MYOD1_HUMAN
ID MYOD1_HUMAN Reviewed; 320 AA.
AC P15172; O75321;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Myoblast determination protein 1;
DE AltName: Full=Class C basic helix-loop-helix protein 1;
DE Short=bHLHc1;
DE AltName: Full=Myogenic factor 3;
DE Short=Myf-3;
GN Name=MYOD1; Synonyms=BHLHC1, MYF3, MYOD;
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].
RX PubMed=1850513; DOI=10.1093/nar/19.5.1148;
RA Pearson-White S.H.;
RT "Human MyoD: cDNA and deduced amino acid sequence.";
RL Nucleic Acids Res. 19:1148-1148(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9546368;
RA Chen B., Dias P., Jenkins J.J. III, Savell V.H., Parham D.M.;
RT "Methylation alterations of the MyoD1 upstream region are predictive of
RT subclassification of human rhabdomyosarcomas.";
RL Am. J. Pathol. 152:1071-1079(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-320.
RC TISSUE=Skeletal muscle;
RX PubMed=2583111; DOI=10.1002/j.1460-2075.1989.tb08535.x;
RA Braun T., Bober E., Buschhausen-Denker G., Kohtz S., Grzeschik K.-H.,
RA Arnold H.H.;
RT "Differential expression of myogenic determination genes in muscle cells:
RT possible autoactivation by the Myf gene products.";
RL EMBO J. 8:3617-3625(1989).
RN [7]
RP UBIQUITINATION AT MET-1.
RX PubMed=9774340; DOI=10.1093/emboj/17.20.5964;
RA Breitschopf K., Bengal E., Ziv T., Admon A., Ciechanover A.;
RT "A novel site for ubiquitination: the N-terminal residue, and not internal
RT lysines of MyoD, is essential for conjugation and degradation of the
RT protein.";
RL EMBO J. 17:5964-5973(1998).
RN [8]
RP REVIEW ON ACETYLATION/DEACETYLATION.
RX PubMed=11532390; DOI=10.1016/s0959-437x(00)00224-0;
RA McKinsey T.A., Zhang C.L., Olson E.N.;
RT "Control of muscle development by dueling HATs and HDACs.";
RL Curr. Opin. Genet. Dev. 11:497-504(2001).
RN [9]
RP INTERACTION WITH CDK9.
RX PubMed=12037670; DOI=10.1038/sj.onc.1205493;
RA Simone C., Stiegler P., Bagella L., Pucci B., Bellan C., De Falco G.,
RA De Luca A., Guanti G., Puri P.L., Giordano A.;
RT "Activation of MyoD-dependent transcription by cdk9/cyclin T2.";
RL Oncogene 21:4137-4148(2002).
RN [10]
RP INTERACTION WITH SUV39H1.
RX PubMed=16858404; DOI=10.1038/sj.emboj.7601229;
RA Mal A.K.;
RT "Histone methyltransferase Suv39h1 represses MyoD-stimulated myogenic
RT differentiation.";
RL EMBO J. 25:3323-3334(2006).
RN [11]
RP METHYLATION AT LYS-104.
RX PubMed=22215600; DOI=10.1073/pnas.1111628109;
RA Ling B.M., Bharathy N., Chung T.K., Kok W.K., Li S., Tan Y.H., Rao V.K.,
RA Gopinadhan S., Sartorelli V., Walsh M.J., Taneja R.;
RT "Lysine methyltransferase G9a methylates the transcription factor MyoD and
RT regulates skeletal muscle differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:841-846(2012).
RN [12]
RP INTERACTION WITH CSRP3.
RX PubMed=24860983; DOI=10.1111/febs.12859;
RA Vafiadaki E., Arvanitis D.A., Papalouka V., Terzis G., Roumeliotis T.I.,
RA Spengos K., Garbis S.D., Manta P., Kranias E.G., Sanoudou D.;
RT "Muscle lim protein isoform negatively regulates striated muscle actin
RT dynamics and differentiation.";
RL FEBS J. 281:3261-3279(2014).
RN [13]
RP INVOLVEMENT IN MYODRIF, AND VARIANT MYODRIF 63-SER--LEU-320 DEL.
RX PubMed=26733463; DOI=10.1136/jmedgenet-2015-103620;
RA Watson C.M., Crinnion L.A., Murphy H., Newbould M., Harrison S.M.,
RA Lascelles C., Antanaviciute A., Carr I.M., Sheridan E., Bonthron D.T.,
RA Smith A.;
RT "Deficiency of the myogenic factor MyoD causes a perinatally lethal fetal
RT akinesia.";
RL J. Med. Genet. 53:264-269(2016).
RN [14]
RP INVOLVEMENT IN MYODRIF.
RX PubMed=31260566; DOI=10.1111/cge.13596;
RA Shukla A., Narayanan D.L., Asher U., Girisha K.M.;
RT "A novel bi-allelic loss-of-function variant in MYOD1: Further evidence for
RT gene-disease association and phenotypic variability in MYOD1-related
RT myopathy.";
RL Clin. Genet. 96:276-277(2019).
RN [15]
RP VARIANT MYODRIF 233-GLU--LEU-320 DEL.
RX PubMed=30403323; DOI=10.1111/ene.13782;
RA Lopes F., Miguet M., Mucha B.E., Gauthier J., Saillour V., Nguyen C.E.,
RA Vanasse M., Ellezam B., Michaud J.L., Soucy J.F., Campeau P.M.;
RT "MYOD1 involvement in myopathy.";
RL Eur. J. Neurol. 25:e123-e124(2018).
RN [16]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-262 AND VAL-309.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Acts as a transcriptional activator that promotes
CC transcription of muscle-specific target genes and plays a role in
CC muscle differentiation. Together with MYF5 and MYOG, co-occupies
CC muscle-specific gene promoter core region during myogenesis. Induces
CC fibroblasts to differentiate into myoblasts. Interacts with and is
CC inhibited by the twist protein. This interaction probably involves the
CC basic domains of both proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Seems to form active heterodimers with ITF-2. Interacts with
CC SUV39H1. Interacts with DDX5. Interacts with CHD2. Interacts with
CC TSC22D3 (By similarity). Interacts with SETD3 (By similarity).
CC Interacts with P-TEFB complex; promotes the transcriptional activity of
CC MYOD1 through its CDK9-mediated phosphorylation (By similarity)
CC (PubMed:12037670). Interacts with CSRP3. Interacts with NUPR1 (By
CC similarity). {ECO:0000250|UniProtKB:P10085,
CC ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:16858404,
CC ECO:0000269|PubMed:24860983}.
CC -!- INTERACTION:
CC P15172; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-488878, EBI-541426;
CC P15172; Q86VI1: EXOC3L1; NbExp=3; IntAct=EBI-488878, EBI-2813180;
CC P15172; Q6QHK4: FIGLA; NbExp=3; IntAct=EBI-488878, EBI-11976617;
CC P15172; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-488878, EBI-11955401;
CC P15172; P61968: LMO4; NbExp=3; IntAct=EBI-488878, EBI-2798728;
CC P15172; O43680: TCF21; NbExp=3; IntAct=EBI-488878, EBI-723267;
CC P15172; P15923-1: TCF3; NbExp=2; IntAct=EBI-488878, EBI-769645;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by CDK9. This phosphorylation promotes its function
CC in muscle differentiation. {ECO:0000269|PubMed:12037670}.
CC -!- PTM: Acetylated by a complex containing EP300 and PCAF. The acetylation
CC is essential to activate target genes. Conversely, its deacetylation by
CC SIRT1 inhibits its function (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated on the N-terminus; which is required for proteasomal
CC degradation. {ECO:0000269|PubMed:9774340}.
CC -!- PTM: Methylation at Lys-104 by EHMT2/G9a inhibits myogenic activity.
CC {ECO:0000269|PubMed:22215600}.
CC -!- DISEASE: Myopathy, congenital, with diaphragmatic defects, respiratory
CC insufficiency, and dysmorphic facies (MYODRIF) [MIM:618975]: An
CC autosomal recessive muscular disorder characterized by hypotonia and
CC respiratory insufficiency apparent soon after birth, high diaphragmatic
CC dome on imaging, poor overall growth, pectus excavatum, dysmorphic
CC facies, and renal anomalies in some affected individuals. Additional
CC variable features include delayed motor development, mildly decreased
CC endurance, distal arthrogryposis, and lung hypoplasia resulting in
CC early death. {ECO:0000269|PubMed:26733463, ECO:0000269|PubMed:30403323,
CC ECO:0000269|PubMed:31260566}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=MyoD entry;
CC URL="https://en.wikipedia.org/wiki/MyoD";
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DR EMBL; X56677; CAA40000.1; -; mRNA.
DR EMBL; AF027148; AAC29001.1; -; Genomic_DNA.
DR EMBL; BT007157; AAP35821.1; -; mRNA.
DR EMBL; CH471064; EAW68427.1; -; Genomic_DNA.
DR EMBL; BC064493; AAH64493.1; -; mRNA.
DR EMBL; X17650; CAA35640.1; -; mRNA.
DR CCDS; CCDS7826.1; -.
DR PIR; S26827; S26827.
DR RefSeq; NP_002469.2; NM_002478.4.
DR AlphaFoldDB; P15172; -.
DR SMR; P15172; -.
DR BioGRID; 110737; 165.
DR CORUM; P15172; -.
DR DIP; DIP-704N; -.
DR IntAct; P15172; 112.
DR MINT; P15172; -.
DR STRING; 9606.ENSP00000250003; -.
DR iPTMnet; P15172; -.
DR PhosphoSitePlus; P15172; -.
DR BioMuta; MYOD1; -.
DR DMDM; 209572729; -.
DR MassIVE; P15172; -.
DR PaxDb; P15172; -.
DR PeptideAtlas; P15172; -.
DR PRIDE; P15172; -.
DR ProteomicsDB; 53118; -.
DR Antibodypedia; 12172; 1102 antibodies from 46 providers.
DR DNASU; 4654; -.
DR Ensembl; ENST00000250003.4; ENSP00000250003.3; ENSG00000129152.4.
DR GeneID; 4654; -.
DR KEGG; hsa:4654; -.
DR MANE-Select; ENST00000250003.4; ENSP00000250003.3; NM_002478.5; NP_002469.2.
DR UCSC; uc001mni.4; human.
DR CTD; 4654; -.
DR DisGeNET; 4654; -.
DR GeneCards; MYOD1; -.
DR HGNC; HGNC:7611; MYOD1.
DR HPA; ENSG00000129152; Tissue enriched (skeletal).
DR MalaCards; MYOD1; -.
DR MIM; 159970; gene.
DR MIM; 618975; phenotype.
DR neXtProt; NX_P15172; -.
DR OpenTargets; ENSG00000129152; -.
DR Orphanet; 994; Fetal akinesia deformation sequence.
DR PharmGKB; PA31416; -.
DR VEuPathDB; HostDB:ENSG00000129152; -.
DR eggNOG; KOG3960; Eukaryota.
DR GeneTree; ENSGT00950000182959; -.
DR HOGENOM; CLU_066887_0_0_1; -.
DR InParanoid; P15172; -.
DR OMA; GPMEMTE; -.
DR OrthoDB; 1471470at2759; -.
DR PhylomeDB; P15172; -.
DR TreeFam; TF316344; -.
DR PathwayCommons; P15172; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; P15172; -.
DR SIGNOR; P15172; -.
DR BioGRID-ORCS; 4654; 14 hits in 1092 CRISPR screens.
DR ChiTaRS; MYOD1; human.
DR GeneWiki; MyoD; -.
DR GenomeRNAi; 4654; -.
DR Pharos; P15172; Tbio.
DR PRO; PR:P15172; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P15172; protein.
DR Bgee; ENSG00000129152; Expressed in triceps brachii and 51 other tissues.
DR Genevisible; P15172; HS.
DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL.
DR GO; GO:0000791; C:euchromatin; ISS:ARUK-UCL.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005667; C:transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:ARUK-UCL.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0042693; P:muscle cell fate commitment; ISS:BHF-UCL.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0007518; P:myoblast fate determination; IEA:Ensembl.
DR GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
DR GO; GO:0014904; P:myotube cell development; IDA:BHF-UCL.
DR GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl.
DR GO; GO:2000818; P:negative regulation of myoblast proliferation; IEA:Ensembl.
DR GO; GO:0051099; P:positive regulation of binding; IEA:Ensembl.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IDA:BHF-UCL.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IBA:GO_Central.
DR GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IBA:GO_Central.
DR GO; GO:0043503; P:skeletal muscle fiber adaptation; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; TAS:ProtInc.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR022032; Myf5.
DR InterPro; IPR002546; MyoD_N.
DR InterPro; IPR039704; Myogenic_factor.
DR PANTHER; PTHR11534; PTHR11534; 1.
DR Pfam; PF01586; Basic; 1.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF12232; Myf5; 1.
DR SMART; SM00520; BASIC; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Developmental protein; Differentiation;
KW Disease variant; DNA-binding; Methylation; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..320
FT /note="Myoblast determination protein 1"
FT /id="PRO_0000127360"
FT DOMAIN 109..160
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 174..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="N6-methyllysine; by EHMT2"
FT /evidence="ECO:0000269|PubMed:22215600"
FT CROSSLNK 1
FT /note="Peptide (Met-Gly) (interchain with G-Cter in
FT ubiquitin)"
FT /evidence="ECO:0000269|PubMed:9774340"
FT VARIANT 63..320
FT /note="Missing (in MYODRIF)"
FT /evidence="ECO:0000269|PubMed:26733463"
FT /id="VAR_084715"
FT VARIANT 233..320
FT /note="Missing (in MYODRIF; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30403323"
FT /id="VAR_084716"
FT VARIANT 262
FT /note="E -> K (in a breast cancer sample; somatic mutation;
FT dbSNP:rs930939009)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036392"
FT VARIANT 309
FT /note="A -> V (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1471293207)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036393"
FT CONFLICT 124
FT /note="K -> E (in Ref. 6; CAA35640)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="Missing (in Ref. 1; CAA40000 and 6; CAA35640)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="C -> Y (in Ref. 1; CAA40000 and 6; CAA35640)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 34501 MW; 75E624D2ED5B0B33 CRC64;
MELLSPPLRD VDLTAPDGSL CSFATTDDFY DDPCFDSPDL RFFEDLDPRL MHVGALLKPE
EHSHFPAAVH PAPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAAFYA
PGPLPPGRGG EHYSGDSDAS SPRSNCSDGM MDYSGPPSGA RRRNCYEGAY YNEAPSEPRP
GKSAAVSSLD CLSSIVERIS TESPAAPALL LADVPSESPP RRQEAAAPSE GESSGDPTQS
PDAAPQCPAG ANPNPIYQVL
