STM1_YEAST
ID STM1_YEAST Reviewed; 273 AA.
AC P39015; D6VYE5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Suppressor protein STM1;
DE AltName: Full=3BP1;
DE AltName: Full=GU4 nucleic-binding protein 2;
DE Short=G4p2 protein;
DE AltName: Full=POP2 multicopy suppressor protein 4;
DE AltName: Full=Ribosomal subunits association factor;
DE Short=AF;
DE AltName: Full=TOM1 suppressor protein 1;
DE AltName: Full=Triplex-binding protein 1;
GN Name=STM1; Synonyms=MPT4, STO1; OrderedLocusNames=YLR150W;
GN ORFNames=L9634.1;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9504907; DOI=10.1093/genetics/148.2.571;
RA Hata H., Mitsui H., Liu H., Bai Y., Denis C.L., Shimizu Y., Sakai A.;
RT "Dhh1p, a putative RNA helicase, associates with the general transcription
RT factors Pop2p and Ccr4p from Saccharomyces cerevisiae.";
RL Genetics 148:571-579(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7548221; DOI=10.1016/0167-4781(95)00123-x;
RA Utsugi T., Toh-e A., Kikuchi Y.;
RT "A high dose of the STM1 gene suppresses the temperature sensitivity of the
RT tom1 and htr1 mutants in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1263:285-288(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 122-145 AND 146-170,
RP AND DNA-BINDING.
RX PubMed=7721866; DOI=10.1074/jbc.270.16.9413;
RA Frantz J.D., Gilbert W.;
RT "A yeast gene product, G4p2, with a specific affinity for quadruplex
RT nucleic acids.";
RL J. Biol. Chem. 270:9413-9419(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [5]
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 [6]
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 [7]
RP PROTEIN SEQUENCE OF 2-27; 34-46 AND 263-273, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 106-114 AND 265-273, AND DNA-BINDING.
RX PubMed=10681538; DOI=10.1074/jbc.275.8.5573;
RA Nelson L.D., Musso M., Van Dyke M.W.;
RT "The yeast STM1 gene encodes a purine motif triple helical DNA-binding
RT protein.";
RL J. Biol. Chem. 275:5573-5581(2000).
RN [9]
RP PROTEIN SEQUENCE OF 110-137.
RX PubMed=15654430; DOI=10.1590/s0074-02762004000700012;
RA Correia H., Medina R., Hernandez A., Bustamante E., Chakraburtty K.,
RA Herrera F.;
RT "Similarity between the association factor of ribosomal subunits and the
RT protein Stm1p from Saccharomyces cerevisiae.";
RL Mem. Inst. Oswaldo Cruz 99:733-737(2004).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11514626; DOI=10.1091/mbc.12.8.2422;
RA Ligr M., Velten I., Froehlich E., Madeo F., Ledig M., Froehlich K.-U.,
RA Wolf D.H., Hilt W.;
RT "The proteasomal substrate Stm1 participates in apoptosis-like cell death
RT in yeast.";
RL Mol. Biol. Cell 12:2422-2432(2001).
RN [11]
RP INTERACTION WITH CDC13.
RX PubMed=12207228; DOI=10.1007/s00438-002-0712-3;
RA Hayashi N., Murakami S.;
RT "STM1, a gene which encodes a guanine quadruplex binding protein, interacts
RT with CDC13 in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 267:806-813(2002).
RN [12]
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 [13]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15044472; DOI=10.1074/jbc.m401981200;
RA Van Dyke M.W., Nelson L.D., Weilbaecher R.G., Mehta D.V.;
RT "Stm1p, a G4 quadruplex and purine motif triplex nucleic acid-binding
RT protein, interacts with ribosomes and subtelomeric Y' DNA in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 279:24323-24333(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, 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-55 AND SER-229, 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-118, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP 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 [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-121; LYS-171 AND
RP LYS-184, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Binds specifically G4 quadruplex (these are four-stranded
CC right-handed helices, stabilized by guanine base quartets) and purine
CC motif triplex (characterized by a third, antiparallel purine-rich DNA
CC strand located within the major groove of a homopurine stretch of
CC duplex DNA) nucleic acid structures. These structures may be present at
CC telomeres or in rRNAs. Acts with CDC13 to control telomere length
CC homeostasis. Involved in the control of the apoptosis-like cell death.
CC {ECO:0000269|PubMed:15044472}.
CC -!- SUBUNIT: Interacts with CDC13. Associates with mature 80S ribosomes.
CC Associates with the telomere-proximal Y' element.
CC {ECO:0000269|PubMed:12207228, ECO:0000269|PubMed:15044472}.
CC -!- INTERACTION:
CC P39015; P33203: PRP40; NbExp=2; IntAct=EBI-11238, EBI-701;
CC P39015; P39940: RSP5; NbExp=3; IntAct=EBI-11238, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, perinuclear
CC region. Note=Concentrated in the perinuclear region.
CC -!- MISCELLANEOUS: Present with 46842 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; D26183; BAA05171.1; -; Genomic_DNA.
DR EMBL; D32208; BAA06907.1; -; Genomic_DNA.
DR EMBL; U20616; AAA70169.1; -; Genomic_DNA.
DR EMBL; Z73322; CAA97722.1; -; Genomic_DNA.
DR EMBL; U53879; AAB82384.1; -; Genomic_DNA.
DR EMBL; AY557944; AAS56270.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09461.1; -; Genomic_DNA.
DR PIR; S48511; S48511.
DR RefSeq; NP_013251.1; NM_001182037.1.
DR PDB; 4U3M; X-ray; 3.00 A; SM/sM=1-273.
DR PDB; 4U3N; X-ray; 3.20 A; SM/sM=1-273.
DR PDB; 4U3U; X-ray; 2.90 A; SM/sM=1-273.
DR PDB; 4U4N; X-ray; 3.10 A; SM/sM=1-273.
DR PDB; 4U4O; X-ray; 3.60 A; SM/sM=1-273.
DR PDB; 4U4Q; X-ray; 3.00 A; SM/sM=1-273.
DR PDB; 4U4R; X-ray; 2.80 A; SM/sM=1-273.
DR PDB; 4U4U; X-ray; 3.00 A; SM/sM=1-273.
DR PDB; 4U4Y; X-ray; 3.20 A; SM/sM=1-273.
DR PDB; 4U4Z; X-ray; 3.10 A; SM/sM=1-273.
DR PDB; 4U50; X-ray; 3.20 A; SM/sM=1-273.
DR PDB; 4U51; X-ray; 3.20 A; SM/sM=1-273.
DR PDB; 4U52; X-ray; 3.00 A; SM/sM=1-273.
DR PDB; 4U53; X-ray; 3.30 A; SM/sM=1-273.
DR PDB; 4U55; X-ray; 3.20 A; SM/sM=1-273.
DR PDB; 4U56; X-ray; 3.45 A; SM/sM=1-273.
DR PDB; 4U6F; X-ray; 3.10 A; SM/sM=1-273.
DR PDB; 4V88; X-ray; 3.00 A; Ah/Ch=1-273.
DR PDB; 4V8Y; EM; 4.30 A; A7=1-273.
DR PDB; 4V8Z; EM; 6.60 A; A7=1-273.
DR PDB; 5DAT; X-ray; 3.15 A; SM/sM=1-273.
DR PDB; 5DC3; X-ray; 3.25 A; SM/sM=1-273.
DR PDB; 5DGE; X-ray; 3.45 A; SM/sM=1-273.
DR PDB; 5FCI; X-ray; 3.40 A; SM/sM=1-141.
DR PDB; 5FCJ; X-ray; 3.10 A; SM/sM=1-141.
DR PDB; 5I4L; X-ray; 3.10 A; SM=1-150, sM=1-118.
DR PDB; 5LYB; X-ray; 3.25 A; SM=9-141, sM=23-85.
DR PDB; 5NDG; X-ray; 3.70 A; SM/sM=2-273.
DR PDB; 5NDV; X-ray; 3.30 A; SM/sM=2-273.
DR PDB; 5NDW; X-ray; 3.70 A; SM/sM=2-273.
DR PDB; 5OBM; X-ray; 3.40 A; SM/sM=2-273.
DR PDB; 5TGA; X-ray; 3.30 A; SM=9-141, sM=23-85.
DR PDB; 5TGM; X-ray; 3.50 A; SM=21-141, sM=23-85.
DR PDB; 6HHQ; X-ray; 3.10 A; i/sM=1-273.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 6HHQ; -.
DR AlphaFoldDB; P39015; -.
DR SMR; P39015; -.
DR BioGRID; 31419; 391.
DR DIP; DIP-1675N; -.
DR IntAct; P39015; 25.
DR MINT; P39015; -.
DR STRING; 4932.YLR150W; -.
DR iPTMnet; P39015; -.
DR MaxQB; P39015; -.
DR PaxDb; P39015; -.
DR PRIDE; P39015; -.
DR TopDownProteomics; P39015; -.
DR EnsemblFungi; YLR150W_mRNA; YLR150W; YLR150W.
DR GeneID; 850843; -.
DR KEGG; sce:YLR150W; -.
DR SGD; S000004140; STM1.
DR VEuPathDB; FungiDB:YLR150W; -.
DR eggNOG; ENOG502QS5P; Eukaryota.
DR HOGENOM; CLU_043312_2_0_1; -.
DR InParanoid; P39015; -.
DR OMA; KADKKWA; -.
DR BioCyc; YEAST:G3O-32286-MON; -.
DR PRO; PR:P39015; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P39015; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0045142; F:triplex DNA binding; IDA:SGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:SGD.
DR GO; GO:0043558; P:regulation of translational initiation in response to stress; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IGI:SGD.
DR GO; GO:0031929; P:TOR signaling; IMP:SGD.
DR GO; GO:0006414; P:translational elongation; IMP:SGD.
DR DisProt; DP00994; -.
DR InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR InterPro; IPR019084; Stm1-like_N.
DR Pfam; PF09598; Stm1_N; 1.
DR SMART; SM01233; HABP4_PAI-RBP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7"
FT CHAIN 2..273
FT /note="Suppressor protein STM1"
FT /id="PRO_0000072278"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 133
FT /note="E -> Q (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="K -> E (in Ref. 3; AAA70169)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="E -> G (in Ref. 3; AAA70169)"
FT /evidence="ECO:0000305"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 67..72
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4U56"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:4U3U"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 273 AA; 29995 MW; CD01C5C047F99523 CRC64;
MSNPFDLLGN DVEDADVVVL PPKEIVKSNT SSKKADVPPP SADPSKARKN RPRPSGNEGA
IRDKTAGRRN NRSKDVTDSA TTKKSNTRRA TDRHSRTGKT DTKKKVNQGW GDDKKELSAE
KEAQADAAAE IAEDAAEAED AGKPKTAQLS LQDYLNQQAN NQFNKVPEAK KVELDAERIE
TAEKEAYVPA TKVKNVKSKQ LKTKEYLEFD ATFVESNTRK NFGDRNNNSR NNFNNRRGGR
GARKGNNTAN ATNSANTVQK NRNIDVSNLP SLA
