EIF3B_YEAST
ID EIF3B_YEAST Reviewed; 763 AA.
AC P06103; D6W356;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Cell cycle regulation and translation initiation protein;
DE AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit;
DE Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Translation initiation factor eIF3 p90 subunit;
GN Name=PRT1 {ECO:0000255|HAMAP-Rule:MF_03001}; Synonyms=CDC63;
GN OrderedLocusNames=YOR361C;
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=3029094; DOI=10.1016/s0021-9258(18)61583-2;
RA Hanic-Joyce P.J., Singer R.A., Johnston G.C.;
RT "Molecular characterization of the yeast PRT1 gene in which mutations
RT affect translation initiation and regulation of cell proliferation.";
RL J. Biol. Chem. 262:2845-2851(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 IDENTIFICATION IN THE EIF-3 CORE COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9671501; DOI=10.1128/mcb.18.8.4935;
RA Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R.,
RA Qin J., Hinnebusch A.G.;
RT "Identification of a translation initiation factor 3 (eIF3) core complex,
RT conserved in yeast and mammals, that interacts with eIF5.";
RL Mol. Cell. Biol. 18:4935-4946(1998).
RN [5]
RP FUNCTION.
RX PubMed=11387228; DOI=10.1093/emboj/20.11.2954;
RA Phan L., Schoenfeld L.W., Valasek L., Nielsen K.H., Hinnebusch A.G.;
RT "A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates
RT ribosome binding of mRNA and tRNA(i)Met.";
RL EMBO J. 20:2954-2965(2001).
RN [6]
RP INTERACTION WITH PCI8.
RX PubMed=11457827; DOI=10.1074/jbc.m102161200;
RA Shalev A., Valasek L., Pise-Masison C.A., Radonovich M., Phan L.,
RA Clayton J., He H., Brady J.N., Hinnebusch A.G., Asano K.;
RT "Saccharomyces cerevisiae protein Pci8p and human protein eIF3e/Int-6
RT interact with the eIF3 core complex by binding to cognate eIF3b subunits.";
RL J. Biol. Chem. 276:34948-34957(2001).
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 INTERACTION WITH HCR1; NIP1; TIF32; TIF34; TIF35; EIF-1; EIF-2 AND EIF-5,
RP ASSOCIATION WITH THE 40S RIBOSOME, AND MUTAGENESIS OF 124-LYS--GLU-130.
RX PubMed=16581774; DOI=10.1128/mcb.26.8.2984-2998.2006;
RA Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.;
RT "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of
RT eukaryotic initiation factor 3 in yeast.";
RL Mol. Cell. Biol. 26:2984-2998(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-669, AND
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 IDENTIFICATION IN THE EIF-3 COMPLEX WITH NIP1; TIF32; TIF34 AND TIF35.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND TYR-67, 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).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:11387228}.
CC -!- SUBUNIT: The eukaryotic translation initiation factor 3 (eIF-3) core
CC complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex
CC of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5
CC and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. {ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:9671501}.
CC -!- INTERACTION:
CC P06103; Q05911: ADE13; NbExp=2; IntAct=EBI-8973, EBI-14263;
CC P06103; P32497: NIP1; NbExp=12; IntAct=EBI-8973, EBI-8965;
CC P06103; P06103: PRT1; NbExp=2; IntAct=EBI-8973, EBI-8973;
CC P06103; P38249: RPG1; NbExp=13; IntAct=EBI-8973, EBI-8981;
CC P06103; P40217: TIF34; NbExp=17; IntAct=EBI-8973, EBI-8951;
CC P06103; Q04067: TIF35; NbExp=14; IntAct=EBI-8973, EBI-8958;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 47500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; J02674; AAA34917.1; -; Genomic_DNA.
DR EMBL; Z75269; CAA99690.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11122.1; -; Genomic_DNA.
DR PIR; A29562; A29562.
DR RefSeq; NP_015006.3; NM_001183781.3.
DR PDB; 3JAP; EM; 4.90 A; r=704-734.
DR PDB; 3JAQ; EM; 6.00 A; r=704-737.
DR PDB; 3NS5; X-ray; 2.60 A; A/B=76-161.
DR PDB; 3NS6; X-ray; 1.25 A; A/B=76-170.
DR PDB; 3ZWL; X-ray; 2.20 A; E/F=693-739.
DR PDB; 4U1E; X-ray; 2.00 A; B=694-737.
DR PDB; 4U1F; X-ray; 2.20 A; A/B=172-665.
DR PDB; 6FYX; EM; 3.05 A; p=1-763.
DR PDB; 6FYY; EM; 3.05 A; p=1-763.
DR PDB; 6GSM; EM; 5.15 A; p=77-737.
DR PDB; 6GSN; EM; 5.75 A; p=72-737.
DR PDB; 6ZCE; EM; 5.30 A; p=1-763.
DR PDB; 6ZU9; EM; 6.20 A; p=1-763.
DR PDBsum; 3JAP; -.
DR PDBsum; 3JAQ; -.
DR PDBsum; 3NS5; -.
DR PDBsum; 3NS6; -.
DR PDBsum; 3ZWL; -.
DR PDBsum; 4U1E; -.
DR PDBsum; 4U1F; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P06103; -.
DR SMR; P06103; -.
DR BioGRID; 34746; 205.
DR ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR DIP; DIP-2519N; -.
DR IntAct; P06103; 46.
DR MINT; P06103; -.
DR STRING; 4932.YOR361C; -.
DR iPTMnet; P06103; -.
DR MaxQB; P06103; -.
DR PaxDb; P06103; -.
DR PRIDE; P06103; -.
DR EnsemblFungi; YOR361C_mRNA; YOR361C; YOR361C.
DR GeneID; 854543; -.
DR KEGG; sce:YOR361C; -.
DR SGD; S000005888; PRT1.
DR VEuPathDB; FungiDB:YOR361C; -.
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_4_0_1; -.
DR InParanoid; P06103; -.
DR OMA; NVADCKI; -.
DR BioCyc; YEAST:G3O-33831-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR EvolutionaryTrace; P06103; -.
DR PRO; PR:P06103; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P06103; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:SGD.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IDA:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR14068; PTHR14068; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..763
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000123535"
FT DOMAIN 77..162
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 228..266
FT /note="WD 1"
FT REPEAT 277..325
FT /note="WD 2"
FT REPEAT 373..416
FT /note="WD 3"
FT REPEAT 484..524
FT /note="WD 4"
FT REPEAT 544..589
FT /note="WD 5"
FT REPEAT 605..650
FT /note="WD 6"
FT REGION 1..136
FT /note="Sufficient for interaction with HCR1 and TIF32"
FT /evidence="ECO:0000269|PubMed:16581774"
FT REGION 28..261
FT /note="Sufficient for interaction with PIC8"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 124..130
FT /note="KGFLFVE->AAAAAAA: Impairs interaction with HCR1 and
FT TIF32, impairs interaction of the eIF-3 complex with eIF-1,
FT eIF-2 and the 40S ribosome, and impairs initiation of
FT translation."
FT /evidence="ECO:0000269|PubMed:16581774"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3NS6"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3NS6"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:3NS6"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:3NS6"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3NS6"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:3NS6"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:3NS6"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3NS6"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3NS6"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3NS6"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4U1F"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:4U1F"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:4U1F"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:4U1F"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:4U1F"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:4U1F"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 435..443
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 447..457
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 464..472
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 480..484
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 519..527
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 538..547
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 558..565
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 575..580
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 611..615
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:4U1F"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 646..651
FT /evidence="ECO:0007829|PDB:4U1F"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:4U1F"
FT HELIX 694..728
FT /evidence="ECO:0007829|PDB:4U1E"
SQ SEQUENCE 763 AA; 88130 MW; F5E4E783408EE948 CRC64;
MKNFLPRTLK NIYELYFNNI SVHSIVSRNT QLKRSKIIQM TTETFEDIKL EDIPVDDIDF
SDLEEQYKVT EEFNFDQYIV VNGAPVIPSA KVPVLKKALT SLFSKAGKVV NMEFPIDEAT
GKTKGFLFVE CGSMNDAKKI IKSFHGKRLD LKHRLFLYTM KDVERYNSDD FDTEFREPDM
PTFVPSSSLK SWLMDDKVRD QFVLQDDVKT SVFWNSMFNE EDSLVESREN WSTNYVRFSP
KGTYLFSYHQ QGVTAWGGPN FDRLRRFYHP DVRNSSVSPN EKYLVTFSTE PIIVEEDNEF
SPFTKKNEGH QLCIWDIASG LLMATFPVIK SPYLKWPLVR WSYNDKYCAR MVGDSLIVHD
ATKNFMPLEA KALKPSGIRD FSFAPEGVKL QPFRNGDEPS VLLAYWTPET NNSACTATIA
EVPRGRVLKT VNLVQVSNVT LHWQNQAEFL CFNVERHTKS GKTQFSNLQI CRLTERDIPV
EKVELKDSVF EFGWEPHGNR FVTISVHEVA DMNYAIPANT IRFYAPETKE KTDVIKRWSL
VKEIPKTFAN TVSWSPAGRF VVVGALVGPN MRRSDLQFYD MDYPGEKNIN DNNDVSASLK
DVAHPTYSAA TNITWDPSGR YVTAWSSSLK HKVEHGYKIF NIAGNLVKED IIAGFKNFAW
RPRPASILSN AERKKVRKNL REWSAQFEEQ DAMEADTAMR DLILHQRELL KQWTEYREKI
GQEMEKSMNF KIFDVQPEDA SDDFTTIEEI VEEVLEETKE KVE
