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 27-MAR-2024, entry version 218. 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="https://atlasgeneticsoncology.org/gene/40425/EIF3A"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7QP6; EM; 4.70 A; u=1-1382. DR PDB; 7QP7; EM; 3.70 A; u=1-1382. DR PDB; 8PPL; EM; 2.65 A; Iu=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 PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 8PPL; -. DR AlphaFoldDB; Q14152; -. DR EMDB; EMD-10769; -. DR EMDB; EMD-10773; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-17805; -. DR SMR; Q14152; -. DR BioGRID; 114210; 325. DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex. DR CORUM; Q14152; -. DR DIP; DIP-31114N; -. DR IntAct; Q14152; 118. DR MINT; Q14152; -. DR STRING; 9606.ENSP00000358140; -. DR MoonProt; Q14152; -. DR GlyGen; Q14152; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q14152; -. DR MetOSite; Q14152; -. DR PhosphoSitePlus; Q14152; -. DR SwissPalm; Q14152; -. DR BioMuta; EIF3A; -. DR DMDM; 6685537; -. DR EPD; Q14152; -. DR jPOST; Q14152; -. DR MassIVE; Q14152; -. DR MaxQB; Q14152; -. DR PaxDb; 9606-ENSP00000358140; -. DR PeptideAtlas; Q14152; -. DR ProteomicsDB; 26155; -. DR ProteomicsDB; 59854; -. [Q14152-1] DR Pumba; Q14152; -. DR Antibodypedia; 32084; 322 antibodies from 33 providers. DR DNASU; 8661; -. DR Ensembl; ENST00000369144.8; ENSP00000358140.3; ENSG00000107581.14. [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 AGR; HGNC:3271; -. 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; EHITNKR; -. DR OrthoDB; 10990at2759; -. 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; 833 hits in 1165 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 216 other cell types or tissues. 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 Gene3D; 1.25.40.860; -; 2. DR Gene3D; 4.10.860.10; UVR domain; 1. DR HAMAP; MF_03000; eIF3a; 1. DR InterPro; IPR027512; EIF3A. DR InterPro; IPR000717; PCI_dom. DR PANTHER; PTHR14005:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A; 1. DR PANTHER; PTHR14005; EUKARYOTIC TRANSLATION INITIATION FACTOR 3, THETA SUBUNIT; 1. DR Pfam; PF01399; PCI; 1. DR SMART; SM00088; PINT; 1. DR PROSITE; PS50250; PCI; 1. DR UCD-2DPAGE; Q14152; -. DR Genevisible; Q14152; HS. 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 //