EIF3A_YEAST
ID EIF3A_YEAST Reviewed; 964 AA.
AC P38249; D6VQ78;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3a {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Eukaryotic translation initiation factor 3 110 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
DE Short=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=Translation initiation factor eIF3, p110 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03000};
GN Name=RPG1 {ECO:0000255|HAMAP-Rule:MF_03000}; Synonyms=TIF32;
GN OrderedLocusNames=YBR079C; ORFNames=YBR0734;
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 200060 / W303;
RX PubMed=10358023; DOI=10.1074/jbc.274.24.16802;
RA Vornlocher H.-P., Hanachi P., Ribeiro S., Hershey J.W.B.;
RT "A 110-kilodalton subunit of translation initiation factor eIF3 and an
RT associated 135-kilodalton protein are encoded by the Saccharomyces
RT cerevisiae TIF32 and TIF31 genes.";
RL J. Biol. Chem. 274:16802-16812(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 FUNCTION, AND INTERACTION WITH PRT1.
RX PubMed=9694884; DOI=10.1074/jbc.273.33.21253;
RA Valasek L., Trachsel H., Hasek J., Ruis H.;
RT "Rpg1, the Saccharomyces cerevisiae homologue of the largest subunit of
RT mammalian translation initiation factor 3, is required for translational
RT activity.";
RL J. Biol. Chem. 273:21253-21260(1998).
RN [6]
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 [7]
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 [8]
RP FUNCTION, ASSOCIATION WITH THE 40S RIBOSOME, AND INTERACTION WITH 18S RRNA
RP AND RPS0A.
RX PubMed=12651896; DOI=10.1101/gad.1065403;
RA Valasek L., Mathew A.A., Shin B.-S., Nielsen K.H., Szamecz B.,
RA Hinnebusch A.G.;
RT "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical
RT connections with the 40S ribosome in vivo.";
RL Genes Dev. 17:786-799(2003).
RN [9]
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 [10]
RP 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 [11]
RP INTERACTION WITH PRT1, AND ASSOCIATION WITH THE 40S RIBOSOME.
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691 AND THR-935, AND
RP 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 [13]
RP FUNCTION, AND MUTAGENESIS OF 692-LEU--ILE-701.
RX PubMed=18765792; DOI=10.1101/gad.480508;
RA Szamecz B., Rutkai E., Cuchalova L., Munzarova V., Herrmannova A.,
RA Nielsen K.H., Burela L., Hinnebusch A.G., Valasek L.;
RT "eIF3a cooperates with sequences 5' of uORF1 to promote resumption of
RT scanning by post-termination ribosomes for reinitiation on GCN4 mRNA.";
RL Genes Dev. 22:2414-2425(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, 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 [15]
RP IDENTIFICATION IN THE EIF-3 COMPLEX WITH NIP1; PRT1; 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 [16]
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_03000, ECO:0000269|PubMed:11387228,
CC ECO:0000269|PubMed:12651896, ECO:0000269|PubMed:18765792,
CC ECO:0000269|PubMed:9694884}.
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. TIF32, NIP1 and TIF-5/eIF-5 comprise a minimal 40S-ribosome-
CC binding unit. TIF32 interacts with 18S ribosomal RNA and RPS0A.
CC {ECO:0000269|PubMed:12651896, ECO:0000269|PubMed:16581774,
CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:9671501,
CC ECO:0000269|PubMed:9694884}.
CC -!- INTERACTION:
CC P38249; P32497: NIP1; NbExp=13; IntAct=EBI-8981, EBI-8965;
CC P38249; P06103: PRT1; NbExp=13; IntAct=EBI-8981, EBI-8973;
CC P38249; P40217: TIF34; NbExp=8; IntAct=EBI-8981, EBI-8951;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000}.
CC -!- MISCELLANEOUS: Present with 52700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
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DR EMBL; AF004912; AAB82416.1; -; Genomic_DNA.
DR EMBL; X76294; CAA53937.1; -; Genomic_DNA.
DR EMBL; Z35948; CAA85024.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07198.1; -; Genomic_DNA.
DR PIR; S45944; S45944.
DR RefSeq; NP_009635.1; NM_001178427.1.
DR PDB; 3JAP; EM; 4.90 A; o=1-495.
DR PDB; 4K51; X-ray; 2.65 A; A/B=276-494.
DR PDB; 4U1C; X-ray; 3.50 A; A=225-495.
DR PDB; 4U1D; X-ray; 3.30 A; A/B/C=1-494.
DR PDB; 4U1E; X-ray; 2.00 A; I=1-347.
DR PDB; 6FYX; EM; 3.05 A; o=1-964.
DR PDB; 6FYY; EM; 3.05 A; o=1-964.
DR PDB; 6GSM; EM; 5.15 A; o=5-492.
DR PDB; 6GSN; EM; 5.75 A; o=5-492.
DR PDB; 6ZCE; EM; 5.30 A; o=1-964.
DR PDB; 6ZU9; EM; 6.20 A; o=1-964.
DR PDBsum; 3JAP; -.
DR PDBsum; 4K51; -.
DR PDBsum; 4U1C; -.
DR PDBsum; 4U1D; -.
DR PDBsum; 4U1E; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P38249; -.
DR SMR; P38249; -.
DR BioGRID; 32781; 306.
DR ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR DIP; DIP-5870N; -.
DR IntAct; P38249; 38.
DR MINT; P38249; -.
DR STRING; 4932.YBR079C; -.
DR iPTMnet; P38249; -.
DR MaxQB; P38249; -.
DR PaxDb; P38249; -.
DR PRIDE; P38249; -.
DR EnsemblFungi; YBR079C_mRNA; YBR079C; YBR079C.
DR GeneID; 852371; -.
DR KEGG; sce:YBR079C; -.
DR SGD; S000000283; RPG1.
DR VEuPathDB; FungiDB:YBR079C; -.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_2_1_1; -.
DR InParanoid; P38249; -.
DR OMA; VMYQTTA; -.
DR BioCyc; YEAST:G3O-29047-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 PRO; PR:P38249; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38249; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:SGD.
DR GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IBA:GO_Central.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0002188; P:translation reinitiation; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..964
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000123544"
FT DOMAIN 321..496
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 503..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 625..668
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 702..734
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COILED 796..869
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 512..541
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 935
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MUTAGEN 692..701
FT /note="LDLDTIKQVI->AAAAAAAAAA: Reduces interaction of eIF-3
FT with the 40S ribosome."
FT /evidence="ECO:0000269|PubMed:18765792"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 49..61
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 83..106
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 152..169
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 176..192
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 196..216
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:4U1D"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 318..333
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 349..354
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 363..371
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 382..392
FT /evidence="ECO:0007829|PDB:4K51"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 400..411
FT /evidence="ECO:0007829|PDB:4K51"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 421..439
FT /evidence="ECO:0007829|PDB:4K51"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:4K51"
FT HELIX 462..474
FT /evidence="ECO:0007829|PDB:4K51"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:4U1D"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:4K51"
SQ SEQUENCE 964 AA; 110344 MW; 93EFFA6B2FC8286D CRC64;
MAPPPFRPEN AIKRADELIS VGEKQAALQS LHDFITARRI RWATPSTVEP VVFKFLEIGV
ELKKGKLLKD GLHQYKKLIQ GSTEGLVSVG AVARKFIDLV ESKIASEQTR ADELQKQEID
DDLEGGVTPE NLLISVYESD QSVAGFNDEA ITSWLRFTWE SYRAVLDLLR NNALLEITYS
GVVKKTMHFC LKYQRKNEFK RLAEMLRQHL DAANYQQSKS GNNLVDLSDA DTLQRYLDQR
FQQVDVSVKL ELWHEAYRSI EDVFHLMKIS KRAPKPSTLA NYYENLVKVF FVSGDPLLHT
TAWKKFYKLY STNPRATEEE FKTYSSTIFL SAISTQLDEI PSIGYDPHLR MYRLLNLDAK
PTRKEMLQSI IEDESIYGKV DEELKELYDI IEVNFDVDTV KQQLENLLVK LSSKTYFSQY
IAPLRDVIMR RVFVAASQKF TTVSQSELYK LATLPAPLDL SAWDIEKSLL QAAVEDYVSI
TIDHESAKVT FAKDPFDIFA STASKEVSEE ENTEPEVQEE KEETDEALGP QETEDGEEKE
EESDPVIIRN SYIHNKLLEL SNVLHDVDSF NNASYMEKVR IARETLIKKN KDDLEKISKI
VDERVKRSQE QKQKHMEHAA LHAEQDAEVR QQRILEEKAA IEAKLEEEAH RRLIEKKKRE
FEAIKEREIT KMITEVNAKG HVYIDPNEAK SLDLDTIKQV IIAEVSKNKS ELESRMEYAM
KKLDHTERAL RKVELPLLQK EVDKLQETDT ANYEAMKKKI VDAAKAEYEA RMADRKNLVM
VYDDYLKFKE HVSGTKESEL AAIRNQKKAE LEAAKKARIE EVRKRRYEEA IARRKEEIAN
AERQKRAQEL AEATRKQREI EEAAAKKSTP YSFRAGNREP PSTPSTLPKA TVSPDKAKLD
MIAQKQREME EAIEQRLAGR TAGGSSPATP ATPATPATPT PSSGPKKMTM AEKLRAKRLA
KGGR
