CWC2_YEAST
ID CWC2_YEAST Reviewed; 339 AA.
AC Q12046; D6VRE5;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Pre-mRNA-splicing factor CWC2;
DE AltName: Full=Complexed with CEF1 protein 2;
DE AltName: Full=PRP19-associated complex protein 40;
DE AltName: Full=Synthetic lethal with CLF1 protein 3;
GN Name=CWC2; Synonyms=NTC40, SLC3; OrderedLocusNames=YDL209C; ORFNames=D1041;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9046097;
RX DOI=10.1002/(sici)1097-0061(199702)13:2<163::aid-yea54>3.0.co;2-4;
RA Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
RA Schmidt E.R.;
RT "The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new
RT open reading frames, nine known genes and one gene for Gly-tRNA.";
RL Yeast 13:163-169(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP INTERACTION WITH PRP19.
RX PubMed=9528791; DOI=10.1128/mcb.18.4.2196;
RA Chen H.-R., Jan S.-P., Tsao T.Y., Sheu Y.-J., Banroques J., Cheng S.-C.;
RT "Snt309p, a component of the Prp19p-associated complex that interacts with
RT Prp19p and associates with the spliceosome simultaneously with or
RT immediately after dissociation of U4 in the same manner as Prp19p.";
RL Mol. Cell. Biol. 18:2196-2204(1998).
RN [6]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [7]
RP INTERACTION WITH PRP19 AND ISY1.
RX PubMed=12088152; DOI=10.1017/s1355838202025050;
RA Ohi M.D., Gould K.L.;
RT "Characterization of interactions among the Cef1p-Prp19p-associated
RT splicing complex.";
RL RNA 8:798-815(2002).
RN [8]
RP MUTAGENESIS OF GLY-79.
RX PubMed=12871902; DOI=10.1093/genetics/164.3.895;
RA Vincent K., Wang Q., Jay S., Hobbs K., Rymond B.C.;
RT "Genetic interactions with CLF1 identify additional pre-mRNA splicing
RT factors and a link between activators of yeast vesicular transport and
RT splicing.";
RL Genetics 164:895-907(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PRP19.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP FUNCTION, MUTAGENESIS OF CYS-73; CYS-87 AND PHE-186, AND RNA-BINDING.
RX PubMed=19435883; DOI=10.1093/nar/gkp341;
RA McGrail J.C., Krause A., O'Keefe R.T.;
RT "The RNA binding protein Cwc2 interacts directly with the U6 snRNA to link
RT the nineteen complex to the spliceosome during pre-mRNA splicing.";
RL Nucleic Acids Res. 37:4205-4217(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-336, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
RP FUNCTION, RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22246180; DOI=10.1038/emboj.2011.502;
RA Rasche N., Dybkov O., Schmitzova J., Akyildiz B., Fabrizio P., Luhrmann R.;
RT "Cwc2 and its human homologue RBM22 promote an active conformation of the
RT spliceosome catalytic centre.";
RL EMBO J. 31:1591-1604(2012).
CC -!- FUNCTION: Involved in the first step of pre-mRNA splicing. Required for
CC cell growth and cell cycle control. Plays a role in the levels of the
CC U1, U4, U5 and U6 snRNAs and the maintenance of the U4/U6 snRNA
CC complex. May provide the link between the 'nineteen complex' NTC
CC spliceosome protein complex and the spliceosome through the U6 snRNA.
CC Associates predominantly with U6 snRNAs in assembled active
CC spliceosomes. Binds directly to the internal stem-loop (ISL) domain of
CC the U6 snRNA and to the pre-mRNA intron near the 5' splice site during
CC the activation and catalytic phases of the spliceosome cycle. Binds
CC also to U1, U4, U5 and U6 snRNAs and to pre-mRNAs, in vitro. Is not
CC required for the Prp2-mediated remodeling of the activated spliceosome.
CC {ECO:0000269|PubMed:19435883, ECO:0000269|PubMed:22246180}.
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and at
CC least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21,
CC CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1,
CC MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46,
CC SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1,
CC SYF2, RSE1 and YJU2. Interacts with ISY1. Interacts with PRP19.
CC {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152,
CC ECO:0000269|PubMed:14690591, ECO:0000269|PubMed:9528791}.
CC -!- INTERACTION:
CC Q12046; P32523: PRP19; NbExp=13; IntAct=EBI-553, EBI-493;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The C-terminal RRM domain and the zinc finger motif are
CC necessary for RNA-binding.
CC -!- MISCELLANEOUS: Present with 2650 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRM CWC2 family. {ECO:0000305}.
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DR EMBL; X99000; CAA67482.1; -; Genomic_DNA.
DR EMBL; Z74257; CAA98787.1; -; Genomic_DNA.
DR EMBL; AY693022; AAT93041.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11655.1; -; Genomic_DNA.
DR PIR; S67768; S67768.
DR RefSeq; NP_010072.1; NM_001180269.1.
DR PDB; 3TP2; X-ray; 2.40 A; A/B=1-227.
DR PDB; 3U1L; X-ray; 1.64 A; A=1-240.
DR PDB; 3U1M; X-ray; 1.95 A; A=1-240.
DR PDB; 5GM6; EM; 3.50 A; R=1-339.
DR PDB; 5GMK; EM; 3.40 A; R=1-339.
DR PDB; 5LJ3; EM; 3.80 A; M=1-339.
DR PDB; 5LJ5; EM; 3.80 A; M=1-339.
DR PDB; 5LQW; EM; 5.80 A; F=1-339.
DR PDB; 5MPS; EM; 3.85 A; M=1-339.
DR PDB; 5MQ0; EM; 4.17 A; M=1-339.
DR PDB; 5WSG; EM; 4.00 A; R=1-339.
DR PDB; 5Y88; EM; 3.70 A; N=1-339.
DR PDB; 5YLZ; EM; 3.60 A; N=1-339.
DR PDB; 6BK8; EM; 3.30 A; G=1-339.
DR PDB; 6EXN; EM; 3.70 A; M=1-339.
DR PDB; 6J6G; EM; 3.20 A; R=1-339.
DR PDB; 6J6H; EM; 3.60 A; R=1-339.
DR PDB; 6J6N; EM; 3.86 A; R=1-339.
DR PDB; 6J6Q; EM; 3.70 A; R=1-339.
DR PDBsum; 3TP2; -.
DR PDBsum; 3U1L; -.
DR PDBsum; 3U1M; -.
DR PDBsum; 5GM6; -.
DR PDBsum; 5GMK; -.
DR PDBsum; 5LJ3; -.
DR PDBsum; 5LJ5; -.
DR PDBsum; 5LQW; -.
DR PDBsum; 5MPS; -.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5WSG; -.
DR PDBsum; 5Y88; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR PDBsum; 6J6G; -.
DR PDBsum; 6J6H; -.
DR PDBsum; 6J6N; -.
DR PDBsum; 6J6Q; -.
DR AlphaFoldDB; Q12046; -.
DR SMR; Q12046; -.
DR BioGRID; 31837; 114.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-5164N; -.
DR IntAct; Q12046; 51.
DR STRING; 4932.YDL209C; -.
DR iPTMnet; Q12046; -.
DR MaxQB; Q12046; -.
DR PaxDb; Q12046; -.
DR PRIDE; Q12046; -.
DR EnsemblFungi; YDL209C_mRNA; YDL209C; YDL209C.
DR GeneID; 851318; -.
DR KEGG; sce:YDL209C; -.
DR SGD; S000002368; CWC2.
DR VEuPathDB; FungiDB:YDL209C; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00390000002792; -.
DR HOGENOM; CLU_043308_0_0_1; -.
DR InParanoid; Q12046; -.
DR OMA; WYNKWSQ; -.
DR BioCyc; YEAST:G3O-29591-MON; -.
DR PRO; PR:Q12046; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12046; protein.
DR GO; GO:0000974; C:Prp19 complex; IPI:SGD.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR CDD; cd12360; RRM_cwf2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039173; Cwc2.
DR InterPro; IPR039171; Cwc2/Slt11.
DR InterPro; IPR034181; Cwc2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR032297; Torus.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14089; PTHR14089; 1.
DR PANTHER; PTHR14089:SF2; PTHR14089:SF2; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF16131; Torus; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Metal-binding; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Zinc; Zinc-finger.
FT CHAIN 1..339
FT /note="Pre-mRNA-splicing factor CWC2"
FT /id="PRO_0000081552"
FT DOMAIN 135..228
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 67..94
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 313..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 73
FT /note="C->Y: Inhibits cell growth."
FT /evidence="ECO:0000269|PubMed:19435883"
FT MUTAGEN 79
FT /note="G->D: No effect. Synthetic lethal when associated
FT with CLF1 lacking a TPR domain."
FT /evidence="ECO:0000269|PubMed:12871902"
FT MUTAGEN 87
FT /note="C->H: Inhibits cell growth."
FT /evidence="ECO:0000269|PubMed:19435883"
FT MUTAGEN 186
FT /note="F->D: Inhibits cell growth."
FT /evidence="ECO:0000269|PubMed:19435883"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:3TP2"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3TP2"
FT HELIX 129..133
FT /evidence="ECO:0007829|PDB:3TP2"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5GMK"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:3U1L"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:3U1L"
FT HELIX 232..260
FT /evidence="ECO:0007829|PDB:6J6G"
SQ SEQUENCE 339 AA; 38431 MW; 371734A11DFDB339 CRC64;
MTSWRDKSAK VQVKESELPS SIPAQTGLTF NIWYNKWSQG FAGNTRFVSP FALQPQLHSG
KTRGDNDGQL FFCLFFAKGM CCLGPKCEYL HHIPDEEDIG KLALRTEVLD CFGREKFADY
REDMGGIGSF RKKNKTLYVG GIDGALNSKH LKPAQIESRI RFVFSRLGDI DRIRYVESKN
CGFVKFKYQA NAEFAKEAMS NQTLLLPSDK EWDDRREGTG LLVKWANEDP DPAAQKRLQE
ELKLESLNMM VHLINNNTNS AGTEVNNKNN ERLDRTFPEA SVDNVKKRLL PLDNGMESDD
FIEKLKKVKK NISRENISSK PSVGKLGGPL LDYLSSDED
