REG1_YEAST
ID REG1_YEAST Reviewed; 1014 AA.
AC Q00816; D6VS13;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Resistance to glucose repression protein 1;
DE AltName: Full=Protein HEX2;
DE AltName: Full=Second-site suppressor of the rna1-1 mutation 1;
GN Name=REG1; Synonyms=HEX2, PZF240, SPP43, SRN1; OrderedLocusNames=YDR028C;
GN ORFNames=YD9813.06C;
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].
RX PubMed=1889400; DOI=10.1111/j.1432-1033.1991.tb16187.x;
RA Niederacher D., Entian K.-D.;
RT "Characterization of Hex2 protein, a negative regulatory element necessary
RT for glucose repression in yeast.";
RL Eur. J. Biochem. 200:311-319(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1588964; DOI=10.1128/mcb.12.6.2673-2680.1992;
RA Tung K.-S., Norbeck L.L., Nolan S.L., Atkinson N.S., Hopper A.K.;
RT "SRN1, a yeast gene involved in RNA processing, is identical to HEX2/REG1,
RT a negative regulator in glucose repression.";
RL Mol. Cell. Biol. 12:2673-2680(1992).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1014.
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 [6]
RP INTERACTION WITH PP1.
RX PubMed=8846786; DOI=10.1002/j.1460-2075.1995.tb00282.x;
RA Tu J.L., Carlson M.;
RT "REG1 binds to protein phosphatase type 1 and regulates glucose repression
RT in Saccharomyces cerevisiae.";
RL EMBO J. 14:5939-5946(1995).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-75, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-421; SER-572 AND
RP SER-576, AND IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-75; TYR-480 AND
RP SER-490, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-254; SER-311;
RP SER-421; SER-576 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-242; SER-421;
RP SER-570; SER-572; SER-576; SER-610; SER-614; THR-896; SER-898 AND SER-980,
RP AND 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 [13]
RP FUNCTION, AND INTERACTION WITH SAK1.
RX PubMed=21216941; DOI=10.1128/ec.00291-10;
RA Liu Y., Xu X., Carlson M.;
RT "Interaction of SNF1 protein kinase with its activating kinase Sak1.";
RL Eukaryot. Cell 10:313-319(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in RNA processing and negative regulation of glucose
CC repression. Regulates the level of two antigens, P43 and P70. Binds to
CC protein phosphatase type 1. Functions with REG2 and SNF1 protein kinase
CC to regulate growth. Might regulate SNF1 directly or indirectly.
CC {ECO:0000269|PubMed:21216941}.
CC -!- SUBUNIT: Interacts with SAK1. {ECO:0000269|PubMed:21216941,
CC ECO:0000269|PubMed:8846786}.
CC -!- INTERACTION:
CC Q00816; P32598: GLC7; NbExp=4; IntAct=EBI-8270, EBI-13715;
CC Q00816; P06782: SNF1; NbExp=7; IntAct=EBI-8270, EBI-17516;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 2560 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M33703; AAA34670.1; -; Genomic_DNA.
DR EMBL; M90540; AAB59326.1; -; Genomic_DNA.
DR EMBL; Z47814; CAA87807.1; -; Genomic_DNA.
DR EMBL; Z74324; CAA98850.1; -; Genomic_DNA.
DR EMBL; X95966; CAA65223.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11873.1; -; Genomic_DNA.
DR PIR; S32613; S32613.
DR RefSeq; NP_010311.1; NM_001180336.1.
DR AlphaFoldDB; Q00816; -.
DR BioGRID; 32078; 139.
DR ComplexPortal; CPX-1266; REG1-GLC7 phosphatase complex.
DR DIP; DIP-2513N; -.
DR ELM; Q00816; -.
DR IntAct; Q00816; 24.
DR MINT; Q00816; -.
DR STRING; 4932.YDR028C; -.
DR iPTMnet; Q00816; -.
DR MaxQB; Q00816; -.
DR PaxDb; Q00816; -.
DR PRIDE; Q00816; -.
DR EnsemblFungi; YDR028C_mRNA; YDR028C; YDR028C.
DR GeneID; 851592; -.
DR KEGG; sce:YDR028C; -.
DR SGD; S000002435; REG1.
DR VEuPathDB; FungiDB:YDR028C; -.
DR eggNOG; ENOG502QSII; Eukaryota.
DR HOGENOM; CLU_012586_0_0_1; -.
DR InParanoid; Q00816; -.
DR OMA; WKYIILK; -.
DR BioCyc; YEAST:G3O-29644-MON; -.
DR ChiTaRS; REG1; yeast.
DR PRO; PR:Q00816; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q00816; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:ComplexPortal.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:SGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:SGD.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IDA:SGD.
DR GO; GO:1904547; P:regulation of cellular response to glucose starvation; IC:ComplexPortal.
DR GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
DR InterPro; IPR013860; AreA_GATA.
DR Pfam; PF08550; DUF1752; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..1014
FT /note="Resistance to glucose repression protein 1"
FT /id="PRO_0000083953"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 277..283
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 595..599
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 873..879
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..757
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 480
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 896
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 376..377
FT /note="DK -> EE (in Ref. 1; AAA34670)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="N -> K (in Ref. 1; AAA34670)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="D -> H (in Ref. 1; AAA34670)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="S -> T (in Ref. 1; AAA34670)"
FT /evidence="ECO:0000305"
FT CONFLICT 988..1014
FT /note="ARGMASKYLHSWKKSDVKPQENGNDSS -> QEVWQASTCTLGKRVTSSHKK
FT MEMTAVRRKNFEVNMKRK (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1014 AA; 112616 MW; 0D4AAC75E111B346 CRC64;
MSTNLANYFA GKKDIENEHV NRNASHESNS KSDVKISGND NDNDEDMGPS VSMAVQAKND
DDFHKSTFNL KRTRSMGLLD EYIDPTKKLL GRSDDLYDND NEYYDNSSNN SSSNSSDDDY
DDGYQEHSTS VSPPPADNDS YLIPQDDNDV VVEPERHVDY LSHEWKESEI SNSWKYIILK
KKKRDVDLVN AARLENASWR TWAKARNNLK TVSPEVVNWS KDSDVTWLYG PIVRDSEGNA
QSEEEHDLER GYGSDDENSK RISMPTKNSK SIAAAPKPIL KKRTVTEIIE DNALWKLNEA
RKHMTEMKHA SVIMDPNGNK NVHDDFDALA AQVNAQYYHY PKESNSSVSL KSQHSDKKDN
STIPNPVGEN SNGGGDKGEE DLHLKSALHV QNNRSTAQSN KSILENSTND RKANLDQNLN
SPDNNRFPSS TSSSNRDNEN NSMGLSSILT SNPSEKSNKP TKNRHIHFND RVEQCMALRY
PASQSEDDES DDENKQYVDV NNNANVTTIN NNRTPLLAIQ HKSIPINSAT EHLNKNTSDD
DTSSQSSSSS HSDDEEHGGL YINARFSRRS DSGVHSPITD NSSVASSTTS RAHVRPIIKL
LPDTTLNYGS DEESDNGEFN GYGNAVSHNV NTSRGYDYIY DYNSVYTGDT SSFLPVDSCD
IVDVPEGMDL QTAIADDNAS NYEFNNAVES KEKHVPQLHK ASANNTTRQH GSHMLLYDDD
NYSSSSDSEQ QFIEDSQYNS SDDEEEEDDD DQEVDDNHDE GLSLRRTLSL GKSGSTNSLY
DLAQPSLSSA TPQQKNPTNF TGGKTDVDKD AQLAVRPYPL KRNSSSGNFI FNSDSEEESS
SEEEQRPLPA NSQLVNRSVL KGSVTPANIS SQKKKALPKQ PKASDSSQSF RIVNNTPSPA
EVGASDVAIE GYFSPRNESI KSVVSGGNMM DHQDHSEMDT LAKGFENCHI NNASKLKDKK
VDSVQTTRKE ASLTDSSNES LHKVVQNARG MASKYLHSWK KSDVKPQENG NDSS
