SAK1_YEAST
ID SAK1_YEAST Reviewed; 1142 AA.
AC P38990; D3DM35;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=SNF1-activating kinase 1;
DE EC=2.7.11.1;
GN Name=SAK1; Synonyms=PAK1; OrderedLocusNames=YER129W; ORFNames=SYGP-ORF45;
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 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 [GENOMIC DNA] OF 1-657, AND FUNCTION.
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=9341678; DOI=10.1007/s004380050544;
RA Hovland P.G., Tecklenberg M., Sclafani R.A.;
RT "Overexpression of the protein kinase Pak1 suppresses yeast DNA polymerase
RT mutations.";
RL Mol. Gen. Genet. 256:45-53(1997).
RN [4]
RP PREDICTION OF FUNCTION.
RX PubMed=9020587; DOI=10.1016/s0968-0004(96)10068-2;
RA Hunter T., Plowman G.D.;
RT "The protein kinases of budding yeast: six score and more.";
RL Trends Biochem. Sci. 22:18-22(1997).
RN [5]
RP FUNCTION.
RX PubMed=12906789; DOI=10.1016/s0960-9822(03)00459-7;
RA Sutherland C.M., Hawley S.A., McCartney R.R., Leech A., Stark M.J.R.,
RA Schmidt M.C., Hardie D.G.;
RT "Elm1p is one of three upstream kinases for the Saccharomyces cerevisiae
RT SNF1 complex.";
RL Curr. Biol. 13:1299-1305(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH SNF1.
RX PubMed=12748292; DOI=10.1128/mcb.23.11.3909-3917.2003;
RA Nath N., McCartney R.R., Schmidt M.C.;
RT "Yeast Pak1 kinase associates with and activates Snf1.";
RL Mol. Cell. Biol. 23:3909-3917(2003).
RN [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=12847291; DOI=10.1073/pnas.1533136100;
RA Hong S.-P., Leiper F.C., Woods A., Carling D., Carlson M.;
RT "Activation of yeast Snf1 and mammalian AMP-activated protein kinase by
RT upstream kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8839-8843(2003).
RN [10]
RP FUNCTION.
RX PubMed=15340085; DOI=10.1128/mcb.24.18.8255-8263.2004;
RA Hedbacker K., Hong S.-P., Carlson M.;
RT "Pak1 protein kinase regulates activation and nuclear localization of Snf1-
RT Gal83 protein kinase.";
RL Mol. Cell. Biol. 24:8255-8263(2004).
RN [11]
RP FUNCTION.
RX PubMed=15824893; DOI=10.1007/s00294-005-0576-2;
RA McCartney R.R., Rubenstein E.M., Schmidt M.C.;
RT "Snf1 kinase complexes with different beta subunits display stress-
RT dependent preferences for the three Snf1-activating kinases.";
RL Curr. Genet. 47:335-344(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1126, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION, ASSOCIATION WITH THE SNF1 KINASE COMPLEX, AND INTERACTION WITH
RP SNF1.
RX PubMed=16201971; DOI=10.1042/bj20051213;
RA Elbing K., McCartney R.R., Schmidt M.C.;
RT "Purification and characterization of the three Snf1-activating kinases of
RT Saccharomyces cerevisiae.";
RL Biochem. J. 393:797-805(2006).
RN [14]
RP FUNCTION, AND DOMAIN.
RX PubMed=16607009; DOI=10.1128/ec.5.4.620-627.2006;
RA Rubenstein E.M., McCartney R.R., Schmidt M.C.;
RT "Regulatory domains of Snf1-activating kinases determine pathway
RT specificity.";
RL Eukaryot. Cell 5:620-627(2006).
RN [15]
RP FUNCTION, AND INTERACTION WITH SNF1.
RX PubMed=16847059; DOI=10.1074/jbc.m603811200;
RA Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.;
RT "Subunits of the Snf1 kinase heterotrimer show interdependence for
RT association and activity.";
RL J. Biol. Chem. 281:26170-26180(2006).
RN [16]
RP FUNCTION.
RX PubMed=17438333; DOI=10.1074/jbc.m700146200;
RA Hong S.-P., Carlson M.;
RT "Regulation of snf1 protein kinase in response to environmental stress.";
RL J. Biol. Chem. 282:16838-16845(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1126, 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964, AND IDENTIFICATION BY
RP 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 [20]
RP FUNCTION.
RX PubMed=19284616; DOI=10.1186/1471-2164-10-105;
RA Thorsen M., Perrone G.G., Kristiansson E., Traini M., Ye T., Dawes I.W.,
RA Nerman O., Tamas M.J.;
RT "Genetic basis of arsenite and cadmium tolerance in Saccharomyces
RT cerevisiae.";
RL BMC Genomics 10:105-105(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-1126, 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 [22]
RP FUNCTION.
RX PubMed=19880754; DOI=10.1128/ec.00216-09;
RA Orlova M., Ozcetin H., Barrett L., Kuchin S.;
RT "Roles of the Snf1-activating kinases during nitrogen limitation and
RT pseudohyphal differentiation in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 9:208-214(2010).
RN [23]
RP FUNCTION, DOMAIN, AND INTERACTION WITH REG1 AND SNF1.
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).
CC -!- FUNCTION: Serine/threonine-protein kinase that phosphorylates SNF1, the
CC catalytic subunit of the SNF1 kinase complex. Acts as an activator of
CC the SNF1 kinase complex and controls its nuclear localization upon
CC glucose and nitrogen depletion. Also required for SNF1 kinase
CC activation under other stress conditions like alkaline pH or presence
CC of cadmium. {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:12847291,
CC ECO:0000269|PubMed:12906789, ECO:0000269|PubMed:15340085,
CC ECO:0000269|PubMed:15824893, ECO:0000269|PubMed:16201971,
CC ECO:0000269|PubMed:16607009, ECO:0000269|PubMed:16847059,
CC ECO:0000269|PubMed:17438333, ECO:0000269|PubMed:19284616,
CC ECO:0000269|PubMed:19880754, ECO:0000269|PubMed:21216941,
CC ECO:0000269|PubMed:9341678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Associates with the SNF1 kinase complex. Interacts with SNF1
CC and REG1. {ECO:0000269|PubMed:12748292, ECO:0000269|PubMed:16201971,
CC ECO:0000269|PubMed:16847059, ECO:0000269|PubMed:21216941}.
CC -!- INTERACTION:
CC P38990; Q00684: CDC14; NbExp=2; IntAct=EBI-12863, EBI-4192;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The kinase domain is not sufficient by themself for proper
CC function and that the non-conserved N-terminal and C-terminal domains
CC are critical for the biological activity. The C-terminus promotes
CC interaction of ELM1 and TOS3 kinases with SNF1.
CC {ECO:0000269|PubMed:16607009, ECO:0000269|PubMed:21216941}.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U18916; AAC03227.1; -; Genomic_DNA.
DR EMBL; U13398; AAC49840.1; ALT_TERM; Genomic_DNA.
DR EMBL; BK006939; DAA07789.1; -; Genomic_DNA.
DR PIR; S50632; S50632.
DR RefSeq; NP_011055.3; NM_001179019.3.
DR AlphaFoldDB; P38990; -.
DR SMR; P38990; -.
DR BioGRID; 36873; 161.
DR DIP; DIP-5407N; -.
DR IntAct; P38990; 14.
DR MINT; P38990; -.
DR STRING; 4932.YER129W; -.
DR iPTMnet; P38990; -.
DR MaxQB; P38990; -.
DR PaxDb; P38990; -.
DR PRIDE; P38990; -.
DR EnsemblFungi; YER129W_mRNA; YER129W; YER129W.
DR GeneID; 856866; -.
DR KEGG; sce:YER129W; -.
DR SGD; S000000931; SAK1.
DR VEuPathDB; FungiDB:YER129W; -.
DR eggNOG; KOG0585; Eukaryota.
DR GeneTree; ENSGT00940000161828; -.
DR HOGENOM; CLU_003784_0_0_1; -.
DR InParanoid; P38990; -.
DR OMA; CISFMID; -.
DR BioCyc; YEAST:G3O-30292-MON; -.
DR BRENDA; 2.7.11.1; 984.
DR PRO; PR:P38990; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P38990; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0090329; P:regulation of DNA-templated DNA replication; IGI:SGD.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IMP:SGD.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IMP:SGD.
DR GO; GO:2000220; P:regulation of pseudohyphal growth; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1142
FT /note="SNF1-activating kinase 1"
FT /id="PRO_0000086464"
FT DOMAIN 133..448
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 22..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 139..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT CONFLICT 171
FT /note="Q -> H (in Ref. 3; AAC49840)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..268
FT /note="EYL -> DS (in Ref. 3; AAC49840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1142 AA; 126872 MW; 425D71B8340B3F8F CRC64;
MDRSDKKVNV EEVNVPSNLQ IELEKSGTSS SVSLRSPTKS SATNLAGMAE GARDNASIAS
SSVDSLNMLL ERQRVRQLNH PQHQQHISSS LAKTPTTTSS FCSSGSSKNK VKETNRISLT
YDPVSKRKVL NTYEIIKELG HGQHGKVKLA RDILSKQLVA IKIVDRHEKK QRKFFTFIKS
SKISENDKIK REIAIMKKCH HKHVVQLIEV LDDLKSRKIY LVLEYCSRGE VKWCPPDCME
SDAKGPSLLS FQETREILRG VVLGLEYLHY QGIIHRDIKP ANLLISGDGT VKISDFGVSL
AASSTNSSDS SESLDELELA KTVGTPAFFA PEMCLGEDAF TRYNLTKENL FRGSCISFMI
DIWAVGVTLY CLLFGMLPFF SDFELKLFEK IVNDPLKFPT FKEIQSNKVS KVSCEEEYEM
AKDLLLKLLE KNPQKRMTIP AIKKHPFVSW DFDHVPENDE KLLSSVLEQK LRFQCNQTDQ
FEPISISKHE LKNAVSGVGK KIKESVLKSI PLKDPSDLSN KNYLHPTETT RGRGDANVIV
SEGSVLSNIK ELSANDGCLN TDSDTNININ DDDHYSGDDN DGHLTKRELE RELNKFDDKH
EAGNMVNLPI NSSFASLDSF YIDNFAMARM GMSSPEAGDS VSSVPNLPSA PSSTRLGRSP
VFSGVTNQPS PIRPVLPQQK SSFCATGRYD KSHNSLLRNS SSHLTSYNSG RPSSRTGRMN
SRNQNLPKIP NSLSKISTTK LTELRVPKDS EIPSPAKNPN ADRLRRFPVK KNTKTPAIKD
PPRININSSD KSGSKNSPIK SLYQRMKQSK DNSKTFEVRR GNFFSHFNGD DDDSSSQSSV
TSSGSESDSE LSSTSSSCTS GTQSRNSSNN NAYSETESLP FEFGVDSEDG SGVLLRDLPN
EDQIRPFLDI QPCRRMKVKS SLNLEPPSVS SSSSSSSDED ELILNVGTAG HRRRHNSSKL
SELSNSPQKG SNNFMYSNGS VHDSETTITP QNMDDLTLHQ ALSRSQPISK PGPLVLPKRL
DQKKATTETS NLTDIVEFNG NNDHRKDKNF DKVLYSRDLL KDALSSTNAG RRRSIPSNKI
RGRKDASITM STNVGNDEHA RNTSCHGDKG QENGAIKQRT HERSRSLTVA ELNEEKRRSA
LP
