NM_198241 5463 1 5 1 PRI 27-NOV-2005 07-NOV-2003 Homo sapiens eukaryotic translation initiation factor 4 gamma, 1 (EIF4G1), transcript variant 2, mRNA NM_198241 NM_198241.1 ref|NM_198241.1| gi|38201622 Homo sapiens (human) Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; Homo 1 (bases 1 to 5463) Marintchev,A. Wagner,G. eIF4G and CBP80 share a common origin and similar domain organization: implications for the structure and function of eIF4G Biochemistry 44 (37), 12265-12272 (2005) 16156639 GeneRIF: The organization of the CBP80-CBP20 complex suggests how the activity of eIF4G in translation initiation could be regulated through a dynamic network of overlapping intra- and intermolecular interactions. 2 (bases 1 to 5463) Gorrini,C. Loreni,F. Gandin,V. Sala,L.A. Sonenberg,N. Marchisio,P.C. Biffo,S. Fibronectin controls cap-dependent translation through beta1 integrin and eukaryotic initiation factors 4 and 2 coordinated pathways Proc. Natl. Acad. Sci. U.S.A. 102 (26), 9200-9205 (2005) 15961545 GeneRIF: FN has a role in controlling translation through beta1 integrin and eukaryotic initiation factors 4 and 2 coordinated pathways 3 (bases 1 to 5463) Byrd,M.P. Zamora,M. Lloyd,R.E. Translation of eukaryotic translation initiation factor 4GI (eIF4GI) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection J. Biol. Chem. 280 (19), 18610-18622 (2005) 15755734 GeneRIF: intact eIF4GI protein is not required for the de novo synthesis of eIF4GI, suggesting its expression can continue under stress or infection conditions where eIF4GI is cleaved 4 (bases 1 to 5463) Foeger,N. Kuehnel,E. Cencic,R. Skern,T. The binding of foot-and-mouth disease virus leader proteinase to eIF4GI involves conserved ionic interactions FEBS J. 272 (10), 2602-2611 (2005) 15885108 GeneRIF: Results identify two conserved basic residues (K646 and R650) in human eukaryotic initiation factor 4GI (eIF4GI) that are important for foot-and-mouth disease virus leader proteinase binding. 5 (bases 1 to 5463) Kudchodkar,S.B. Yu,Y. Maguire,T.G. Alwine,J.C. Human cytomegalovirus infection induces rapamycin-insensitive phosphorylation of downstream effectors of mTOR kinase J. Virol. 78 (20), 11030-11039 (2004) 15452223 GeneRIF: phoshorylation induced by human Cytomegalovirus infections is both mTOR and phosphatidylinositol kinase independent. 6 (bases 1 to 5463) Orton,K.C. Ling,J. Waskiewicz,A.J. Cooper,J.A. Merrick,W.C. Korneeva,N.L. Rhoads,R.E. Sonenberg,N. Traugh,J.A. Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk J. Biol. Chem. 279 (37), 38649-38657 (2004) 15234964 GeneRIF: eIF4G binding to Mnk is inhibted by Mnk1 phosphorylation by caspase-activated Pak2/gamma-PAK 7 (bases 1 to 5463) Beausoleil,S.A. Jedrychowski,M. Schwartz,D. Elias,J.E. Villen,J. Li,J. Cohn,M.A. Cantley,L.C. Gygi,S.P. Large-scale characterization of HeLa cell nuclear phosphoproteins Proc. Natl. Acad. Sci. U.S.A. 101 (33), 12130-12135 (2004) 15302935 8 (bases 1 to 5463) Xi,Q. Cuesta,R. Schneider,R.J. Tethering of eIF4G to adenoviral mRNAs by viral 100k protein drives ribosome shunting Genes Dev. 18 (16), 1997-2009 (2004) 15314025 GeneRIF: role of binding to adenoviral mRNA in ribosome shunting 9 (bases 1 to 5463) Cuesta,R. Xi,Q. Schneider,R.J. Structural basis for competitive inhibition of eIF4G-Mnk1 interaction by the adenovirus 100-kilodalton protein J. Virol. 78 (14), 7707-7716 (2004) 15220445 GeneRIF: Adenovirus 100K protein blocks cellular protein synthesis by coopting eIF4G and cap-initiation complexes and displacing or blocking binding by Mnk1, which occurs only on preassembled complexes, resulting in dephosphorylation of eIF4E. 10 (bases 1 to 5463) Avdulov,S. Li,S. Michalek,V. Burrichter,D. Peterson,M. Perlman,D.M. Manivel,J.C. Sonenberg,N. Yee,D. Bitterman,P.B. Polunovsky,V.A. Activation of translation complex eIF4F is essential for the genesis and maintenance of the malignant phenotype in human mammary epithelial cells Cancer Cell 5 (6), 553-563 (2004) 15193258 GeneRIF: eIF4F activation is an essential component of the malignant phenotype in breast carcinoma 11 (bases 1 to 5463) Coldwell,M.J. Hashemzadeh-Bonehi,L. Hinton,T.M. Morley,S.J. Pain,V.M. Expression of fragments of translation initiation factor eIF4GI reveals a nuclear localisation signal within the N-terminal apoptotic cleavage fragment N-FAG J. Cell. Sci. 117 (PT 12), 2545-2555 (2004) 15128869 GeneRIF: Expression of fragments of eIF4GI reveals a nuclear localization sequence within the N-terminal apoptotic cleavage fragment N-FAG. 12 (bases 1 to 5463) Vitour,D. Lindenbaum,P. Vende,P. Becker,M.M. Poncet,D. RoXaN, a novel cellular protein containing TPR, LD, and zinc finger motifs, forms a ternary complex with eukaryotic initiation factor 4G and rotavirus NSP3 J. Virol. 78 (8), 3851-3862 (2004) 15047801 GeneRIF: RoXaN is capable of interacting with NSP3 and eIF4G I in vivo and during rotavirus infection. Domains of interaction were mapped. 13 (bases 1 to 5463) Robalino,J. Joshi,B. Fahrenkrug,S.C. Jagus,R. Two zebrafish eIF4E family members are differentially expressed and functionally divergent J. Biol. Chem. 279 (11), 10532-10541 (2004) 14701818 14 (bases 1 to 5463) Thompson,S.R. Sarnow,P. Enterovirus 71 contains a type I IRES element that functions when eukaryotic initiation factor eIF4G is cleaved Virology 315 (1), 259-266 (2003) 14592777 GeneRIF: cleavage of EIF4G by Coxsackievirus 2A protease enhances the translation efficiency of EV71 IRES activity 15 (bases 1 to 5463) Hashemzadeh-Bonehi,L. Curtis,P.S. Morley,S.J. Thorpe,J.R. Pain,V.M. Overproduction of a conserved domain of fission yeast and mammalian translation initiation factor eIF4G causes aberrant cell morphology and results in disruption of the localization of F-actin and the organization of microtubules Genes Cells 8 (2), 163-178 (2003) 12581158 GeneRIF: Overexpression of EIF4G1 causes aberrant cell morphology and results in disruption of the localization of F-actin and the organization of microtubules. 16 (bases 1 to 5463) Perales,C. Carrasco,L. Ventoso,I. Cleavage of eIF4G by HIV-1 protease: effects on translation FEBS Lett. 533 (1-3), 89-94 (2003) 12505164 GeneRIF: proteolytic activity of HIV-1 protease on eIF4GI and eIF4GII and its implications for the translation of mRNAs 17 (bases 1 to 5463) Connor,J.H. Lyles,D.S. Vesicular stomatitis virus infection alters the eIF4F translation initiation complex and causes dephosphorylation of the eIF4E binding protein 4E-BP1 J. Virol. 76 (20), 10177-10187 (2002) 12239292 GeneRIF: Vesicular stomatitis virus infection alters the eIF4F translation initiation complex and causes dephosphorylation of the eIF4E binding protein 4E-BP1 18 (bases 1 to 5463) Groft,C.M. Burley,S.K. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization Mol. Cell 9 (6), 1273-1283 (2002) 12086624 GeneRIF: X-ray structure of rotavirus NSP3-C bound to the 30 residue fragment of eIF4G that is also recognized by poly(A) binding protein (PABP) 19 (bases 1 to 5463) Bradley,C.A. Padovan,J.C. Thompson,T.L. Benoit,C.A. Chait,B.T. Rhoads,R.E. Mass spectrometric analysis of the N terminus of translational initiation factor eIF4G-1 reveals novel isoforms J. Biol. Chem. 277 (15), 12559-12571 (2002) 11821405 GeneRIF: mass spectrometric analysis of N terminus reveals novel isoforms 20 (bases 1 to 5463) Wakiyama,M. Miura,K. Inhibition of translation and progesterone-induced maturation of Xenopus oocytes by expressing the amino-terminal portion of the eukaryotic translation initiation factor 4G Biosci. Biotechnol. Biochem. 66 (1), 185-187 (2002) 11866104 GeneRIF: demonstrate that the expression of the amino-terminal one-third of eIF4G, which interacts with eIF4E and PABP, in Xenopus oocyte inhibits translation and progesterone-induced maturation 21 (bases 1 to 5463) Cuesta,R. Xi,Q. Schneider,R.J. Adenovirus-specific translation by displacement of kinase Mnk1 from cap-initiation complex eIF4F EMBO J. 19 (13), 3465-3474 (2000) 10880459 22 (bases 1 to 5463) Vary,T.C. Jefferson,L.S. Kimball,S.R. Amino acid-induced stimulation of translation initiation in rat skeletal muscle Am. J. Physiol. 277 (6 PT 1), E1077-E1086 (1999) 10600798 23 (bases 1 to 5463) Laroia,G. Cuesta,R. Brewer,G. Schneider,R.J. Control of mRNA decay by heat shock-ubiquitin-proteasome pathway Science 284 (5413), 499-502 (1999) 10205060 24 (bases 1 to 5463) Pyronnet,S. Imataka,H. Gingras,A.C. Fukunaga,R. Hunter,T. Sonenberg,N. Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E EMBO J. 18 (1), 270-279 (1999) 9878069 25 (bases 1 to 5463) Imataka,H. Gradi,A. Sonenberg,N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation EMBO J. 17 (24), 7480-7489 (1998) 9857202 26 (bases 1 to 5463) Gradi,A. Imataka,H. Svitkin,Y.V. Rom,E. Raught,B. Morino,S. Sonenberg,N. A novel functional human eukaryotic translation initiation factor 4G Mol. Cell. Biol. 18 (1), 334-342 (1998) 9418880 27 (bases 1 to 5463) Imataka,H. Sonenberg,N. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A Mol. Cell. Biol. 17 (12), 6940-6947 (1997) 9372926 28 (bases 1 to 5463) Eberle,J. Krasagakis,K. Orfanos,C.E. Translation initiation factor eIF-4A1 mRNA is consistently overexpressed in human melanoma cells in vitro Int. J. Cancer 71 (3), 396-401 (1997) 9139875 29 (bases 1 to 5463) Brass,N. Heckel,D. Sahin,U. Pfreundschuh,M. Sybrecht,G.W. Meese,E. Translation initiation factor eIF-4gamma is encoded by an amplified gene and induces an immune response in squamous cell lung carcinoma Hum. Mol. Genet. 6 (1), 33-39 (1997) 9002667 30 (bases 1 to 5463) Lamphear,B.J. Rhoads,R.E. A single amino acid change in protein synthesis initiation factor 4G renders cap-dependent translation resistant to picornaviral 2A proteases Biochemistry 35 (49), 15726-15733 (1996) 8961935 31 (bases 1 to 5463) Yan,R. Rhoads,R.E. Human protein synthesis initiation factor eIF-4 gamma is encoded by a single gene (EIF4G) that maps to chromosome 3q27-qter Genomics 26 (2), 394-398 (1995) 7601469 32 (bases 1 to 5463) Yan,R. Rychlik,W. Etchison,D. Rhoads,R.E. Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma J. Biol. Chem. 267 (32), 23226-23231 (1992) 1429670 REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from AY082886.1, AK096719.1, BX647812.1, AF104913.1, BU683097.1 and BU944064.1.; Summary: The protein encoded by this gene is a component of the protein complex EIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure, and recruitment of mRNA to the ribosome. Alternative splicing results in five transcript variants encoding four distinct isoforms.; Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Variants 1 and 2 encode the same isoform (1).; COMPLETENESS: complete on the 3' end. source 1..5463 organism Homo sapiens mol_type mRNA db_xref taxon:9606 chromosome 3 map 3q27-qter gene 1..5463 1 5463 NM_198241.1 gene EIF4G1 note synonyms: p220, EIF4F, EIF4G, DKFZp686A1451 db_xref GeneID:1981 db_xref HGNC:3296 db_xref MIM:600495 CDS 199..4998 199 4998 NM_198241.1 gene EIF4G1 note isoform 1 is encoded by transcript variant 2; EIF4-gamma; go_component: eukaryotic translation initiation factor 4F complex [goid 0016281] [evidence TAS] [pmid 9857202]; go_function: RNA binding [goid 0003723] [evidence IEA]; go_function: protein binding [goid 0005515] [evidence IPI] [pmid 14701818]; go_function: translation initiation factor activity [goid 0003743] [evidence IEA]; go_function: translation initiation factor activity [goid 0003743] [evidence TAS] [pmid 8961935]; go_function: translation initiation factor activity [goid 0003743] [evidence TAS] [pmid 9372926]; go_process: regulation of translational initiation [goid 0006446] [evidence IEA]; go_process: regulation of translational initiation [goid 0006446] [evidence NAS] [pmid 8961935]; go_process: regulation of translational initiation [goid 0006446] [evidence NAS] [pmid 9372926] codon_start 1 transl_table 1 product eukaryotic translation initiation factor 4 gamma, 1 isoform 1 protein_id NP_937884.1 db_xref GI:38201623 db_xref CCDS:CCDS3259.1 db_xref GeneID:1981 db_xref HGNC:3296 db_xref MIM:600495 translation MNKAPQSTGPPPAPSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQHFYPSRAQPPSSAASRVQSAAPARPGPAAHVYPAGSQVMMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPAPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN STS 2537..3166 2537 3166 NM_198241.1 gene EIF4G1 standard_name GDB:593083 db_xref UniSTS:157934 STS 4822..5110 4822 5110 NM_198241.1 gene EIF4G1 standard_name RH79680 db_xref UniSTS:84472 STS 4875..5432 4875 5432 NM_198241.1 gene EIF4G1 standard_name EIF4G1_3109 db_xref UniSTS:462180 STS 5101..5330 5101 5330 NM_198241.1 gene EIF4G1 standard_name RH68199 db_xref UniSTS:33666 polyA_signal 5423..5428 5423 5428 NM_198241.1 gene EIF4G1 polyA_site 5439 5439 NM_198241.1 gene EIF4G1 polyA_site 5448 5448 NM_198241.1 gene EIF4G1 GAAGCGGTGGCCGCCGAGCGGGATCTGTGCGGGGAGCCGGAAATGGTTGTGGACTACGTCTGTGCGGCTGCGTGGGGCTCGGCCGCGCGGACTGAAGGAGACTGAAGGCCCTCGGATGCCCAGAACCTGTAGGCCGCACCGTGGACTTGTTCTTAATCGAGGGGGTGCTGGGGGGACCCTGATGTGGCACCAAATGAAATGAACAAAGCTCCACAGTCCACAGGCCCCCCACCCGCCCCATCCCCCGGACTCCCACAGCCAGCGTTTCCCCCGGGGCAGACAGCGCCGGTGGTGTTCAGTACGCCACAAGCGACACAAATGAACACGCCTTCTCAGCCCCGCCAGCACTTCTACCCTAGCCGGGCCCAGCCCCCGAGCAGTGCAGCCTCCCGAGTGCAGAGTGCAGCCCCTGCCCGCCCTGGCCCAGCTGCCCATGTCTACCCTGCTGGATCCCAAGTAATGATGATCCCTTCCCAGATCTCCTACCCAGCCTCCCAGGGGGCCTACTACATCCCTGGACAGGGGCGTTCCACATACGTTGTCCCGACACAGCAGTACCCTGTGCAGCCAGGAGCCCCAGGCTTCTATCCAGGTGCAAGCCCTACAGAATTTGGGACCTACGCTGGCGCCTACTATCCAGCCCAAGGGGTGCAGCAGTTTCCCACTGGCGTGGCCCCCGCCCCAGTTTTGATGAACCAGCCACCCCAGATTGCTCCCAAGAGGGAGCGTAAGACGATCCGAATTCGAGATCCAAACCAAGGAGGAAAGGATATCACAGAGGAGATCATGTCTGGGGCCCGCACTGCCTCCACACCCACCCCTCCCCAGACGGGAGGCGGTCTGGAGCCTCAAGCTAATGGGGAGACGCCCCAGGTTGCTGTCATTGTCCGGCCAGATGACCGGTCACAGGGAGCAATCATTGCTGACCGGCCAGGGCTGCCTGGCCCAGAGCATAGCCCTTCAGAATCCCAGCCTTCGTCGCCTTCTCCGACCCCATCACCATCCCCAGTCTTGGAACCGGGGTCTGAGCCTAATCTCGCAGTCCTCTCTATTCCTGGGGACACTATGACAACTATACAAATGTCTGTAGAAGAATCAACCCCCATCTCCCGTGAAACTGGGGAGCCATATCGCCTCTCTCCAGAACCCACTCCTCTCGCCGAACCCATACTGGAAGTAGAAGTGACACTTAGCAAACCGGTTCCAGAATCTGAGTTTTCTTCCAGTCCTCTCCAGGCTCCCACCCCTTTGGCATCTCACACAGTGGAAATTCATGAGCCTAATGGCATGGTCCCATCTGAAGATCTGGAACCAGAGGTGGAGTCAAGCCCAGAGCTTGCTCCTCCCCCAGCTTGCCCCTCCGAATCCCCTGTGCCCATTGCTCCAACTGCCCAACCTGAGGAACTGCTCAACGGAGCCCCCTCGCCACCAGCTGTGGACTTAAGCCCAGTCAGTGAGCCAGAGGAGCAGGCCAAGGAGGTGACAGCATCAATGGCGCCCCCCACCATCCCCTCTGCTACTCCAGCTACGGCTCCTTCAGCTACTTCCCCAGCTCAGGAGGAGGAAATGGAAGAAGAAGAAGAAGAGGAAGAAGGAGAAGCAGGAGAAGCAGGAGAAGCTGAGAGTGAGAAAGGAGGAGAGGAACTGCTCCCCCCAGAGAGTACCCCTATTCCAGCCAACTTGTCTCAGAATTTGGAGGCAGCAGCAGCCACTCAAGTGGCAGTATCTGTGCCAAAGAGGAGACGGAAAATTAAGGAGCTAAATAAGAAGGAGGCTGTTGGAGACCTTCTGGATGCCTTCAAGGAGGCGAACCCGGCAGTACCAGAGGTGGAAAATCAGCCTCCTGCAGGCAGCAATCCAGGCCCAGAGTCTGAGGGCAGTGGTGTGCCCCCACGTCCTGAGGAAGCAGATGAGACCTGGGACTCAAAGGAAGACAAAATTCACAATGCTGAGAACATCCAGCCCGGGGAACAGAAGTATGAATATAAGTCAGATCAGTGGAAGCCTCTAAACCTAGAGGAGAAAAAACGTTACGACCGTGAGTTCCTGCTTGGTTTTCAGTTCATCTTTGCCAGTATGCAGAAGCCAGAGGGATTGCCACATATCAGTGACGTGGTGCTGGACAAGGCCAATAAAACACCACTGCGGCCACTGGATCCCACTAGACTACAAGGCATAAATTGTGGCCCAGACTTCACTCCATCCTTTGCCAACCTTGGCCGGACAACCCTTAGCACCCGTGGGCCCCCAAGGGGTGGGCCAGGTGGGGAGCTGCCCCGTGGGCCGGCTGGCCTGGGACCCCGGCGCTCTCAGCAGGGACCCCGAAAAGAACCACGCAAGATCATTGCCACAGTGTTAATGACCGAAGATATAAAACTGAACAAAGCAGAGAAAGCCTGGAAACCCAGCAGCAAGCGGACGGCGGCTGATAAGGATCGAGGGGAAGAAGATGCTGATGGCAGCAAAACCCAGGACCTATTCCGCAGGGTGCGCTCCATCCTGAATAAACTGACACCCCAGATGTTCCAGCAGCTGATGAAGCAAGTGACGCAGCTGGCCATCGACACCGAGGAACGCCTCAAAGGGGTCATTGACCTCATTTTTGAGAAGGCCATTTCAGAGCCCAACTTCTCTGTGGCCTATGCCAACATGTGCCGCTGCCTCATGGCGCTGAAAGTGCCCACTACGGAAAAGCCAACAGTGACTGTGAACTTCCGAAAGCTGTTGTTGAATCGATGTCAGAAGGAGTTTGAGAAAGACAAAGATGATGATGAGGTTTTTGAGAAGAAGCAAAAAGAGATGGATGAAGCTGCTACGGCAGAGGAACGAGGACGCCTGAAGGAAGAGCTGGAAGAGGCTCGGGACATAGCCCGGCGGCGCTCTTTAGGGAATATCAAGTTTATTGGAGAGTTGTTCAAACTGAAGATGTTAACAGAGGCAATAATGCATGACTGTGTGGTCAAACTGCTTAAGAACCATGATGAAGAGTCCCTTGAGTGCCTTTGTCGTCTGCTCACCACCATTGGCAAAGACCTGGACTTTGAAAAAGCCAAGCCCCGAATGGATCAGTATTTCAACCAGATGGAAAAAATCATTAAAGAAAAGAAGACGTCATCCCGCATCCGCTTTATGCTGCAGGACGTGCTGGATCTGCGAGGGAGCAATTGGGTGCCACGCCGAGGGGATCAGGGTCCCAAGACCATTGACCAGATCCATAAGGAGGCTGAGATGGAAGAACATCGAGAGCACATCAAAGTGCAGCAGCTCATGGCCAAGGGCAGTGACAAGCGTCGGGGCGGTCCTCCAGGCCCTCCCATCAGCCGTGGACTTCCCCTTGTGGATGATGGTGGCTGGAACACAGTTCCCATCAGCAAAGGTAGCCGCCCCATTGACACCTCACGACTCACCAAGATCACCAAGCCTGGCTCCATCGATTCTAACAACCAGCTCTTTGCACCTGGAGGGCGACTGAGCTGGGGCAAGGGCAGCAGCGGAGGCTCAGGAGCCAAGCCCTCAGACGCAGCATCAGAAGCTGCTCGCCCAGCTACTAGTACTTTGAATCGCTTCTCAGCCCTTCAACAAGCGGTACCCACAGAAAGCACAGATAATAGACGTGTGGTGCAGAGGAGTAGCTTGAGCCGAGAACGAGGCGAGAAAGCTGGAGACCGAGGAGACCGCCTAGAGCGGAGTGAACGGGGAGGGGACCGTGGGGACCGGCTTGATCGTGCGCGGACACCTGCTACCAAGCGGAGCTTCAGCAAGGAAGTGGAGGAGCGGAGTAGAGAACGGCCCTCCCAGCCTGAGGGGCTGCGCAAGGCAGCTAGCCTCACGGAGGATCGGGACCGTGGGCGGGATGCCGTGAAGCGAGAAGCTGCCCTACCCCCAGTGAGCCCCCTGAAGGCGGCTCTCTCTGAGGAGGAGTTAGAGAAGAAATCCAAGGCTATCATTGAGGAATATCTCCATCTCAATGACATGAAAGAGGCAGTCCAGTGCGTGCAGGAGCTGGCCTCACCCTCCTTGCTCTTCATCTTTGTACGGCATGGTGTCGAGTCTACGCTGGAGCGCAGTGCCATTGCTCGTGAGCATATGGGGCAGCTGCTGCACCAGCTGCTCTGTGCTGGGCATCTGTCTACTGCTCAGTACTACCAAGGGTTGTATGAAATCTTGGAATTGGCTGAGGACATGGAAATTGACATCCCCCACGTGTGGCTCTACCTAGCGGAACTGGTAACACCCATTCTGCAGGAAGGTGGGGTGCCCATGGGGGAGCTGTTCAGGGAGATTACAAAGCCTCTGAGACCGTTGGGCAAAGCTGCTTCCCTGTTGCTGGAGATCCTGGGCCTCCTGTGCAAAAGCATGGGTCCTAAAAAGGTGGGGACGCTGTGGCGAGAAGCCGGGCTTAGCTGGAAGGAATTTCTACCTGAAGGCCAGGACATTGGTGCATTCGTCGCTGAACAGAAGGTGGAGTATACCCTGGGAGAGGAGTCGGAAGCCCCTGGCCAGAGGGCACTCCCCTCCGAGGAGCTGAACAGGCAGCTGGAGAAGCTGCTGAAGGAGGGCAGCAGTAACCAGCGGGTGTTCGACTGGATAGAGGCCAACCTGAGTGAGCAGCAGATAGTATCCAACACGTTAGTTCGAGCCCTCATGACGGCTGTCTGCTATTCTGCAATTATTTTTGAGACTCCCCTCCGAGTGGACGTTGCAGTGCTGAAAGCGCGAGCGAAGCTGCTGCAGAAATACCTGTGTGACGAGCAGAAGGAGCTACAGGCGCTCTACGCCCTCCAGGCCCTTGTAGTGACCTTAGAACAGCCTCCCAACCTGCTGCGGATGTTCTTTGACGCACTGTATGACGAGGACGTGGTGAAGGAGGATGCCTTCTACAGTTGGGAGAGTAGCAAGGACCCCGCTGAGCAGCAGGGCAAGGGTGTGGCCCTTAAATCTGTCACAGCCTTCTTCAAGTGGCTCCGTGAAGCAGAGGAGGAGTCTGACCACAACTGAGGGCTGGTGGGGCCGGGGACCTGGAGCCCCATGGACACACAGATGGCCCGGCTAGCCGCCTGGACTGCAGGGGGGCGGCAGCAGCGGCGGTGGCAGTGGGTGCCTGTAGTGTGATGTGTCTGAACTAATAAAGTGGCTGAAGAGGCAGGATGGCTTGGGGCTGCCTGGGCCCCCCTCCAGGATGCCGCCAGGTGTCCCTCTCCTCCCCCTGGGGCACAGAGATATATTATATATAAAGTCTTGAAATTTGGTGTGTCTTGGGGTGGGGAGGGGCACCAACGCCTGCCCCTGGGGTCCTTTTTTTTATTTTCTGAAAATCACTCTCGGGACTGCCGTCCTCGCTGCTGGGGGCATATGCCCCAGCCCCTGTACCACCCCTGCTGTTGCCTGGGCAGGGGGAAGGGGGGGCACGGTGCCTGTAATTATTAAACATGAATTCAATTAAGCTCAAAAAAAAAAAAAAAA