PR38B_HUMAN
ID PR38B_HUMAN Reviewed; 546 AA.
AC Q5VTL8; Q05DD6; Q32Q58; Q5VTL9; Q6PK39; Q7Z6E2; Q86WF3; Q8IWG9; Q9NW40;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Pre-mRNA-splicing factor 38B;
DE AltName: Full=Sarcoma antigen NY-SAR-27;
GN Name=PRPF38B;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Muscle, Skin, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 402-546 (ISOFORM 1).
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527 AND SER-529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-529 AND SER-534, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-527; SER-529 AND
RP SER-534, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-473; SER-475;
RP SER-481; SER-527 AND SER-529, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-290; SER-318;
RP SER-320; SER-527 AND SER-529, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: May be required for pre-mRNA splicing. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VTL8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VTL8-2; Sequence=VSP_025408, VSP_025409;
CC -!- SIMILARITY: Belongs to the PRP38 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO65168.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK001192; BAA91546.1; -; mRNA.
DR EMBL; AL160171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007757; AAH07757.1; ALT_TERM; mRNA.
DR EMBL; BC016296; AAH16296.1; ALT_TERM; mRNA.
DR EMBL; BC024275; AAH24275.1; ALT_TERM; mRNA.
DR EMBL; BC040127; AAH40127.1; ALT_TERM; mRNA.
DR EMBL; BC053838; AAH53838.1; -; mRNA.
DR EMBL; BC107801; AAI07802.1; ALT_TERM; mRNA.
DR EMBL; BC130346; AAI30347.1; -; mRNA.
DR EMBL; BC132963; AAI32964.1; -; mRNA.
DR EMBL; AY211915; AAO65168.1; ALT_INIT; mRNA.
DR CCDS; CCDS788.1; -. [Q5VTL8-1]
DR RefSeq; NP_060531.2; NM_018061.2. [Q5VTL8-1]
DR AlphaFoldDB; Q5VTL8; -.
DR SMR; Q5VTL8; -.
DR BioGRID; 120428; 96.
DR IntAct; Q5VTL8; 19.
DR MINT; Q5VTL8; -.
DR STRING; 9606.ENSP00000359042; -.
DR GlyGen; Q5VTL8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VTL8; -.
DR PhosphoSitePlus; Q5VTL8; -.
DR SwissPalm; Q5VTL8; -.
DR BioMuta; PRPF38B; -.
DR DMDM; 74746965; -.
DR EPD; Q5VTL8; -.
DR jPOST; Q5VTL8; -.
DR MassIVE; Q5VTL8; -.
DR MaxQB; Q5VTL8; -.
DR PaxDb; Q5VTL8; -.
DR PeptideAtlas; Q5VTL8; -.
DR PRIDE; Q5VTL8; -.
DR ProteomicsDB; 65335; -. [Q5VTL8-1]
DR ProteomicsDB; 65336; -. [Q5VTL8-2]
DR Antibodypedia; 53741; 27 antibodies from 15 providers.
DR DNASU; 55119; -.
DR Ensembl; ENST00000370022.9; ENSP00000359039.5; ENSG00000134186.12. [Q5VTL8-2]
DR Ensembl; ENST00000370025.9; ENSP00000359042.4; ENSG00000134186.12. [Q5VTL8-1]
DR GeneID; 55119; -.
DR KEGG; hsa:55119; -.
DR MANE-Select; ENST00000370025.9; ENSP00000359042.4; NM_018061.4; NP_060531.2.
DR UCSC; uc001dvv.5; human. [Q5VTL8-1]
DR CTD; 55119; -.
DR DisGeNET; 55119; -.
DR GeneCards; PRPF38B; -.
DR HGNC; HGNC:25512; PRPF38B.
DR HPA; ENSG00000134186; Low tissue specificity.
DR neXtProt; NX_Q5VTL8; -.
DR OpenTargets; ENSG00000134186; -.
DR PharmGKB; PA142671126; -.
DR VEuPathDB; HostDB:ENSG00000134186; -.
DR eggNOG; KOG2888; Eukaryota.
DR GeneTree; ENSGT01030000234749; -.
DR HOGENOM; CLU_034151_1_2_1; -.
DR InParanoid; Q5VTL8; -.
DR OMA; ERSHKHD; -.
DR OrthoDB; 1488857at2759; -.
DR PhylomeDB; Q5VTL8; -.
DR TreeFam; TF313626; -.
DR PathwayCommons; Q5VTL8; -.
DR SignaLink; Q5VTL8; -.
DR BioGRID-ORCS; 55119; 801 hits in 1092 CRISPR screens.
DR ChiTaRS; PRPF38B; human.
DR GenomeRNAi; 55119; -.
DR Pharos; Q5VTL8; Tdark.
DR PRO; PR:Q5VTL8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5VTL8; protein.
DR Bgee; ENSG00000134186; Expressed in trabecular bone tissue and 188 other tissues.
DR ExpressionAtlas; Q5VTL8; baseline and differential.
DR Genevisible; Q5VTL8; HS.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR005037; PRP38.
DR PANTHER; PTHR23142; PTHR23142; 1.
DR Pfam; PF03371; PRP38; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..546
FT /note="Pre-mRNA-splicing factor 38B"
FT /id="PRO_0000287235"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 292..321
FT /evidence="ECO:0000255"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..282
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..454
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..506
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AXY7"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 187..190
FT /note="DLDV -> FFTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025408"
FT VAR_SEQ 191..546
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025409"
FT CONFLICT 52
FT /note="N -> S (in Ref. 1; BAA91546)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..295
FT /note="EL -> DR (in Ref. 3; AAH40127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 64468 MW; A3082DCF491F88F8 CRC64;
MANNSPALTG NSQPQHQAAA AAAQQQQQCG GGGATKPAVS GKQGNVLPLW GNEKTMNLNP
MILTNILSSP YFKVQLYELK TYHEVVDEIY FKVTHVEPWE KGSRKTAGQT GMCGGVRGVG
TGGIVSTAFC LLYKLFTLKL TRKQVMGLIT HTDSPYIRAL GFMYIRYTQP PTDLWDWFES
FLDDEEDLDV KAGGGCVMTI GEMLRSFLTK LEWFSTLFPR IPVPVQKNID QQIKTRPRKI
KKDGKEGAEE IDRHVERRRS RSPRRSLSPR RSPRRSRSRS HHREGHGSSS FDRELEREKE
RQRLEREAKE REKERRRSRS IDRGLERRRS RSRERHRSRS RSRDRKGDRR DRDREREKEN
ERGRRRDRDY DKERGNEREK ERERSRERSK EQRSRGEVEE KKHKEDKDDR RHRDDKRDSK
KEKKHSRSRS RERKHRSRSR SRNAGKRSRS RSKEKSSKHK NESKEKSNKR SRSGSQGRTD
SVEKSKKREH SPSKEKSRKR SRSKERSHKR DHSDSKDQSD KHDRRRSQSI EQESQEKQHK
NKDETV
