539; -.
DR SIGNOR; P50539; -.
DR BioGRID-ORCS; 4601; 9 hits in 1098 CRISPR screens.
DR ChiTaRS; MXI1; human.
DR GeneWiki; MXI1; -.
DR GenomeRNAi; 4601; -.
DR Pharos; P50539; Tbio.
DR PRO; PR:P50539; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P50539; protein.
DR Bgee; ENSG00000119950; Expressed in cranial nerve II and 216 other tissues.
DR ExpressionAtlas; P50539; baseline and differential.
DR Genevisible; P50539; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; DNA-binding; Nucleus;
KW Proto-oncogene; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..228
FT /note="Max-interacting protein 1"
FT /id="PRO_0000127285"
FT DOMAIN 67..119
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 29..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8918230, ECO:0000303|Ref.5"
FT /id="VSP_012825"
FT VAR_SEQ 1..25
FT /note="MERVKMINVQRLLEAAEFLERRERE -> MGKRGRPRKEARCEGAGLAPAAP
FT PAVPPAVAAPQPPALPEDPAGAKPRCPFSDIFNTSENSMEKHINTFLQNVQILLEAASY
FT LEQIEKENKK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037943"
FT VAR_SEQ 68..77
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_043170"
FT VARIANT 152
FT /note="E -> A (in prostate cancer; dbSNP:rs137852603)"
FT /evidence="ECO:0000269|PubMed:7773287"
FT /id="VAR_004499"
FT CONFLICT 61
FT /note="S -> T (in Ref. 1; AAA75508)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 26062 MW; 82F83F499B907DD3 CRC64;
MERVKMINVQ RLLEAAEFLE RRERECEHGY ASSFPSMPSP RLQHSKPPRR LSRAQKHSSG
SSNTSTANRS THNELEKNRR AHLRLCLERL KVLIPLGPDC TRHTTLGLLN KAKAHIKKLE
EAERKSQHQL ENLEREQRFL KWRLEQLQGP QEMERIRMDS IGSTISSDRS DSEREEIEVD
VESTEFSHGE VDNISTTSIS DIDDHSSLPS IGSDEGYSSA SVKLSFTS
