SIR3_YEAST
ID SIR3_YEAST Reviewed; 978 AA.
AC P06701; D6VZ77; E9P924;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 6.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Regulatory protein SIR3;
DE AltName: Full=Silent information regulator 3;
GN Name=SIR3; Synonyms=CMT1, MAR2, STE8; OrderedLocusNames=YLR442C;
GN ORFNames=L9753.10;
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=6098447; DOI=10.1002/j.1460-2075.1984.tb02214.x;
RA Shore D., Squire M., Nasmyth K.A.;
RT "Characterization of two genes required for the position-effect control of
RT yeast mating-type genes.";
RL EMBO J. 3:2817-2823(1984).
RN [2]
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 [3]
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 [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 PHOSPHORYLATION.
RX PubMed=8909534; DOI=10.1083/jcb.135.3.571;
RA Stone E.M., Pillus L.;
RT "Activation of an MAP kinase cascade leads to Sir3p hyperphosphorylation
RT and strengthens transcriptional silencing.";
RL J. Cell Biol. 135:571-583(1996).
RN [6]
RP REVIEW.
RX PubMed=11722841; DOI=10.1016/s0378-1119(01)00741-7;
RA Gasser S.M., Cockell M.M.;
RT "The molecular biology of the SIR proteins.";
RL Gene 279:1-16(2001).
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 MUTAGENESIS OF ALA-2, AND ACETYLATION AT ALA-2.
RX PubMed=15454564; DOI=10.1534/genetics.104.028803;
RA Wang X., Connelly J.J., Wang C.L., Sternglanz R.;
RT "Importance of the sir3 N terminus and its acetylation for yeast
RT transcriptional silencing.";
RL Genetics 168:547-551(2004).
RN [9]
RP INTERACTION WITH MCM10.
RX PubMed=16328881; DOI=10.1007/s11033-005-2312-x;
RA Douglas N.L., Dozier S.K., Donato J.J.;
RT "Dual roles for Mcm10 in DNA replication initiation and silencing at the
RT mating-type loci.";
RL Mol. Biol. Rep. 32:197-204(2005).
RN [10]
RP 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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-229.
RX PubMed=16641491; DOI=10.1110/ps.052061006;
RA Hou Z., Danzer J.R., Fox C.A., Keck J.L.;
RT "Structure of the Sir3 protein bromo adjacent homology (BAH) domain from S.
RT cerevisiae at 1.95 A resolution.";
RL Protein Sci. 15:1182-1186(2006).
CC -!- FUNCTION: The proteins SIR1 through SIR4 are required for
CC transcriptional repression of the silent mating type loci, HML and HMR.
CC The proteins SIR2 through SIR4 repress mulitple loci by modulating
CC chromatin structure. Involves the compaction of chromatin fiber into a
CC more condensed form.
CC -!- SUBUNIT: Homodimer and interacts with SIR4 and RAP1 C-terminus.
CC Interacts with MCM10. {ECO:0000269|PubMed:16328881}.
CC -!- INTERACTION:
CC P06701; P11938: RAP1; NbExp=8; IntAct=EBI-17230, EBI-14821;
CC P06701; P06701: SIR3; NbExp=8; IntAct=EBI-17230, EBI-17230;
CC P06701; P11978: SIR4; NbExp=8; IntAct=EBI-17230, EBI-17237;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: N-terminal acetylation by NatA is important for transcriptional
CC silencing activity. {ECO:0000269|PubMed:15454564}.
CC -!- MISCELLANEOUS: Present with 1400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X01420; CAA25668.1; -; Genomic_DNA.
DR EMBL; U21094; AAB67522.1; -; Genomic_DNA.
DR EMBL; AY693157; AAT93176.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09743.1; -; Genomic_DNA.
DR PIR; S59410; RGBYI3.
DR RefSeq; NP_013547.3; NM_001182330.3.
DR PDB; 2FL7; X-ray; 1.85 A; A=1-229.
DR PDB; 2FVU; X-ray; 2.00 A; A/B=1-219.
DR PDB; 3OWT; X-ray; 2.00 A; C=456-481.
DR PDB; 3TE6; X-ray; 2.80 A; A/B=530-845.
DR PDB; 3TU4; X-ray; 3.00 A; K/L=1-213.
DR PDB; 3ZCO; X-ray; 2.70 A; A=840-978.
DR PDB; 4JJN; X-ray; 3.09 A; K/L=2-382.
DR PDB; 4KUD; X-ray; 3.20 A; K/L=2-219.
DR PDB; 4KUI; X-ray; 1.85 A; A=2-219.
DR PDB; 4KUL; X-ray; 2.62 A; A=2-219.
DR PDB; 4LD9; X-ray; 3.31 A; K/L=2-229.
DR PDBsum; 2FL7; -.
DR PDBsum; 2FVU; -.
DR PDBsum; 3OWT; -.
DR PDBsum; 3TE6; -.
DR PDBsum; 3TU4; -.
DR PDBsum; 3ZCO; -.
DR PDBsum; 4JJN; -.
DR PDBsum; 4KUD; -.
DR PDBsum; 4KUI; -.
DR PDBsum; 4KUL; -.
DR PDBsum; 4LD9; -.
DR AlphaFoldDB; P06701; -.
DR SMR; P06701; -.
DR BioGRID; 31701; 113.
DR ComplexPortal; CPX-1811; Sir2-3-4 silent chromatin complex.
DR DIP; DIP-595N; -.
DR IntAct; P06701; 46.
DR MINT; P06701; -.
DR STRING; 4932.YLR442C; -.
DR CarbonylDB; P06701; -.
DR iPTMnet; P06701; -.
DR MaxQB; P06701; -.
DR PaxDb; P06701; -.
DR PRIDE; P06701; -.
DR EnsemblFungi; YLR442C_mRNA; YLR442C; YLR442C.
DR GeneID; 851163; -.
DR KEGG; sce:YLR442C; -.
DR SGD; S000004434; SIR3.
DR VEuPathDB; FungiDB:YLR442C; -.
DR eggNOG; KOG1514; Eukaryota.
DR GeneTree; ENSGT00530000063498; -.
DR HOGENOM; CLU_012774_1_1_1; -.
DR InParanoid; P06701; -.
DR OMA; SANTHYD; -.
DR BioCyc; YEAST:G3O-32498-MON; -.
DR EvolutionaryTrace; P06701; -.
DR PRO; PR:P06701; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P06701; protein.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:SGD.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0000792; C:heterochromatin; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031491; F:nucleosome binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IMP:SGD.
DR GO; GO:0031507; P:heterochromatin assembly; IMP:SGD.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0034398; P:telomere tethering at nuclear periphery; IMP:SGD.
DR DisProt; DP00533; -.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID50067; -.
DR InterPro; IPR041083; AAA_lid_10.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR020793; ORC1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10763:SF23; PTHR10763:SF23; 1.
DR Pfam; PF17872; AAA_lid_10; 1.
DR Pfam; PF01426; BAH; 1.
DR SMART; SM00439; BAH; 1.
DR PROSITE; PS51038; BAH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15454564"
FT CHAIN 2..978
FT /note="Regulatory protein SIR3"
FT /id="PRO_0000097768"
FT DOMAIN 48..188
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 218..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:15454564"
FT MUTAGEN 2
FT /note="A->G: No acetylation, reduced silencing activity."
FT /evidence="ECO:0000269|PubMed:15454564"
FT MUTAGEN 2
FT /note="A->Q: No acetylation, No silencing activity."
FT /evidence="ECO:0000269|PubMed:15454564"
FT MUTAGEN 2
FT /note="A->S: No effect."
FT /evidence="ECO:0000269|PubMed:15454564"
FT MUTAGEN 2
FT /note="A->T: Reduced silencing activity."
FT /evidence="ECO:0000269|PubMed:15454564"
FT CONFLICT 74
FT /note="I -> T (in Ref. 4; AAT93176)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="P -> S (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="T -> P (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="S -> G (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="K -> Q (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 429..430
FT /note="NE -> KK (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="L -> V (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="Q -> R (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="I -> V (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="E -> D (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="R -> G (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="S -> T (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="D -> N (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="L -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="V -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 925
FT /note="Q -> K (in Ref. 1; CAA25668)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:2FVU"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:4KUI"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4KUI"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3TU4"
FT TURN 31..35
FT /evidence="ECO:0007829|PDB:3TU4"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2FL7"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4KUI"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2FL7"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3TU4"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2FL7"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4JJN"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:2FL7"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2FL7"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:4KUD"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4KUI"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:2FL7"
FT HELIX 465..475
FT /evidence="ECO:0007829|PDB:3OWT"
FT HELIX 535..568
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 574..578
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 583..598
FT /evidence="ECO:0007829|PDB:3TE6"
FT TURN 599..603
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 622..632
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 643..652
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 675..685
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 691..696
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 704..708
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 711..714
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 717..721
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 727..741
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 745..749
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 782..796
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 799..820
FT /evidence="ECO:0007829|PDB:3TE6"
FT STRAND 831..833
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 837..843
FT /evidence="ECO:0007829|PDB:3TE6"
FT HELIX 851..856
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 860..873
FT /evidence="ECO:0007829|PDB:3ZCO"
FT STRAND 874..876
FT /evidence="ECO:0007829|PDB:3ZCO"
FT STRAND 880..882
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 883..896
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 901..910
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 920..923
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 928..937
FT /evidence="ECO:0007829|PDB:3ZCO"
FT STRAND 940..945
FT /evidence="ECO:0007829|PDB:3ZCO"
FT STRAND 947..949
FT /evidence="ECO:0007829|PDB:3ZCO"
FT STRAND 952..956
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 959..968
FT /evidence="ECO:0007829|PDB:3ZCO"
FT HELIX 970..972
FT /evidence="ECO:0007829|PDB:3ZCO"
SQ SEQUENCE 978 AA; 111360 MW; CA2503D7645397AC CRC64;
MAKTLKDLDG WQVIITDDQG RVIDDNNRRR SRKRGGENVF LKRISDGLSF GKGESVIFND
NVTETYSVYL IHEIRLNTLN NVVEIWVFSY LRWFELKPKL YYEQFRPDLI KEDHPLEFYK
DKFFNEVNKS ELYLTAELSE IWLKDFIAVG QILPESQWND SSIDKIEDRD FLVRYACEPT
AEKFVPIDIF QIIRRVKEME PKQSDEYLKR VSVPVSGQKT NRQVMHKMGV ERSSKRLAKK
PSMKKIKIEP SADDDVNNGN IPSQRGTSTT HGSISPQEES VSPNISSASP SALTSPTDSS
KILQKRSISK ELIVSEEIPI NSSEQESDYE PNNETSVLSS KPGSKPEKTS TELVDGRENF
VYANNPEVSD DGGLEEETDE VSSESSDEAI IPVNKRRGAH GSELSSKIRK IHIQETQEFS
KNYTTETDNE MNGNGKPGIP RGNTKIHSMN ENPTPEKGNA KMIDFATLSK LKKKYQIILD
RFAPDNQVTD SSQLNKLTDE QSSLDVAGLE DKFRKACSSS GRETILSNFN ADINLEESIR
ESLQKRELLK SQVEDFTRIF LPIYDSLMSS QNKLFYITNA DDSTKFQLVN DVMDELITSS
ARKELPIFDY IHIDALELAG MDALYEKIWF AISKENLCGD ISLEALNFYI TNVPKAKKRK
TLILIQNPEN LLSEKILQYF EKWISSKNSK LSIICVGGHN VTIREQINIM PSLKAHFTEI
KLNKVDKNEL QQMIITRLKS LLKPFHVKVN DKKEMTIYNN IREGQNQKIP DNVIVINHKI
NNKITQLIAK NVANVSGSTE KAFKICEAAV EISKKDFVRK GGLQKGKLVV SQEMVPRYFS
EAINGFKDET ISKKIIGMSL LMRTFLYTLA QETEGTNRHT LALETVLIKM VKMLRDNPGY
KASKEIKKVI CGAWEPAITI EKLKQFSWIS VVNDLVGEKL VVVVLEEPSA SIMVELKLPL
EINYAFSMDE EFKNMDCI
