EIF3A_HUMAN
ID EIF3A_HUMAN Reviewed; 1382 AA.
AC Q14152; B1AMV5; B4DYS1; F5H335; O00653; Q15778;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 209.
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 subunit 10 {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=eIF-3-theta {ECO:0000255|HAMAP-Rule:MF_03000};
DE AltName: Full=eIF3 p167;
DE AltName: Full=eIF3 p180;
DE AltName: Full=eIF3 p185;
GN Name=EIF3A {ECO:0000255|HAMAP-Rule:MF_03000};
GN Synonyms=EIF3S10 {ECO:0000255|HAMAP-Rule:MF_03000}, KIAA0139;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Lymphoblastoma;
RX PubMed=9150439; DOI=10.1089/dna.1997.16.515;
RA Scholler J.K., Kanner S.B.;
RT "The human p167 gene encodes a unique structural protein that contains
RT centrosomin A homology and associates with a multicomponent complex.";
RL DNA Cell Biol. 16:515-531(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Keratinocyte, and Liver;
RX PubMed=9054404; DOI=10.1074/jbc.272.11.7106;
RA Johnson K.R., Merrick W.C., Zoll W.L., Zhu Y.;
RT "Identification of cDNA clones for the large subunit of eukaryotic
RT translation initiation factor 3. Comparison of homologues from human,
RT Nicotiana tabacum, Caenorhabditis elegans, and Saccharomyces cerevisiae.";
RL J. Biol. Chem. 272:7106-7113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Myelomonocyte;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LYS-386.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 2-13; 15-36; 69-75; 85-91; 144-151; 173-183; 252-264;
RP 279-298; 309-317; 322-335; 341-351; 368-388; 439-469; 490-546; 582-589;
RP 624-632; 694-711; 719-740; 776-782; 817-824; 838-847; 850-856; 862-868;
RP 877-885; 1071-1080; 1122-1130; 1142-1150 AND 1358-1366, CLEAVAGE OF
RP INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma, and Mammary carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Matallanas D., Cooper W.N.,
RA Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP FUNCTION, AND INTERACTION WITH EIF3B AND KRT7.
RX PubMed=11169732;
RX DOI=10.1002/1097-4644(20010315)80:4<483::aid-jcb1002>3.0.co;2-b;
RA Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.;
RT "Molecular interaction between human tumor marker protein p150, the largest
RT subunit of eIF3, and intermediate filament protein K7.";
RL J. Cell. Biochem. 80:483-490(2001).
RN [9]
RP INTERACTION WITH EIF3B.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [10]
RP INTERACTION WITH EIF3B.
RX PubMed=14688252; DOI=10.1074/jbc.m312745200;
RA Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
RA Hershey J.W.B.;
RT "The j-subunit of human translation initiation factor eIF3 is required for
RT the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits
RT in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [11]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [12]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.m605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [13]
RP FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [14]
RP INTERACTION WITH EIF3E.
RX PubMed=17468741; DOI=10.1038/sj.embor.7400955;
RA Morris C., Wittmann J., Jaeck H.-M., Jalinot P.;
RT "Human INT6/eIF3e is required for nonsense-mediated mRNA decay.";
RL EMBO Rep. 8:596-602(2007).
RN [15]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=18056426; DOI=10.1101/gad.439507;
RA Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
RT "The mechanism of an exceptional case of reinitiation after translation of
RT a long ORF reveals why such events do not generally occur in mammalian mRNA
RT translation.";
RL Genes Dev. 21:3149-3162(2007).
RN [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-881; SER-1198;
RP SER-1336 AND SER-1364, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492; SER-584; SER-881;
RP SER-882; SER-895; SER-949; SER-1028; SER-1188; SER-1198; SER-1262 AND
RP SER-1336, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=23766293; DOI=10.1093/nar/gkt510;
RA Sun C., Querol-Audi J., Mortimer S.A., Arias-Palomo E., Doudna J.A.,
RA Nogales E., Cate J.H.;
RT "Two RNA-binding motifs in eIF3 direct HCV IRES-dependent translation.";
RL Nucleic Acids Res. 41:7512-7521(2013).
RN [25]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=24357634; DOI=10.1002/embj.201386124;
RA Sweeney T.R., Abaeva I.S., Pestova T.V., Hellen C.U.;
RT "The mechanism of translation initiation on Type 1 picornavirus IRESs.";
RL EMBO J. 33:76-92(2014).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, AND RNA-BINDING.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [30]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis (PubMed:17581632,
CC PubMed:25849773). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17581632, PubMed:11169732). The
CC eIF-3 complex specifically targets and initiates translation of a
CC subset of mRNAs involved in cell proliferation, including cell cycling,
CC differentiation and apoptosis, and uses different modes of RNA stem-
CC loop binding to exert either translational activation or repression
CC (PubMed:25849773, PubMed:27462815). {ECO:0000255|HAMAP-Rule:MF_03000,
CC ECO:0000269|PubMed:11169732, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- FUNCTION: (Microbial infection) Essential for the initiation of
CC translation on type-1 viral ribosomal entry sites (IRESs), like for
CC HCV, PV, EV71 or BEV translation (PubMed:23766293, PubMed:24357634).
CC {ECO:0000269|PubMed:23766293, ECO:0000269|PubMed:24357634}.
CC -!- FUNCTION: (Microbial infection) In case of FCV infection, plays a role
CC in the ribosomal termination-reinitiation event leading to the
CC translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
CC -!- SUBUNIT: Interacts with EIF4G1 (By similarity). Component of the
CC eukaryotic translation initiation factor 3 (eIF-3) complex, which is
CC composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F,
CC EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex
CC appears to include 3 stable modules: module A is composed of EIF3A,
CC EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and
CC EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3L and
CC EIF3K. EIF3C of module C binds EIF3B of module A and EIF3H of module B,
CC thereby linking the three modules. EIF3J is a labile subunit that binds
CC to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with
CC RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of
CC EIF4B to eIF-3. Also interacts with KRT7 and PIWIL2. {ECO:0000250,
CC ECO:0000269|PubMed:11169732, ECO:0000269|PubMed:14519125,
CC ECO:0000269|PubMed:14688252, ECO:0000269|PubMed:16766523,
CC ECO:0000269|PubMed:17322308, ECO:0000269|PubMed:17468741,
CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773}.
CC -!- INTERACTION:
CC Q14152; P41567: EIF1; NbExp=2; IntAct=EBI-366617, EBI-726200;
CC Q14152; P47813: EIF1AX; NbExp=2; IntAct=EBI-366617, EBI-1045377;
CC Q14152; P55884: EIF3B; NbExp=9; IntAct=EBI-366617, EBI-366696;
CC Q14152; Q99613: EIF3C; NbExp=14; IntAct=EBI-366617, EBI-353741;
CC Q14152; P08729: KRT7; NbExp=3; IntAct=EBI-366617, EBI-297833;
CC Q14152; Q04864: REL; NbExp=3; IntAct=EBI-366617, EBI-307352;
CC Q14152; Q92900-2: UPF1; NbExp=5; IntAct=EBI-366617, EBI-373492;
CC Q14152; Q9DCH4: Eif3f; Xeno; NbExp=4; IntAct=EBI-366617, EBI-1634316;
CC Q14152; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-366617, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03000,
CC ECO:0000269|PubMed:9150439}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14152-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14152-2; Sequence=VSP_055471;
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03000,
CC ECO:0000269|PubMed:17322308}.
CC -!- MASS SPECTROMETRY: Mass=166758.3; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit A family. {ECO:0000255|HAMAP-
CC Rule:MF_03000}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09488.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EIF3AID40425ch10q26.html";
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DR EMBL; U58046; AAB41584.1; -; mRNA.
DR EMBL; U58047; AAB41586.1; -; Genomic_DNA.
DR EMBL; U78311; AAB80695.1; -; mRNA.
DR EMBL; D50929; BAA09488.2; ALT_INIT; mRNA.
DR EMBL; AK302575; BAG63833.1; -; mRNA.
DR EMBL; AL355598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49408.1; -; Genomic_DNA.
DR CCDS; CCDS7608.1; -. [Q14152-1]
DR RefSeq; NP_003741.1; NM_003750.2. [Q14152-1]
DR PDB; 3J8B; EM; -; A=1-494.
DR PDB; 3J8C; EM; -; A=1-494.
DR PDB; 6YBD; EM; 3.30 A; u=1-1382.
DR PDB; 6YBT; EM; 6.00 A; u=33-1382.
DR PDB; 6ZMW; EM; 3.70 A; u=1-1382.
DR PDB; 6ZON; EM; 3.00 A; A=1-601.
DR PDB; 6ZP4; EM; 2.90 A; A=1-1382.
DR PDB; 6ZVJ; EM; 3.80 A; A=4-725.
DR PDB; 7A09; EM; 3.50 A; A=1-1382.
DR PDBsum; 3J8B; -.
DR PDBsum; 3J8C; -.
DR PDBsum; 6YBD; -.
DR PDBsum; 6YBT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; Q14152; -.
DR SMR; Q14152; -.
DR BioGRID; 114210; 225.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; Q14152; -.
DR DIP; DIP-31114N; -.
DR IntAct; Q14152; 114.
DR MINT; Q14152; -.
DR STRING; 9606.ENSP00000358140; -.
DR MoonProt; Q14152; -.
DR GlyGen; Q14152; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14152; -.
DR MetOSite; Q14152; -.
DR PhosphoSitePlus; Q14152; -.
DR SwissPalm; Q14152; -.
DR BioMuta; EIF3A; -.
DR DMDM; 6685537; -.
DR UCD-2DPAGE; Q14152; -.
DR EPD; Q14152; -.
DR jPOST; Q14152; -.
DR MassIVE; Q14152; -.
DR MaxQB; Q14152; -.
DR PaxDb; Q14152; -.
DR PeptideAtlas; Q14152; -.
DR PRIDE; Q14152; -.
DR ProteomicsDB; 26155; -.
DR ProteomicsDB; 59854; -. [Q14152-1]
DR Antibodypedia; 32084; 294 antibodies from 33 providers.
DR DNASU; 8661; -.
DR Ensembl; ENST00000369144.8; ENSP00000358140.3; ENSG00000107581.13. [Q14152-1]
DR Ensembl; ENST00000541549.2; ENSP00000438178.2; ENSG00000107581.13. [Q14152-1]
DR GeneID; 8661; -.
DR KEGG; hsa:8661; -.
DR MANE-Select; ENST00000369144.8; ENSP00000358140.3; NM_003750.4; NP_003741.1.
DR UCSC; uc001ldu.4; human. [Q14152-1]
DR CTD; 8661; -.
DR DisGeNET; 8661; -.
DR GeneCards; EIF3A; -.
DR HGNC; HGNC:3271; EIF3A.
DR HPA; ENSG00000107581; Low tissue specificity.
DR MIM; 602039; gene.
DR neXtProt; NX_Q14152; -.
DR OpenTargets; ENSG00000107581; -.
DR PharmGKB; PA27699; -.
DR VEuPathDB; HostDB:ENSG00000107581; -.
DR eggNOG; KOG2072; Eukaryota.
DR GeneTree; ENSGT00730000111063; -.
DR HOGENOM; CLU_002096_1_1_1; -.
DR InParanoid; Q14152; -.
DR OMA; VMYQTTA; -.
DR OrthoDB; 967904at2759; -.
DR PhylomeDB; Q14152; -.
DR TreeFam; TF101522; -.
DR PathwayCommons; Q14152; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; Q14152; -.
DR SIGNOR; Q14152; -.
DR BioGRID-ORCS; 8661; 800 hits in 1087 CRISPR screens.
DR ChiTaRS; EIF3A; human.
DR GeneWiki; EIF3A; -.
DR GenomeRNAi; 8661; -.
DR Pharos; Q14152; Tbio.
DR PRO; PR:Q14152; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q14152; protein.
DR Bgee; ENSG00000107581; Expressed in tendon of biceps brachii and 214 other tissues.
DR Genevisible; Q14152; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:UniProtKB.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IDA:UniProtKB.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IC:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
DR HAMAP; MF_03000; eIF3a; 1.
DR InterPro; IPR027512; EIF3A.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR14005; PTHR14005; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Initiation factor;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.7"
FT CHAIN 2..1382
FT /note="Eukaryotic translation initiation factor 3 subunit
FT A"
FT /id="PRO_0000123537"
FT DOMAIN 315..498
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REPEAT 925..934
FT /note="1"
FT REPEAT 935..942
FT /note="2; truncated"
FT REPEAT 943..952
FT /note="3"
FT REPEAT 953..962
FT /note="4"
FT REPEAT 963..972
FT /note="5"
FT REPEAT 973..982
FT /note="6"
FT REPEAT 983..992
FT /note="7"
FT REPEAT 993..1002
FT /note="8"
FT REPEAT 1003..1012
FT /note="9"
FT REPEAT 1013..1022
FT /note="10"
FT REPEAT 1023..1032
FT /note="11"
FT REPEAT 1033..1042
FT /note="12"
FT REPEAT 1043..1052
FT /note="13"
FT REPEAT 1054..1063
FT /note="14"
FT REPEAT 1064..1073
FT /note="15"
FT REPEAT 1074..1083
FT /note="16"
FT REPEAT 1084..1093
FT /note="17"
FT REPEAT 1094..1103
FT /note="18"
FT REPEAT 1104..1113
FT /note="19"
FT REPEAT 1114..1123
FT /note="20"
FT REPEAT 1124..1133
FT /note="21"
FT REPEAT 1134..1143
FT /note="22"
FT REPEAT 1144..1152
FT /note="23; truncated"
FT REPEAT 1153..1162
FT /note="24"
FT REPEAT 1163..1172
FT /note="25; approximate"
FT REGION 664..835
FT /note="Interaction with EIF3B"
FT REGION 810..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..1172
FT /note="25 X 10 AA approximate tandem repeats of [DE]-[DE]-
FT [DE]-R-[SEVGFPILV]-[HPSN]-[RSW]-[RL]-[DRGTIHN]-[EPMANLGDT]"
FT COILED 82..120
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000"
FT COMPBIAS 866..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:23186163"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 895
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1028
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1198
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:23186163"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:23186163"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03000,
FT ECO:0000269|PubMed:17322308"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055471"
FT VARIANT 386
FT /note="E -> K (in dbSNP:rs967185)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024438"
FT VARIANT 694
FT /note="K -> N (in dbSNP:rs431898)"
FT /id="VAR_048921"
FT VARIANT 993
FT /note="D -> E (in dbSNP:rs532138)"
FT /id="VAR_048922"
FT CONFLICT 520
FT /note="R -> G (in Ref. 4; BAG63833)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="D -> G (in Ref. 4; BAG63833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1272
FT /note="D -> G (in Ref. 4; BAG63833)"
FT /evidence="ECO:0000305"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 16..22
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 84..102
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 124..128
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 147..162
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 171..187
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 223..241
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 289..306
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 367..370
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 390..395
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 429..443
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 464..475
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 526..535
FT /evidence="ECO:0007829|PDB:6YBD"
FT TURN 536..539
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 540..559
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:6YBD"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:6YBD"
SQ SEQUENCE 1382 AA; 166569 MW; 485C01B28D67EBBA CRC64;
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD
LRKSHLAKEG LYQYKNICQQ VNIKSLEDVV RAYLKMAEEK TEAAKEESQQ MVLDIEDLDN
IQTPESVLLS AVSGEDTQDR TDRLLLTPWV KFLWESYRQC LDLLRNNSRV ERLYHDIAQQ
AFKFCLQYTR KAEFRKLCDN LRMHLSQIQR HHNQSTAINL NNPESQSMHL ETRLVQLDSA
ISMELWQEAF KAVEDIHGLF SLSKKPPKPQ LMANYYNKVS TVFWKSGNAL FHASTLHRLY
HLSREMRKNL TQDEMQRMST RVLLATLSIP ITPERTDIAR LLDMDGIIVE KQRRLATLLG
LQAPPTRIGL INDMVRFNVL QYVVPEVKDL YNWLEVEFNP LKLCERVTKV LNWVREQPEK
EPELQQYVPQ LQNNTILRLL QQVSQIYQSI EFSRLTSLVP FVDAFQLERA IVDAARHCDL
QVRIDHTSRT LSFGSDLNYA TREDAPIGPH LQSMPSEQIR NQLTAMSSVL AKALEVIKPA
HILQEKEEQH QLAVTAYLKN SRKEHQRILA RRQTIEERKE RLESLNIQRE KEELEQREAE
LQKVRKAEEE RLRQEAKERE KERILQEHEQ IKKKTVRERL EQIKKTELGA KAFKDIDIED
LEELDPDFIM AKQVEQLEKE KKELQERLKN QEKKIDYFER AKRLEEIPLI KSAYEEQRIK
DMDLWEQQEE ERITTMQLER EKALEHKNRM SRMLEDRDLF VMRLKAARQS VYEEKLKQFE
ERLAEERHNR LEERKRQRKE ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE
LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSRW GDRDSEGTWR
KGPEADSEWR RGPPEKEWRR GEGRDEDRSH RRDEERPRRL GDDEDREPSL RPDDDRVPRR
GMDDDRGPRR GPEEDRFSRR GADDDRPSWR NTDDDRPPRR IADEDRGNWR HADDDRPPRR
GLDEDRGSWR TADEDRGPRR GMDDDRGPRR GGADDERSSW RNADDDRGPR RGLDDDRGPR
RGMDDDRGPR RGMDDDRGPR RGMDDDRGPR RGLDDDRGPW RNADDDRIPR RGAEDDRGPW
RNMDDDRLSR RADDDRFPRR GDDSRPGPWR PLVKPGGWRE KEKAREESWG PPRESRPSEE
REWDREKERD RDNQDREEND KDPERERDRE RDVDREDRFR RPRDEGGWRR GPAEESSSWR
DSSRRDDRDR DDRRRERDDR RDLRERRDLR DDRDRRGPPL RSEREEVSSW RRADDRKDDR
VEERDPPRRV PPPALSRDRE RDRDREREGE KEKASWRAEK DRESLRRTKN ETDEDGWTTV
RR
