ID NSRP1_HUMAN Reviewed; 558 AA. AC Q9H0G5; Q6FI71; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 03-MAY-2023, entry version 155. DE RecName: Full=Nuclear speckle splicing regulatory protein 1; DE AltName: Full=Coiled-coil domain-containing protein 55; DE AltName: Full=Nuclear speckle-related protein 70; DE Short=NSrp70; GN Name=NSRP1; Synonyms=CCDC55, NSRP70; 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]. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, AND 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-275, AND IDENTIFICATION BY RP 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-248; SER-254 AND RP SER-255, AND 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 IDENTIFICATION BY MASS SPECTROMETRY [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-254 AND SER-255, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, AND RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION, INTERACTION WITH SRSF1 AND SRSF2, RNA-BINDING, MUTAGENESIS OF RP 536-ARG-ASP-537, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=21296756; DOI=10.1093/nar/gkq1267; RA Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.; RT "NSrp70 is a novel nuclear speckle-related protein that modulates RT alternative pre-mRNA splicing in vivo."; RL Nucleic Acids Res. 39:4300-4314(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-33; SER-248; SER-254 RP AND SER-255, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-248 AND THR-275, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-210, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-281, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [18] RP VARIANT NEDSSBA 18-GLN--ASP-558 DEL, AND INVOLVEMENT IN NEDSSBA. RX PubMed=34385670; DOI=10.1038/s41436-021-01291-x; RA Calame D.G., Bakhtiari S., Logan R., Coban-Akdemir Z., Du H., Mitani T., RA Fatih J.M., Hunter J.V., Herman I., Pehlivan D., Jhangiani S.N., Person R., RA Schnur R.E., Jin S.C., Bilguvar K., Posey J.E., Koh S., Firouzabadi S.G., RA Alehabib E., Tafakhori A., Esmkhani S., Gibbs R.A., Noureldeen M.M., RA Zaki M.S., Marafi D., Darvish H., Kruer M.C., Lupski J.R.; RT "Biallelic loss-of-function variants in the splicing regulator NSRP1 cause RT a severe neurodevelopmental disorder with spastic cerebral palsy and RT epilepsy."; RL Genet. Med. 23:2455-2460(2021). CC -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative CC splicing regulation. {ECO:0000269|PubMed:21296756}. CC -!- SUBUNIT: Interacts (via C-terminus) with SRSF1. Interacts (via C- CC terminus) with SRSF2. {ECO:0000269|PubMed:21296756}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21296756}. Nucleus CC speckle {ECO:0000269|PubMed:21296756}. Note=Colocalizes with splicing CC factors SRSF1 and SRSF2 in speckles. CC -!- TISSUE SPECIFICITY: Expressed in dendritic cells, T-cells, B-cells and CC natural killer cells. Expressed in secondary lymphoid organs such as CC spleen and mesenteric, axillary and brachial lymph nodes. CC {ECO:0000269|PubMed:21296756}. CC -!- INDUCTION: Up-regulated in motile T-cells. CC {ECO:0000269|PubMed:21296756}. CC -!- DISEASE: Neurodevelopmental disorder with spasticity, seizures, and CC brain abnormalities (NEDSSBA) [MIM:620001]: An autosomal recessive CC disorder characterized by developmental delay apparent in infancy, CC impaired intellectual development with poor or absent speech, epilepsy, CC variable microcephaly, hypotonia, and spastic cerebral palsy. Brain CC abnormalities include simplified gyral pattern, defects of the CC operculum, and vermian hypoplasia. Death in early childhood may occur. CC {ECO:0000269|PubMed:34385670}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the NSRP1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL136806; CAB66740.1; -; mRNA. DR EMBL; CR533555; CAG38586.1; -; mRNA. DR EMBL; AC104984; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC040118; AAH40118.1; -; mRNA. DR EMBL; BC105044; AAI05045.1; -; mRNA. DR EMBL; BC105046; AAI05047.1; -; mRNA. DR CCDS; CCDS11255.1; -. DR RefSeq; NP_001248396.1; NM_001261467.1. DR RefSeq; NP_115517.1; NM_032141.3. DR AlphaFoldDB; Q9H0G5; -. DR SMR; Q9H0G5; -. DR BioGRID; 123876; 194. DR IntAct; Q9H0G5; 22. DR MINT; Q9H0G5; -. DR STRING; 9606.ENSP00000247026; -. DR GlyGen; Q9H0G5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H0G5; -. DR PhosphoSitePlus; Q9H0G5; -. DR BioMuta; NSRP1; -. DR DMDM; 74733524; -. DR EPD; Q9H0G5; -. DR jPOST; Q9H0G5; -. DR MassIVE; Q9H0G5; -. DR MaxQB; Q9H0G5; -. DR PaxDb; Q9H0G5; -. DR PeptideAtlas; Q9H0G5; -. DR ProteomicsDB; 80276; -. DR Antibodypedia; 2855; 112 antibodies from 24 providers. DR DNASU; 84081; -. DR Ensembl; ENST00000247026.10; ENSP00000247026.5; ENSG00000126653.18. DR GeneID; 84081; -. DR KEGG; hsa:84081; -. DR MANE-Select; ENST00000247026.10; ENSP00000247026.5; NM_032141.4; NP_115517.1. DR UCSC; uc002heu.5; human. DR AGR; HGNC:25305; -. DR CTD; 84081; -. DR DisGeNET; 84081; -. DR GeneCards; NSRP1; -. DR HGNC; HGNC:25305; NSRP1. DR HPA; ENSG00000126653; Low tissue specificity. DR MalaCards; NSRP1; -. DR MIM; 616173; gene. DR MIM; 620001; phenotype. DR neXtProt; NX_Q9H0G5; -. DR OpenTargets; ENSG00000126653; -. DR PharmGKB; PA142672171; -. DR VEuPathDB; HostDB:ENSG00000126653; -. DR eggNOG; KOG2117; Eukaryota. DR GeneTree; ENSGT00940000154049; -. DR HOGENOM; CLU_548527_0_0_1; -. DR InParanoid; Q9H0G5; -. DR OMA; RYGLIMP; -. DR OrthoDB; 1387859at2759; -. DR PhylomeDB; Q9H0G5; -. DR TreeFam; TF319359; -. DR PathwayCommons; Q9H0G5; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q9H0G5; -. DR BioGRID-ORCS; 84081; 138 hits in 1156 CRISPR screens. DR ChiTaRS; NSRP1; human. DR GeneWiki; CCDC55_(gene); -. DR GenomeRNAi; 84081; -. DR Pharos; Q9H0G5; Tbio. DR PRO; PR:Q9H0G5; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9H0G5; protein. DR Bgee; ENSG00000126653; Expressed in sural nerve and 185 other tissues. DR ExpressionAtlas; Q9H0G5; baseline and differential. DR Genevisible; Q9H0G5; HS. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0032502; P:developmental process; IMP:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR InterPro; IPR046850; NRP1_C. DR InterPro; IPR042816; Nsrp1. DR InterPro; IPR018612; NSRP1_N. DR PANTHER; PTHR31938; NUCLEAR SPECKLE SPLICING REGULATORY PROTEIN 1; 1. DR PANTHER; PTHR31938:SF4; NUCLEAR SPECKLE SPLICING REGULATORY PROTEIN 1; 1. DR Pfam; PF20427; NRP1_C; 1. DR Pfam; PF09745; NSRP1_N; 1. PE 1: Evidence at protein level; KW Coiled coil; Disease variant; Epilepsy; Intellectual disability; KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; RNA-binding; Ubl conjugation. FT CHAIN 1..558 FT /note="Nuclear speckle splicing regulatory protein 1" FT /id="PRO_0000240434" FT REGION 21..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 106..170 FT /note="Necessary for alternative splicing activity" FT REGION 204..534 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 104..170 FT /evidence="ECO:0000255" FT COILED 379..427 FT /evidence="ECO:0000255" FT COMPBIAS 40..54 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 204..219 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 235..301 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..489 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 498..534 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 27 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 248 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 254 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 255 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 275 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:23186163" FT MOD_RES 457 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q4FZU3" FT CROSSLNK 199 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 210 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447" FT CROSSLNK 281 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 18..558 FT /note="Missing (in NEDSSBA)" FT /evidence="ECO:0000269|PubMed:34385670" FT /id="VAR_087656" FT VARIANT 86 FT /note="K -> T (in dbSNP:rs11544945)" FT /id="VAR_054104" FT MUTAGEN 536..537 FT /note="RD->AA: Inhibits nuclear localization and FT alternative splicing activity." FT /evidence="ECO:0000269|PubMed:21296756" FT CONFLICT 270 FT /note="E -> G (in Ref. 1; CAG38586)" FT /evidence="ECO:0000305" SQ SEQUENCE 558 AA; 66390 MW; 99B7BDBCFD06F98D CRC64; MAIPGRQYGL ILPKKTQQLH PVLQKPSVFG NDSDDDDETS VSESLQREAA KKQAMKQTKL EIQKALAEDA TVYEYDSIYD EMQKKKEENN PKLLLGKDRK PKYIHNLLKA VEIRKKEQEK RMEKKIQRER EMEKGEFDDK EAFVTSAYKK KLQERAEEEE REKRAAALEA CLDVTKQKDL SGFYRHLLNQ AVGEEEVPKC SFREARSGIK EEKSRGFSNE VSSKNRIPQE KCILQTDVKV EENPDADSDF DAKSSADDEI EETRVNCRRE KVIETPENDF KHHRSQNHSR SPSEERGHST RHHTKGSRTS RGHEKREDQH QQKQSRDQEN HYTDRDYRKE RDSHRHREAS HRDSHWKRHE QEDKPRARDQ RERSDRVWKR EKDREKYSQR EQERDRQQND QNRPSEKGEK EEKSKAKEEH MKVRKERYEN NDKYRDREKR EVGVQSSERN QDRKESSPNS RAKDKFLDQE RSNKMRNMAK DKERNQEKPS NSESSLGAKH RLTEEGQEKG KEQERPPEAV SKFAKRNNEE TVMSARDRYL ARQMARVNAK TYIEKEDD //