TNNT_DROME
ID TNNT_DROME Reviewed; 397 AA.
AC P19351; E1JJP1; E1JJP2; E1JJP3; E4NKN4; F2FB91; Q59E46; Q59E47; Q6T2Y5;
AC Q6T2Y6; Q6T2Y7; Q6T2Y8; Q6T2Y9; Q8SZI3; Q960L9; Q9VYB3; Q9VYB4; Q9VYB5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Troponin T, skeletal muscle;
DE AltName: Full=Protein intended thorax;
DE AltName: Full=Protein upheld;
GN Name=up; Synonyms=int; ORFNames=CG7107;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Canton-S; TISSUE=Asynchronous muscle;
RX PubMed=2852258; DOI=10.1016/0022-2836(88)90360-9;
RA Bullard B., Leonard K., Larkins A., Butcher G., Karlik C., Fyrberg E.A.;
RT "Troponin of asynchronous flight muscle.";
RL J. Mol. Biol. 204:621-637(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SEQUENCE REVISION, FUNCTION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S;
RX PubMed=2124273; DOI=10.1016/0022-2836(90)90390-8;
RA Fryberg E.A., Fryberg C.C., Beall C., Saville D.L.;
RT "Drosophila melanogaster troponin-T mutations engender three distinct
RT syndromes of myofibrillar abnormalities.";
RL J. Mol. Biol. 216:657-675(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RA Herranz-Barranco R.;
RT "Gene evolution of the troponin complex in insects.";
RL Thesis (2003), Universidad Autonoma de Madrid (UAM), Spain.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
RA Nongthomba U., Ansari M., Sparrow J.;
RT "Drosophila TpnT exon 10 is alternatively spliced.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-8 (ISOFORMS 2/3/6/8/9).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
CC -!- FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin,
CC the thin filament regulatory complex which confers calcium-sensitivity
CC to striated muscle actomyosin ATPase activity.
CC {ECO:0000269|PubMed:2124273}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1; Synonyms=A;
CC IsoId=P19351-1; Sequence=Displayed;
CC Name=2; Synonyms=T-2;
CC IsoId=P19351-2; Sequence=VSP_015192;
CC Name=3; Synonyms=T-1;
CC IsoId=P19351-3; Sequence=VSP_015192, VSP_015194;
CC Name=4; Synonyms=G;
CC IsoId=P19351-4; Sequence=VSP_015195;
CC Name=5; Synonyms=K;
CC IsoId=P19351-5; Sequence=VSP_041843, VSP_015194, VSP_015195;
CC Name=6; Synonyms=E, T-4;
CC IsoId=P19351-6; Sequence=VSP_015191;
CC Name=7; Synonyms=B;
CC IsoId=P19351-7; Sequence=VSP_015193;
CC Name=8; Synonyms=T-3;
CC IsoId=P19351-8; Sequence=VSP_015192, VSP_015193;
CC Name=9; Synonyms=T-5;
CC IsoId=P19351-9; Sequence=VSP_015191, VSP_015196;
CC Name=10; Synonyms=D;
CC IsoId=P19351-10; Sequence=VSP_015189;
CC Name=11; Synonyms=I;
CC IsoId=P19351-11; Sequence=VSP_015196;
CC Name=12; Synonyms=L;
CC IsoId=P19351-12; Sequence=VSP_041843, VSP_041844, VSP_015195;
CC Name=13; Synonyms=J;
CC IsoId=P19351-13; Sequence=VSP_015193, VSP_015196;
CC -!- TISSUE SPECIFICITY: Isoform 3 is expressed in the hypoderm. Isoform 8
CC is expressed in the dorsal vessel. Isoform 6 is expressed in adult TDT
CC muscle and isoform 9 in adult IFM, flight and jump muscles.
CC {ECO:0000269|PubMed:2124273}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed only in larvae.
CC -!- PTM: Some glutamate residues are polyglycylated by TTLL3B. This
CC modification occurs exclusively on glutamate residues and results in
CC polyglycine chains on the gamma-carboxyl group.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit 3 distinct syndromes of
CC myofibrillar abnormalities; elimination of thin filaments except where
CC they are bound by electron-dense material presumed to be Z-disk
CC proteins, degeneration of muscles and reduction in the diameter of the
CC myofibril lattice. {ECO:0000269|PubMed:2124273}.
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48497.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; X54504; CAA38366.1; -; mRNA.
DR EMBL; AY439172; AAR24583.1; -; Genomic_DNA.
DR EMBL; AY439172; AAR24584.1; -; Genomic_DNA.
DR EMBL; AY439172; AAR24585.1; -; Genomic_DNA.
DR EMBL; AY439172; AAR24586.1; -; Genomic_DNA.
DR EMBL; AY439172; AAR24587.1; -; Genomic_DNA.
DR EMBL; AY665838; AAU09446.1; -; mRNA.
DR EMBL; AE014298; AAF48288.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48289.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48290.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52491.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52492.1; -; Genomic_DNA.
DR EMBL; AE014298; AAX52493.2; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95277.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95278.1; -; Genomic_DNA.
DR EMBL; AE014298; ACZ95279.1; -; Genomic_DNA.
DR EMBL; AY051989; AAK93413.1; -; mRNA.
DR EMBL; AY070875; AAL48497.1; ALT_SEQ; mRNA.
DR EMBL; BT125831; ADR83716.1; -; mRNA.
DR EMBL; BT126178; ADZ99430.1; -; mRNA.
DR PIR; S02708; S02708.
DR PIR; S13251; S13251.
DR RefSeq; NP_001014737.1; NM_001014737.2. [P19351-4]
DR RefSeq; NP_001014738.2; NM_001014738.3. [P19351-5]
DR RefSeq; NP_001014739.1; NM_001014739.2. [P19351-6]
DR RefSeq; NP_001162741.1; NM_001169270.2. [P19351-9]
DR RefSeq; NP_001162742.1; NM_001169271.2. [P19351-11]
DR RefSeq; NP_001162743.1; NM_001169272.2. [P19351-13]
DR RefSeq; NP_001162744.1; NM_001169273.2. [P19351-12]
DR RefSeq; NP_001259522.1; NM_001272593.2. [P19351-3]
DR RefSeq; NP_001259523.1; NM_001272594.2. [P19351-2]
DR RefSeq; NP_001259524.1; NM_001272595.2. [P19351-8]
DR RefSeq; NP_001285213.1; NM_001298284.1. [P19351-8]
DR RefSeq; NP_001285214.1; NM_001298285.1. [P19351-8]
DR RefSeq; NP_001285215.1; NM_001298286.1. [P19351-10]
DR RefSeq; NP_525088.2; NM_080349.3. [P19351-1]
DR RefSeq; NP_727718.1; NM_167375.2. [P19351-7]
DR RefSeq; NP_727719.1; NM_167376.2. [P19351-10]
DR AlphaFoldDB; P19351; -.
DR SMR; P19351; -.
DR BioGRID; 58691; 43.
DR IntAct; P19351; 3.
DR STRING; 7227.FBpp0073682; -.
DR PaxDb; P19351; -.
DR PeptideAtlas; P19351; -.
DR PRIDE; P19351; -.
DR DNASU; 32314; -.
DR EnsemblMetazoa; FBtr0073851; FBpp0073682; FBgn0004169. [P19351-1]
DR EnsemblMetazoa; FBtr0073852; FBpp0073683; FBgn0004169. [P19351-7]
DR EnsemblMetazoa; FBtr0073853; FBpp0073684; FBgn0004169. [P19351-10]
DR EnsemblMetazoa; FBtr0100561; FBpp0100013; FBgn0004169. [P19351-6]
DR EnsemblMetazoa; FBtr0100563; FBpp0100015; FBgn0004169. [P19351-4]
DR EnsemblMetazoa; FBtr0301919; FBpp0291133; FBgn0004169. [P19351-9]
DR EnsemblMetazoa; FBtr0301920; FBpp0291134; FBgn0004169. [P19351-11]
DR EnsemblMetazoa; FBtr0301921; FBpp0291135; FBgn0004169. [P19351-13]
DR EnsemblMetazoa; FBtr0301922; FBpp0291136; FBgn0004169. [P19351-5]
DR EnsemblMetazoa; FBtr0301923; FBpp0291137; FBgn0004169. [P19351-12]
DR EnsemblMetazoa; FBtr0310136; FBpp0301821; FBgn0004169. [P19351-3]
DR EnsemblMetazoa; FBtr0310137; FBpp0301822; FBgn0004169. [P19351-2]
DR EnsemblMetazoa; FBtr0310138; FBpp0301823; FBgn0004169. [P19351-8]
DR EnsemblMetazoa; FBtr0340617; FBpp0309481; FBgn0004169. [P19351-8]
DR EnsemblMetazoa; FBtr0340618; FBpp0309482; FBgn0004169. [P19351-8]
DR EnsemblMetazoa; FBtr0345131; FBpp0311352; FBgn0004169. [P19351-10]
DR GeneID; 32314; -.
DR KEGG; dme:Dmel_CG7107; -.
DR CTD; 104073; -.
DR FlyBase; FBgn0004169; up.
DR VEuPathDB; VectorBase:FBgn0004169; -.
DR eggNOG; KOG3634; Eukaryota.
DR GeneTree; ENSGT00730000112220; -.
DR InParanoid; P19351; -.
DR OMA; WGRRENE; -.
DR PhylomeDB; P19351; -.
DR SignaLink; P19351; -.
DR BioGRID-ORCS; 32314; 0 hits in 3 CRISPR screens.
DR ChiTaRS; up; fly.
DR GenomeRNAi; 32314; -.
DR PRO; PR:P19351; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004169; Expressed in oviduct (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P19351; baseline and differential.
DR Genevisible; P19351; DM.
DR GO; GO:0005865; C:striated muscle thin filament; IDA:FlyBase.
DR GO; GO:0005861; C:troponin complex; IDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
DR GO; GO:0005523; F:tropomyosin binding; IDA:FlyBase.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0048644; P:muscle organ morphogenesis; IMP:FlyBase.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:FlyBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR027707; TNNT.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR11521; PTHR11521; 1.
DR Pfam; PF00992; Troponin; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Muscle protein; Reference proteome.
FT CHAIN 1..397
FT /note="Troponin T, skeletal muscle"
FT /id="PRO_0000186185"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..397
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_015189"
FT VAR_SEQ 9..31
FT /note="Missing (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015191"
FT VAR_SEQ 9
FT /note="Missing (in isoform 2, isoform 3 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:2124273,
FT ECO:0000303|PubMed:2852258"
FT /id="VSP_015192"
FT VAR_SEQ 10
FT /note="Missing (in isoform 5 and isoform 12)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_041843"
FT VAR_SEQ 24..31
FT /note="Missing (in isoform 7, isoform 8 and isoform 13)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_015193"
FT VAR_SEQ 24
FT /note="K -> KK (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_015194"
FT VAR_SEQ 25..31
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_041844"
FT VAR_SEQ 155
FT /note="Missing (in isoform 4, isoform 5 and isoform 12)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_015195"
FT VAR_SEQ 288..311
FT /note="WDEISKDSNEKIWNEKKEQYTGRQ -> YNTVYAETLEKTWQERQERFTQRT
FT (in isoform 9, isoform 11 and isoform 13)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015196"
FT CONFLICT 119
FT /note="R -> A (in Ref. 1; no nucleotide entry and 2;
FT CAA38366)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="G -> A (in Ref. 1; no nucleotide entry and 2;
FT CAA38366)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="A -> D (in Ref. 1; no nucleotide entry and 2;
FT CAA38366)"
FT /evidence="ECO:0000305"
FT CONFLICT P19351-5:9
FT /note="S -> SS (in Ref. 8; ADR83716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 47448 MW; 9D1E9074548CB8D5 CRC64;
MSDDEEYTSS EEEEVVEETR EETKPPQTPA EGEGDPEFIK RQDQKRSDLD DQLKEYITEW
RKQRSKEEDE LKKLKEKQAK RKVTRAEEEQ KMAQRKKEEE ERRVREAEEK KQREIEEKRM
RLEEAEKKRQ AMLQAMKDKD KKGPNFTIAK KDAGVLGLSS AAMERNKTKE QLEEEKKISL
SFRIKPLAIE GFGEAKLREK AQELWELIVK LETEKYDLEE RQKRQDYDLK ELKERQKQQL
RHKALKKGLD PEALTGKYPP KIQVASKYER RVDTRSYDDK KKLFEGGWDE ISKDSNEKIW
NEKKEQYTGR QKSKLPKWFG ERPGKKAGEP ETPEGEEDAK ADEDIVEDDE EVEEEVVEEE
DEEAEEDEEE EEEEEEEEEE EEEEEEEEEE EEEEEEE
