ID   TRDN_HUMAN              Reviewed;         729 AA.
AC   Q13061; A5D6W5; F5H2W7; Q6NSB8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 4.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=Triadin;
GN   Name=TRDN;
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), AND VARIANTS VAL-201 AND SER-438.
RC   TISSUE=Skeletal muscle;
RX   PubMed=7588753; DOI=10.1111/j.1432-1033.1995.258_1.x;
RA   Taske N.L., Eyre H.J., O'Brien R.O., Sutherland G.R., Denborough M.A.,
RA   Foster P.S.;
RT   "Molecular cloning of the cDNA encoding human skeletal muscle triadin and
RT   its localisation to chromosome 6q22-6q23.";
RL   Eur. J. Biochem. 233:258-265(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANTS
RP   SER-128 AND VAL-201.
RC   TISSUE=Skeletal 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   [4]
RP   INTERACTION WITH CASQ2.
RX   PubMed=15485681; DOI=10.1016/j.cardiores.2004.09.009;
RA   Houle T.D., Ram M.L., Cala S.E.;
RT   "Calsequestrin mutant D307H exhibits depressed binding to its protein
RT   targets and a depressed response to calcium.";
RL   Cardiovasc. Res. 64:227-233(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, VARIANT CARDAR ARG-59, CHARACTERIZATION OF VARIANT
RP   CARDAR ARG-59, AND FUNCTION.
RX   PubMed=22422768; DOI=10.1093/hmg/dds104;
RA   Roux-Buisson N., Cacheux M., Fourest-Lieuvin A., Fauconnier J., Brocard J.,
RA   Denjoy I., Durand P., Guicheney P., Kyndt F., Leenhardt A., Le Marec H.,
RA   Lucet V., Mabo P., Probst V., Monnier N., Ray P.F., Santoni E.,
RA   Tremeaux P., Lacampagne A., Faure J., Lunardi J., Marty I.;
RT   "Absence of triadin, a protein of the calcium release complex, is
RT   responsible for cardiac arrhythmia with sudden death in human.";
RL   Hum. Mol. Genet. 21:2759-2767(2012).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH RYR1 AND CASQ1.
RX   PubMed=24325401; DOI=10.1042/bj20130719;
RA   Rossi D., Bencini C., Maritati M., Benini F., Lorenzini S., Pierantozzi E.,
RA   Scarcella A.M., Paolini C., Protasi F., Sorrentino V.;
RT   "Distinct regions of triadin are required for targeting and retention at
RT   the junctional domain of the sarcoplasmic reticulum.";
RL   Biochem. J. 458:407-417(2014).
CC   -!- FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the
CC       sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key
CC       step in triggering skeletal and heart muscle contraction. Required for
CC       normal organization of the triad junction, where T-tubules and the
CC       sarcoplasmic reticulum terminal cisternae are in close contact (By
CC       similarity). Required for normal skeletal muscle strength. Plays a role
CC       in excitation-contraction coupling in the heart and in regulating the
CC       rate of heart beats. {ECO:0000250|UniProtKB:E9Q9K5,
CC       ECO:0000269|PubMed:22422768}.
CC   -!- SUBUNIT: Homooligomer of variable subunit number; disulfide-linked (By
CC       similarity). Interacts with CASQ1 and RYR1 in skeletal muscle.
CC       Interacts with CASQ2. {ECO:0000250|UniProtKB:Q28820,
CC       ECO:0000269|PubMed:15485681, ECO:0000269|PubMed:24325401}.
CC   -!- INTERACTION:
CC       Q13061-2; Q8WWG9: KCNE4; NbExp=3; IntAct=EBI-17257686, EBI-11750916;
CC       Q13061-2; P23284: PPIB; NbExp=3; IntAct=EBI-17257686, EBI-359252;
CC       Q13061-2; Q16849-3: PTPRN; NbExp=3; IntAct=EBI-17257686, EBI-10200782;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22422768}.
CC       Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:22422768,
CC       ECO:0000269|PubMed:24325401}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:22422768, ECO:0000269|PubMed:24325401}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q13061-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13061-2; Sequence=VSP_045563, VSP_045564, VSP_045565;
CC       Name=3;
CC         IsoId=Q13061-3; Sequence=VSP_045561, VSP_045562;
CC   -!- PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:E9Q9K5}.
CC   -!- DISEASE: Cardiac arrhythmia syndrome, with or without skeletal muscle
CC       weakness (CARDAR) [MIM:615441]: An autosomal recessive cardiac disorder
CC       characterized by stress-induced arrhythmias in infancy or early
CC       childhood. Patients present with recurrent syncope or cardiac arrest
CC       after physical activity or emotional stress. Sudden death may occur in
CC       early childhood. Some patients have muscle weakness.
CC       {ECO:0000269|PubMed:22422768}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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DR   EMBL; U18985; AAA75315.1; -; mRNA.
DR   EMBL; AL133257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL357352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL603902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL603911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC070290; AAH70290.1; -; mRNA.
DR   EMBL; BC139910; AAI39911.1; -; mRNA.
DR   CCDS; CCDS55053.1; -. [Q13061-1]
DR   CCDS; CCDS59034.1; -. [Q13061-2]
DR   CCDS; CCDS59035.1; -. [Q13061-3]
DR   PIR; S68191; S68191.
DR   RefSeq; NP_001242949.1; NM_001256020.1. [Q13061-2]
DR   RefSeq; NP_001242951.1; NM_001256022.1. [Q13061-3]
DR   RefSeq; NP_006064.2; NM_006073.3. [Q13061-1]
DR   AlphaFoldDB; Q13061; -.
DR   SMR; Q13061; -.
DR   BioGRID; 115627; 59.
DR   IntAct; Q13061; 38.
DR   STRING; 9606.ENSP00000333984; -.
DR   TCDB; 8.A.28.1.3; the ankyrin (ankyrin) family.
DR   GlyCosmos; Q13061; 3 sites, 1 glycan.
DR   GlyGen; Q13061; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13061; -.
DR   PhosphoSitePlus; Q13061; -.
DR   BioMuta; TRDN; -.
DR   EPD; Q13061; -.
DR   MassIVE; Q13061; -.
DR   PaxDb; 9606-ENSP00000439281; -.
DR   PeptideAtlas; Q13061; -.
DR   ProteomicsDB; 26096; -.
DR   ProteomicsDB; 59126; -. [Q13061-1]
DR   Antibodypedia; 51878; 53 antibodies from 12 providers.
DR   DNASU; 10345; -.
DR   Ensembl; ENST00000334268.9; ENSP00000333984.5; ENSG00000186439.15. [Q13061-1]
DR   Ensembl; ENST00000542443.5; ENSP00000437684.1; ENSG00000186439.15. [Q13061-3]
DR   Ensembl; ENST00000628709.2; ENSP00000486095.1; ENSG00000186439.15. [Q13061-2]
DR   GeneID; 10345; -.
DR   KEGG; hsa:10345; -.
DR   MANE-Select; ENST00000334268.9; ENSP00000333984.5; NM_006073.4; NP_006064.2.
DR   UCSC; uc010keo.3; human. [Q13061-1]
DR   AGR; HGNC:12261; -.
DR   CTD; 10345; -.
DR   DisGeNET; 10345; -.
DR   GeneCards; TRDN; -.
DR   GeneReviews; TRDN; -.
DR   HGNC; HGNC:12261; TRDN.
DR   HPA; ENSG00000186439; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR   MalaCards; TRDN; -.
DR   MIM; 603283; gene.
DR   MIM; 615441; phenotype.
DR   neXtProt; NX_Q13061; -.
DR   OpenTargets; ENSG00000186439; -.
DR   Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
DR   Orphanet; 101016; Romano-Ward syndrome.
DR   PharmGKB; PA36941; -.
DR   VEuPathDB; HostDB:ENSG00000186439; -.
DR   eggNOG; ENOG502S0X4; Eukaryota.
DR   GeneTree; ENSGT00510000049207; -.
DR   HOGENOM; CLU_104022_2_0_1; -.
DR   InParanoid; Q13061; -.
DR   OMA; QIHKQDI; -.
DR   OrthoDB; 5363225at2759; -.
DR   TreeFam; TF350396; -.
DR   PathwayCommons; Q13061; -.
DR   Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR   Reactome; R-HSA-5578775; Ion homeostasis.
DR   SignaLink; Q13061; -.
DR   BioGRID-ORCS; 10345; 11 hits in 1117 CRISPR screens.
DR   ChiTaRS; TRDN; human.
DR   GeneWiki; Triadin; -.
DR   GenomeRNAi; 10345; -.
DR   Pharos; Q13061; Tbio.
DR   PRO; PR:Q13061; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q13061; Protein.
DR   Bgee; ENSG00000186439; Expressed in skeletal muscle tissue of rectus abdominis and 123 other cell types or tissues.
DR   ExpressionAtlas; Q13061; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
DR   GO; GO:0030314; C:junctional membrane complex; ISS:BHF-UCL.
DR   GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; ISS:BHF-UCL.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:BHF-UCL.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; TAS:BHF-UCL.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; TAS:BHF-UCL.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISS:BHF-UCL.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:BHF-UCL.
DR   GO; GO:0090158; P:endoplasmic reticulum membrane organization; ISS:BHF-UCL.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0060047; P:heart contraction; IMP:BHF-UCL.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; ISS:BHF-UCL.
DR   GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR   GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
DR   GO; GO:1901846; P:positive regulation of cell communication by electrical coupling involved in cardiac conduction; ISS:BHF-UCL.
DR   GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL.
DR   GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; ISS:BHF-UCL.
DR   GO; GO:0010649; P:regulation of cell communication by electrical coupling; TAS:BHF-UCL.
DR   GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; TAS:BHF-UCL.
DR   GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:BHF-UCL.
DR   GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:BHF-UCL.
DR   GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR   InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR   InterPro; IPR010798; Triadin.
DR   PANTHER; PTHR14106; TRIADIN; 1.
DR   PANTHER; PTHR14106:SF0; TRIADIN; 1.
DR   Pfam; PF05279; Asp-B-Hydro_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT   CHAIN           1..729
FT                   /note="Triadin"
FT                   /id="PRO_0000065626"
FT   TOPO_DOM        1..47
FT                   /note="Cytoplasmic"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..729
FT                   /note="Lumenal"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..131
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..300
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..566
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        573..678
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        647
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        270
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q28820"
FT   DISULFID        691
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q28820"
FT   VAR_SEQ         162..167
FT                   /note="VTHKEK -> EVGHSS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045561"
FT   VAR_SEQ         168..729
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045562"
FT   VAR_SEQ         265..284
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045563"
FT   VAR_SEQ         311..317
FT                   /note="EKEGEKK -> GKYFFFS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045564"
FT   VAR_SEQ         318..729
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_045565"
FT   VARIANT         59
FT                   /note="T -> R (in CARDAR; results in intracellular
FT                   retention and degradation of the mutant protein;
FT                   dbSNP:rs397515459)"
FT                   /evidence="ECO:0000269|PubMed:22422768"
FT                   /id="VAR_067350"
FT   VARIANT         128
FT                   /note="T -> S (in dbSNP:rs9490809)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_057008"
FT   VARIANT         201
FT                   /note="L -> V (in dbSNP:rs6902416)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:7588753"
FT                   /id="VAR_065263"
FT   VARIANT         339
FT                   /note="S -> N (in dbSNP:rs35766971)"
FT                   /id="VAR_057009"
FT   VARIANT         396
FT                   /note="K -> N (in dbSNP:rs6901953)"
FT                   /id="VAR_065264"
FT   VARIANT         404
FT                   /note="V -> G (in dbSNP:rs28494009)"
FT                   /id="VAR_057010"
FT   VARIANT         419
FT                   /note="D -> E (in dbSNP:rs17737379)"
FT                   /id="VAR_057011"
FT   VARIANT         438
FT                   /note="I -> S (in dbSNP:rs2873479)"
FT                   /evidence="ECO:0000269|PubMed:7588753"
FT                   /id="VAR_065265"
FT   VARIANT         470
FT                   /note="L -> M (in dbSNP:rs6569336)"
FT                   /id="VAR_057012"
FT   VARIANT         540
FT                   /note="I -> M (in dbSNP:rs7771303)"
FT                   /id="VAR_057013"
SQ   SEQUENCE   729 AA;  81595 MW;  0D9653203D52FA05 CRC64;
     MTEITAEGNA STTTTVIDSK NGSVPKSPGK VLKRTVTEDI VTTFSSPAAW LLVIALIITW
     SAVAIVMFDL VDYKNFSASS IAKIGSDPLK LVRDAMEETT DWIYGFFSLL SDIISSEDEE
     DDDGDEDTDK GEIDEPPLRK KEIHKDKTEK QEKPERKIQT KVTHKEKEKG KEKVREKEKP
     EKKATHKEKI EKKEKPETKT LAKEQKKAKT AEKSEEKTKK EVKGGKQEKV KQTAAKVKEV
     QKTPSKPKEK EDKEKAAVSK HEQKDQYAFC RYMIDIFVHG DLKPGQSPAI PPPLPTEQAS
     RPTPASPALE EKEGEKKKAE KKVTSETKKK EKEDIKKKSE KETAIDVEKK EPGKASETKQ
     GTVKIAAQAA AKKDEKKEDS KKTKKPAEVE QPKGKKQEKK EKHVEPAKSP KKEHSVPSDK
     QVKAKTERAK EEIGAVSIKK AVPGKKEEKT TKTVEQEIRK EKSGKTSSIL KDKEPIKGKE
     EKVPASLKEK EPETKKDEKM SKAGKEVKPK PPQLQGKKEE KPEPQIKKEA KPAISEKVQI
     HKQDIVKPEK TVSHGKPEEK VLKQVKAVTI EKTAKPKPTK KAEHREREPP SIKTDKPKPT
     PKGTSEVTES GKKKTEISEK ESKEKADMKH LREEKVSTRK ESLQLHNVTK AEKPARVSKD
     VEDVPASKKA KEGTEDVSPT KQKSPISFFQ CVYLDGYNGY GFQFPFTPAD RPGESSGQAN
     SPGQKQQGQ
//