KCS1_YEAST
ID KCS1_YEAST Reviewed; 1050 AA.
AC Q12494; D6VS03; P89899; Q7LGR2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Inositol hexakisphosphate kinase 1;
DE Short=InsP6 kinase 1;
DE EC=2.7.4.21;
DE AltName: Full=InsP6 kinase KCS1;
DE AltName: Full=PKC1 suppressor protein 1;
GN Name=KCS1; OrderedLocusNames=YDR017C; ORFNames=PZF1050;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=8601473; DOI=10.1093/genetics/141.4.1275;
RA Huang K.N., Symington L.S.;
RT "Suppressors of a Saccharomyces cerevisiae pkc1 mutation identify alleles
RT of the phosphatase gene PTC1 and of a novel gene encoding a putative basic
RT leucine zipper protein.";
RL Genetics 141:1275-1285(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896275;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1085::aid-yea9>3.3.co;2-s;
RA Eide L.G., Sander C., Prydz H.;
RT "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome
RT IV from Saccharomyces cerevisiae reveal 23 open reading frames.";
RL Yeast 12:1085-1090(1996).
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 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 [5]
RP FUNCTION.
RX PubMed=10574768; DOI=10.1016/s0960-9822(00)80055-x;
RA Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H.;
RT "Synthesis of diphosphoinositol pentakisphosphate by a newly identified
RT family of higher inositol polyphosphate kinases.";
RL Curr. Biol. 9:1323-1326(1999).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10827188; DOI=10.1074/jbc.m002750200;
RA Saiardi A., Caffrey J.J., Snyder S.H., Shears S.B.;
RT "The inositol hexakisphosphate kinase family. Catalytic flexibility and
RT function in yeast vacuole biogenesis.";
RL J. Biol. Chem. 275:24686-24692(2000).
RN [7]
RP FUNCTION.
RX PubMed=11956213; DOI=10.1074/jbc.m202206200;
RA Dubois E., Scherens B., Vierendeels F., Ho M.M.W., Messenguy F.,
RA Shears S.B.;
RT "In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of
RT Kcs1p is required for resistance to salt stress, cell wall integrity, and
RT vacuolar morphogenesis.";
RL J. Biol. Chem. 277:23755-23763(2002).
RN [8]
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 [9]
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 [10]
RP FUNCTION.
RX PubMed=15561716; DOI=10.1074/jbc.m412070200;
RA York S.J., Armbruster B.N., Greenwell P., Petes T.D., York J.D.;
RT "Inositol diphosphate signaling regulates telomere length.";
RL J. Biol. Chem. 280:4264-4269(2005).
RN [11]
RP FUNCTION.
RX PubMed=15866881; DOI=10.1074/jbc.m414579200;
RA Auesukaree C., Tochio H., Shirakawa M., Kaneko Y., Harashima S.;
RT "Plc1p, Arg82p, and Kcs1p, enzymes involved in inositol pyrophosphate
RT synthesis, are essential for phosphate regulation and polyphosphate
RT accumulation in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:25127-25133(2005).
RN [12]
RP FUNCTION.
RX PubMed=15944147; DOI=10.1074/jbc.m505089200;
RA Seeds A.M., Bastidas R.J., York J.D.;
RT "Molecular definition of a novel inositol polyphosphate metabolic pathway
RT initiated by inositol 1,4,5-trisphosphate 3-kinase activity in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:27654-27661(2005).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537; SER-566 AND SER-589, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-396; SER-583 AND
RP SER-670, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-396; SER-469;
RP SER-537; SER-539; SER-646; SER-664 AND SER-670, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Converts inositol hexakisphosphate (InsP6) to
CC diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Involved in
CC phosphate regulation and polyphosphate accumulation. Required for
CC resistance to salt stress, cell wall integrity, vacuole morphogenesis,
CC and telomere maintenance. {ECO:0000269|PubMed:10574768,
CC ECO:0000269|PubMed:10827188, ECO:0000269|PubMed:11956213,
CC ECO:0000269|PubMed:15561716, ECO:0000269|PubMed:15866881,
CC ECO:0000269|PubMed:15944147, ECO:0000269|PubMed:8601473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol hexakisphosphate + ATP = 5-diphospho-1D-myo-
CC inositol 1,2,3,4,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:12793,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628,
CC ChEBI:CHEBI:456216; EC=2.7.4.21;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-diphospho-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP +
CC H(+) = 1,5-bis(diphospho)-1D-myo-inositol 2,3,4,6-tetrakisphosphate +
CC ADP; Xref=Rhea:RHEA:37467, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:74946, ChEBI:CHEBI:77983, ChEBI:CHEBI:456216;
CC EC=2.7.4.21;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 uM for InsP6 {ECO:0000269|PubMed:10827188};
CC KM=1.2 uM for InsP5 {ECO:0000269|PubMed:10827188};
CC Vmax=2 umol/min/mg enzyme {ECO:0000269|PubMed:10827188};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {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; S81651; AAB36234.1; -; Genomic_DNA.
DR EMBL; X95966; CAA65208.1; -; Genomic_DNA.
DR EMBL; Z49770; CAA89842.1; -; Genomic_DNA.
DR EMBL; Z74313; CAA98837.1; -; Genomic_DNA.
DR EMBL; Z74314; CAA98839.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11863.1; -; Genomic_DNA.
DR PIR; S54640; S54640.
DR RefSeq; NP_010300.3; NM_001180325.3.
DR AlphaFoldDB; Q12494; -.
DR SMR; Q12494; -.
DR BioGRID; 32067; 289.
DR DIP; DIP-1402N; -.
DR IntAct; Q12494; 6.
DR MINT; Q12494; -.
DR STRING; 4932.YDR017C; -.
DR iPTMnet; Q12494; -.
DR MaxQB; Q12494; -.
DR PaxDb; Q12494; -.
DR PRIDE; Q12494; -.
DR EnsemblFungi; YDR017C_mRNA; YDR017C; YDR017C.
DR GeneID; 851580; -.
DR KEGG; sce:YDR017C; -.
DR SGD; S000002424; KCS1.
DR VEuPathDB; FungiDB:YDR017C; -.
DR eggNOG; KOG1620; Eukaryota.
DR HOGENOM; CLU_004422_0_0_1; -.
DR InParanoid; Q12494; -.
DR OMA; HARGHIT; -.
DR BioCyc; YEAST:G3O-29635-MON; -.
DR BRENDA; 2.7.4.21; 984.
DR Reactome; R-SCE-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-SCE-1855191; Synthesis of IPs in the nucleus.
DR SABIO-RK; Q12494; -.
DR PRO; PR:Q12494; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12494; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IDA:SGD.
DR GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IDA:SGD.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010919; P:regulation of inositol phosphate biosynthetic process; IMP:SGD.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 1.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1050
FT /note="Inositol hexakisphosphate kinase 1"
FT /id="PRO_0000255955"
FT REGION 87..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 772..780
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1050 AA; 119550 MW; 9C7507CA5F4B0FC7 CRC64;
MDTSHEIHDK IPDTLREQQQ HLRQKESEGC ITTLKDLNVP ETKKLSSVLH GRKASTYLRI
FRDDECLADN NNGVDSNNGG SVTCADKITR SEATPKSVPE GLQVSEKKNN PDTLSSSLSS
FILSNHEEPA IKPNKHVAHR NNITETGQGS GEDIAKQQSH QPQVLHHQTS LKPIQNVDEG
CISPKSTYQE SLHGISEDLT LKPVSSATYY PHKSKADSGY EEKDKMENDI DTIQPATINC
ASGIATLPSS YNRHTFKVKT YSTLSQSLRQ ENVNNRSNEK KPQQFVPHSE SIKEKPNTFE
QDKEGEQADE EEDEGDNEHR EYPLAVELKP FTNRVGGHTA IFRFSKRAVC KALVNRENRW
YENIELCHKE LLQFMPRYIG VLNVRQHFQS KDDFLSDLDQ ENNGKNDTSN ENKDIEVNHN
NNDDIALNTE PTGTPLTHIH SFPLEHSSRQ VLEKEHPEIE SVHPHVKRSL SSSNQPSLLP
EVVLNDNRHI IPESLWYKYS DSPNSAPNDS YFSSSSSHNS CSFGERGNTN KLKRRDSGST
MINTELKNLV IREVFAPKCF RRKRNSNTTT MGNHNARLGS SPSFLTQKSR ASSHDASNTS
MKTLGDSSSQ ASLQMDDSKV NPNLQDPFLK KSLHEKISNA LDGSHSVMDL KQFHKNEQIK
HKNSFCNSLS PILTATNSRD DGEFATSPNY ISNAQDGVFD MDEDTGNETI NMDNHGCHLD
SGKNMIIKSL AYNVSNDYSH HDIESITFEE TSHTIVSKFI LLEDLTRNMN KPCALDLKMG
TRQYGVDAKR AKQLSQRAKC LKTTSRRLGV RICGLKVWNK DYYITRDKYF GRRVKVGWQF
ARVLARFLYD GKTIESLIRQ IPRLIKQLDT LYSEIFNLKG YRLYGASLLL MYDGDANKSN
SKRKKAANVK VNLIDFARCV TKEDAMECMD KFRIPPKSPN IEDKGFLRGV KSLRFYLLLI
WNYLTSDMPL IFDEVEMNDM ISEEADSNSF TSATGSKINF NSKWDWLDEF DKEDEEMYND
PNSKLRQKWR KYELIFDAEP RYNDDAQVSD
