TRHY_HUMAN
ID TRHY_HUMAN Reviewed; 1943 AA.
AC Q07283; Q5VUI3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Trichohyalin;
GN Name=TCHH; Synonyms=THH, THL, TRHY;
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 [GENOMIC DNA], AND VARIANTS ARG-63; VAL-1258 AND
RP GLN-1902.
RX PubMed=7685034; DOI=10.1016/s0021-9258(19)50322-2;
RA Lee S.-C., Kim I.-G., Marekov L.N., O'Keefe E.J., Parry D.A.D.,
RA Steinert P.M.;
RT "The structure of human trichohyalin. Potential multiple roles as a
RT functional EF-hand-like calcium-binding protein, a cornified cell envelope
RT precursor, and an intermediate filament-associated (cross-linking)
RT protein.";
RL J. Biol. Chem. 268:12164-12176(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1776-1943, AND
RP CHARACTERIZATION.
RX PubMed=7686953; DOI=10.1111/1523-1747.ep12362866;
RA O'Keefe E.J., Hamilton E.H., Lee S.-C., Steinert P.M.;
RT "Trichohyalin: a structural protein of hair, tongue, nail, and epidermis.";
RL J. Invest. Dermatol. 101:65S-71S(1993).
RN [4]
RP INVOLVEMENT IN UHS3.
RX PubMed=27866708; DOI=10.1016/j.ajhg.2016.10.004;
RA Ue Basmanav F.B., Cau L., Tafazzoli A., Mechin M.C., Wolf S., Romano M.T.,
RA Valentin F., Wiegmann H., Huchenq A., Kandil R., Garcia Bartels N.,
RA Kilic A., George S., Ralser D.J., Bergner S., Ferguson D.J.,
RA Oprisoreanu A.M., Wehner M., Thiele H., Altmueller J., Nuernberg P.,
RA Swan D., Houniet D., Buechner A., Weibel L., Wagner N., Grimalt R.,
RA Bygum A., Serre G., Blume-Peytavi U., Sprecher E., Schoch S., Oji V.,
RA Hamm H., Farrant P., Simon M., Betz R.C.;
RT "Mutations in three genes encoding proteins involved in hair shaft
RT formation cause uncombable hair syndrome.";
RL Am. J. Hum. Genet. 99:1292-1304(2016).
RN [5]
RP VARIANT PRO-1400.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Intermediate filament-associated protein that associates in
CC regular arrays with keratin intermediate filaments (KIF) of the inner
CC root sheath cells of the hair follicle and the granular layer of the
CC epidermis. It later becomes cross-linked to KIF by isodipeptide bonds.
CC It may serve as scaffold protein, together with involucrin, in the
CC organization of the cell envelope or even anchor the cell envelope to
CC the KIF network. It may be involved in its own calcium-dependent
CC postsynthetic processing during terminal differentiation.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Found in the hard keratinizing tissues such as the
CC inner root sheath (IRS) of hair follicles and medulla, and in the
CC filiform papillae of dorsal tongue epithelium.
CC -!- DEVELOPMENTAL STAGE: Expressed during late differentiation of the
CC epidermis.
CC -!- DOMAIN: Consists of nine domains. Domain 1 contains two EF-hand
CC calcium-binding domains. Domains 2-4, 6, and 8 are almost entirely
CC alpha-helical, configured as a series of peptide repeats of varying
CC regularity, and are thought to form a single-stranded alpha-helical rod
CC stabilized by ionic interactions. Domain 6 is the most regular and may
CC bind KIF directly by ionic interactions. Domains 5 and 7 are less well
CC organized and may induce folds in the molecule. Domain 9 contains the
CC C-terminus, conserved among different species.
CC -!- PTM: Substrate of transglutaminase. Some 200 arginines are probably
CC converted to citrullines by peptidylarginine deimidase.
CC -!- DISEASE: Uncombable hair syndrome 3 (UHS3) [MIM:617252]: A form of
CC uncombable hair syndrome, a condition characterized by scalp hair that
CC is impossible to comb due to the haphazard arrangement of the hair
CC bundles. A characteristic morphologic feature is a triangular to
CC reniform to heart shape on cross-sections, and a groove, canal or
CC flattening along the entire length of the hair. Most individuals are
CC affected early in childhood and the hair takes on a spun-glass
CC appearance with the hair becoming dry, curly, glossy, lighter in color,
CC and progressively uncombable. The hair growth rate can range from slow
CC to normal, and the condition improves with age.
CC {ECO:0000269|PubMed:27866708}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the S100-fused protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA65582.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L09190; AAA65582.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL589986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS41396.1; -.
DR PIR; A45973; A45973.
DR RefSeq; NP_009044.2; NM_007113.3.
DR AlphaFoldDB; Q07283; -.
DR SMR; Q07283; -.
DR BioGRID; 112919; 17.
DR IntAct; Q07283; 6.
DR STRING; 9606.ENSP00000480484; -.
DR CarbonylDB; Q07283; -.
DR iPTMnet; Q07283; -.
DR PhosphoSitePlus; Q07283; -.
DR BioMuta; TCHH; -.
DR DMDM; 215273930; -.
DR EPD; Q07283; -.
DR jPOST; Q07283; -.
DR MassIVE; Q07283; -.
DR MaxQB; Q07283; -.
DR PaxDb; Q07283; -.
DR PeptideAtlas; Q07283; -.
DR PRIDE; Q07283; -.
DR ProteomicsDB; 58508; -.
DR Antibodypedia; 34083; 40 antibodies from 15 providers.
DR DNASU; 7062; -.
DR Ensembl; ENST00000614923.2; ENSP00000480484.1; ENSG00000159450.13.
DR GeneID; 7062; -.
DR KEGG; hsa:7062; -.
DR MANE-Select; ENST00000614923.2; ENSP00000480484.1; NM_007113.4; NP_009044.2.
DR UCSC; uc001ezp.3; human.
DR CTD; 7062; -.
DR DisGeNET; 7062; -.
DR GeneCards; TCHH; -.
DR HGNC; HGNC:11791; TCHH.
DR HPA; ENSG00000159450; Tissue enriched (skin).
DR MalaCards; TCHH; -.
DR MIM; 190370; gene.
DR MIM; 617252; phenotype.
DR neXtProt; NX_Q07283; -.
DR OpenTargets; ENSG00000159450; -.
DR PharmGKB; PA36503; -.
DR VEuPathDB; HostDB:ENSG00000159450; -.
DR eggNOG; ENOG502QQH0; Eukaryota.
DR GeneTree; ENSGT00940000164620; -.
DR HOGENOM; CLU_001958_0_0_1; -.
DR InParanoid; Q07283; -.
DR OMA; QYREAEQ; -.
DR OrthoDB; 1367189at2759; -.
DR TreeFam; TF344077; -.
DR PathwayCommons; Q07283; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q07283; -.
DR BioGRID-ORCS; 7062; 11 hits in 1062 CRISPR screens.
DR ChiTaRS; TCHH; human.
DR GeneWiki; TCHH; -.
DR GenomeRNAi; 7062; -.
DR Pharos; Q07283; Tbio.
DR PRO; PR:Q07283; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q07283; protein.
DR Bgee; ENSG00000159450; Expressed in upper arm skin and 76 other tissues.
DR Genevisible; Q07283; HS.
DR GO; GO:0001533; C:cornified envelope; TAS:Reactome.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR033200; TCHH.
DR PANTHER; PTHR34855; PTHR34855; 4.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Citrullination; Keratinization; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1943
FT /note="Trichohyalin"
FT /id="PRO_0000144042"
FT DOMAIN 23..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 314..326
FT /note="1-1; approximate"
FT REPEAT 327..339
FT /note="1-2; approximate"
FT REPEAT 340..351
FT /note="1-3; approximate"
FT REPEAT 352..364
FT /note="1-4"
FT REPEAT 365..377
FT /note="1-5"
FT REPEAT 378..383
FT /note="2-1"
FT REPEAT 384..389
FT /note="2-2"
FT REPEAT 390..395
FT /note="2-3"
FT REPEAT 396..401
FT /note="2-4"
FT REPEAT 402..407
FT /note="2-5"
FT REPEAT 408..413
FT /note="2-6"
FT REPEAT 414..419
FT /note="2-7"
FT REPEAT 420..425
FT /note="2-8"
FT REPEAT 906..935
FT /note="4-1"
FT REPEAT 936..965
FT /note="4-2"
FT REPEAT 966..995
FT /note="4-3"
FT REPEAT 996..1025
FT /note="4-4"
FT REPEAT 1026..1055
FT /note="4-5"
FT REPEAT 1056..1085
FT /note="4-6"
FT REPEAT 1086..1115
FT /note="4-7"
FT REPEAT 1116..1145
FT /note="4-8"
FT REPEAT 1146..1175
FT /note="4-9"
FT REPEAT 1176..1204
FT /note="4-10"
FT REGION 1..91
FT /note="S-100-like"
FT REGION 110..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..377
FT /note="5 X 13 AA tandem repeats of R-R-E-Q-E-E-E-R-R-E-Q-Q-
FT L"
FT REGION 378..425
FT /note="8 X 6 AA tandem repeats of R-R-E-Q-Q-L"
FT REGION 425..683
FT /note="9 X 28 AA approximate tandem repeats"
FT REGION 426..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..1204
FT /note="10 X 30 AA tandem repeats"
FT REGION 950..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1894
FT /note="23 X 26 AA approximate tandem repeats"
FT REGION 1404..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1834..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000305"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 63
FT /note="L -> R (in dbSNP:rs2515663)"
FT /evidence="ECO:0000269|PubMed:7685034"
FT /id="VAR_047519"
FT VARIANT 237
FT /note="V -> L (in dbSNP:rs3134814)"
FT /id="VAR_047520"
FT VARIANT 552
FT /note="R -> S (in dbSNP:rs6680692)"
FT /id="VAR_047521"
FT VARIANT 790
FT /note="L -> M (in dbSNP:rs11803731)"
FT /id="VAR_047522"
FT VARIANT 1258
FT /note="L -> V (in dbSNP:rs2496253)"
FT /evidence="ECO:0000269|PubMed:7685034"
FT /id="VAR_047523"
FT VARIANT 1400
FT /note="R -> P (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064757"
FT VARIANT 1902
FT /note="K -> Q (in dbSNP:rs1131471)"
FT /evidence="ECO:0000269|PubMed:7685034"
FT /id="VAR_047524"
FT CONFLICT 115
FT /note="Q -> T (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="R -> L (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 617..618
FT /note="EQ -> DE (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 631..632
FT /note="QQ -> HE (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 644..645
FT /note="QQ -> HE (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="R -> G (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="Missing (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289..1290
FT /note="RD -> AN (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1354
FT /note="R -> L (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="R -> L (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1385..1386
FT /note="RQ -> E (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1401..1402
FT /note="CQ -> LE (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1406
FT /note="Missing (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1617
FT /note="Missing (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
FT CONFLICT 1782
FT /note="E -> G (in Ref. 1; AAA65582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1943 AA; 253925 MW; 52FA297BD7AE3E53 CRC64;
MSPLLRSICD ITEIFNQYVS HDCDGAALTK KDLKNLLERE FGAVLRRPHD PKTVDLILEL
LDLDSNGRVD FNEFLLFIFK VAQACYYALG QATGLDEEKR ARCDGKESLL QDRRQEEDQR
RFEPRDRQLE EEPGQRRRQK RQEQERELAE GEEQSEKQER LEQRDRQRRD EELWRQRQEW
QEREERRAEE EQLQSCKGHE TEEFPDEEQL RRRELLELRR KGREEKQQQR RERQDRVFQE
EEEKEWRKRE TVLRKEEEKL QEEEPQRQRE LQEEEEQLRK LERQELRRER QEEEQQQQRL
RREQQLRRKQ EEERREQQEE RREQQERREQ QEERREQQLR REQEERREQQ LRREQEEERR
EQQLRREQEE ERREQQLRRE QQLRREQQLR REQQLRREQQ LRREQQLRRE QQLRREQQLR
REQQLRREQE EERHEQKHEQ ERREQRLKRE QEERRDWLKR EEETERHEQE RRKQQLKRDQ
EEERRERWLK LEEEERREQQ ERREQQLRRE QEERREQRLK RQEEEERLQQ RLRSEQQLRR
EQEERREQLL KREEEKRLEQ ERREQRLKRE QEERRDQLLK REEERRQQRL KREQEERLEQ
RLKREEVERL EQEERREQRL KREEPEEERR QQLLKSEEQE ERRQQQLRRE QQERREQRLK
REEEEERLEQ RLKREHEEER REQELAEEEQ EQARERIKSR IPKWQWQLES EADARQSKVY
SRPRKQEGQR RRQEQEEKRR RRESELQWQE EERAHRQQQE EEQRRDFTWQ WQAEEKSERG
RQRLSARPPL REQRERQLRA EERQQREQRF LPEEEEKEQR RRQRREREKE LQFLEEEEQL
QRRERAQQLQ EEEDGLQEDQ ERRRSQEQRR DQKWRWQLEE ERKRRRHTLY AKPALQEQLR
KEQQLLQEEE EELQREEREK RRRQEQERQY REEEQLQQEE EQLLREEREK RRRQERERQY
RKDKKLQQKE EQLLGEEPEK RRRQEREKKY REEEELQQEE EQLLREEREK RRRQEWERQY
RKKDELQQEE EQLLREEREK RRLQERERQY REEEELQQEE EQLLGEERET RRRQELERQY
RKEEELQQEE EQLLREEPEK RRRQERERQC REEEELQQEE EQLLREEREK RRRQELERQY
REEEEVQQEE EQLLREEPEK RRRQELERQY REEEELQQEE EQLLREEQEK RRQERERQYR
EEEELQRQKR KQRYRDEDQR SDLKWQWEPE KENAVRDNKV YCKGRENEQF RQLEDSQLRD
RQSQQDLQHL LGEQQERDRE QERRRWQQRD RHFPEEEQLE REEQKEAKRR DRKSQEEKQL
LREEREEKRR RQETDRKFRE EEQLLQEREE QPLRRQERDR KFREEELRHQ EQGRKFLEEE
QRLRRQERER KFLKEEQQLR CQEREQQLRQ DRDRKFREEE QQLSRQERDR KFREEEQQVR
RQERERKFLE EEQQLRQERH RKFREEEQLL QEREEQQLHR QERDRKFLEE EQQLRRQERD
RKFREQELRS QEPERKFLEE EQQLHRQQRQ RKFLQEEQQL RRQERGQQRR QDRDRKFREE
EQLRQEREEQ QLSRQERDRK FRLEEQKVRR QEQERKFMED EQQLRRQEGQ QQLRQERDRK
FREDEQLLQE REEQQLHRQE RDRKFLEEEP QLRRQEREQQ LRHDRDRKFR EEEQLLQEGE
EQQLRRQERD RKFREEEQQL RRQERERKFL QEEQQLRRQE LERKFREEEQ LRQETEQEQL
RRQERYRKIL EEEQLRPERE EQQLRRQERD RKFREEEQLR QEREEQQLRS QESDRKFREE
EQLRQEREEQ QLRPQQRDGK YRWEEEQLQL EEQEQRLRQE RDRQYRAEEQ FATQEKSRRE
EQELWQEEEQ KRRQERERKL REEHIRRQQK EEQRHRQVGE IKSQEGKGHG RLLEPGTHQF
ASVPVRSSPL YEYIQEQRSQ YRP
