IF4G_ARATH
ID IF4G_ARATH Reviewed; 1727 AA.
AC Q76E23; Q0WVG9; Q9LKQ7; Q9LY39; Q9M4Q5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Eukaryotic translation initiation factor 4G;
DE Short=eIF-4G;
DE Short=eIF4G;
DE AltName: Full=Protein cucumovirus multiplication 2;
DE AltName: Full=Protein synthesis initiation factor 4G;
GN Name=EIF4G; Synonyms=CUM2; OrderedLocusNames=At3g60240; ORFNames=F27H5_30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), GENE FAMILY, MUTAGENESIS OF
RP PRO-1329, AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=15163703; DOI=10.1128/jvi.78.12.6102-6111.2004;
RA Yoshii M., Nishikiori M., Tomita K., Yoshioka N., Kozuka R., Naito S.,
RA Ishikawa M.;
RT "The Arabidopsis cucumovirus multiplication 1 and 2 loci encode translation
RT initiation factors 4E and 4G.";
RL J. Virol. 78:6102-6111(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 66-1727.
RA Browning K.S., Wong K.;
RT "The sequence of Arabidopsis thaliana EIF4G.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP MUTANT CUM2-1.
RX PubMed=9765416; DOI=10.1128/jvi.72.11.8731-8737.1998;
RA Yoshii M., Yoshioka N., Ishikawa M., Naito S.;
RT "Isolation of an Arabidopsis thaliana mutant in which the multiplication of
RT both cucumber mosaic virus and turnip crinkle virus is affected.";
RL J. Virol. 72:8731-8737(1998).
RN [7]
RP ERRATUM OF PUBMED:9765416.
RX DOI=10.1128/JVI.77.14.8178.2003;
RA Yoshii M., Yoshioka N., Ishikawa M., Naito S.;
RL J. Virol. 77:8178-8178(2003).
RN [8]
RP REVIEW, AND SUBUNIT.
RX PubMed=16343979; DOI=10.1016/j.tplants.2005.11.004;
RA Robaglia C., Caranta C.;
RT "Translation initiation factors: a weak link in plant RNA virus
RT infection.";
RL Trends Plant Sci. 11:40-45(2006).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=17316629; DOI=10.1016/j.febslet.2007.02.007;
RA Nicaise V., Gallois J.L., Chafiai F., Allen L.M., Schurdi-Levraud V.,
RA Browning K.S., Candresse T., Caranta C., Le Gall O., German-Retana S.;
RT "Coordinated and selective recruitment of eIF4E and eIF4G factors for
RT potyvirus infection in Arabidopsis thaliana.";
RL FEBS Lett. 581:1041-1046(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1529, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-985 AND SER-1529, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC secondary structure and recruitment of mRNA to the ribosome. Plays a
CC role in the accumulation of some potyvirus during viral infection.
CC Required for the accumulation of cucumber mosaic virus 3a protein and
CC turnip crinkle virus p28 replication protein during viral infection.
CC These proteins are necessary for cell-to-cell movement of the virus.
CC {ECO:0000269|PubMed:15163703, ECO:0000269|PubMed:17316629}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G. In higher plants two
CC isoforms of EIF4F have been identified, named isoform EIF4F and isoform
CC EIF(iso)4F. Isoform EIF4F has subunits p220 and p26, whereas isoform
CC EIF(iso)4F has subunits p82 and p28. {ECO:0000269|PubMed:16343979}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q76E23-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76E23-2; Sequence=VSP_040521;
CC -!- DISRUPTION PHENOTYPE: Displays resistance to potyvirus (C1YVV)
CC infection. {ECO:0000269|PubMed:17316629}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF73054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB87861.1; Type=Erroneous gene model prediction; Note=The predicted gene At3g60240 has been split into 2 genes: At3g60240 and At3g60245.; Evidence={ECO:0000305};
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DR EMBL; AB107249; BAC98352.1; -; mRNA.
DR EMBL; AL163852; CAB87861.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80027.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80028.1; -; Genomic_DNA.
DR EMBL; AK226781; BAE98879.1; -; mRNA.
DR EMBL; AF263518; AAF73054.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF263834; AAF73056.1; -; mRNA.
DR PIR; T49219; T49219.
DR RefSeq; NP_001078318.1; NM_001084849.2. [Q76E23-2]
DR RefSeq; NP_001078319.1; NM_001084850.1. [Q76E23-1]
DR AlphaFoldDB; Q76E23; -.
DR SMR; Q76E23; -.
DR BioGRID; 10508; 2.
DR STRING; 3702.AT3G60240.4; -.
DR iPTMnet; Q76E23; -.
DR PaxDb; Q76E23; -.
DR PRIDE; Q76E23; -.
DR ProteomicsDB; 232203; -. [Q76E23-1]
DR EnsemblPlants; AT3G60240.3; AT3G60240.3; AT3G60240. [Q76E23-2]
DR EnsemblPlants; AT3G60240.4; AT3G60240.4; AT3G60240. [Q76E23-1]
DR GeneID; 825194; -.
DR Gramene; AT3G60240.3; AT3G60240.3; AT3G60240. [Q76E23-2]
DR Gramene; AT3G60240.4; AT3G60240.4; AT3G60240. [Q76E23-1]
DR KEGG; ath:AT3G60240; -.
DR Araport; AT3G60240; -.
DR TAIR; locus:2081927; AT3G60240.
DR eggNOG; KOG0401; Eukaryota.
DR InParanoid; Q76E23; -.
DR OMA; SICAMSH; -.
DR OrthoDB; 594395at2759; -.
DR PhylomeDB; Q76E23; -.
DR PRO; PR:Q76E23; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q76E23; baseline and differential.
DR Genevisible; Q76E23; AT.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IMP:TAIR.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR23253; PTHR23253; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS51366; MI; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Translation regulation.
FT CHAIN 1..1727
FT /note="Eukaryotic translation initiation factor 4G"
FT /id="PRO_0000245495"
FT DOMAIN 1096..1319
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1539..1663
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..928
FT /note="EIF4E-binding"
FT /evidence="ECO:0000250"
FT REGION 977..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 1529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT VAR_SEQ 104..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15163703"
FT /id="VSP_040521"
FT MUTAGEN 1329
FT /note="P->S: In cum2-1; Reduces cucumber mosaic virus (CMV)
FT or turnip crinkle virus (TCV) multiplication after
FT infection."
FT /evidence="ECO:0000269|PubMed:15163703"
FT CONFLICT 236
FT /note="D -> G (in Ref. 4; BAE98879)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="T -> P (in Ref. 5; AAF73054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1727 AA; 187921 MW; 7522820BD5C697D2 CRC64;
MSYNQSRPDR SETQYRRTGR STGNQQQQQQ HRSSSAAGYG KGAGAPGSAP APSTYPDNSS
LSSNRSFKKP GNAQGGGQPR VNLPPVNHPN NHNNGPNAHS RSQVTGEPGV GGPTNPTESF
NRNTGPIPKA PTSQSTVMSS KINETPNTAK VAASGDASQA FPLQFGSLGP DLMVPARTTS
APPNMDDQKR AQMQQSSLRT ASNVPASVPK KDSSNKGADN QLMRKEGHNP SSEKADIQVP
HIAPPSQTQK SPITNIRMPS VQTPYQHTQV PHPVHFGGPN MHMQTPVTAT SFQMPMPMAL
SMGNTPQIPP QVFYQGHPPH PMHHQGMMHQ AQGHGFATPM GAQIHPQLGH VGVGLSPQYP
QQQGGKYGGA RKTTPVKITH PDTHEELRLD RRGDPYSEGD STALKPHSNP PPRSQPVSSF
APRPVNLVQP SYNSNTMIYP PVSVPLNNGP MSSAQAPRYH YPVIDGSQRV QLINQPAHTA
PQLIRPAAPA HLSSDSTSSV KARNAQNVMS SALPVNAKVS VKPAGVSEKL GSPKDRSHGE
VNISLSQKNV EACSLSSSQQ PKPSFVSGVP NSSAPPAKSP VETVPLAKSS VETVPPVKSS
VETAPVTTTE IRRAEMVSES ISVEDQTCKV EPPHNLTENR GQTMPDSLVS DPETATVAAK
ENLSLPATNG FRKQLLKVST TSDAPTSDSV DTSIDKSTEG SSHASSEISG SSPQEKDLKC
DNRTASDKLD ERSVISDAKH ETLSGVLEKA QNEVDGATDV CPVSEKLAVT DDTSSDLPHS
THVLSSTVPL GHSETHKSAV ETNTRRNTST KGKKKIKEIL QKADAAGTTS DLYMAYKGPE
EKKESSNVVH DVSNQNLLPA IPQAVEAIVD TEPVKNEPED WEDAADVSTP KLETADNSVN
AKRGSSDEVS DNCINTEKKY SRDFLLKFAD LCTALPEGFD VSPDIANALI VAYMGASHHE
HDSYPTPGKV MDRQASGARL DRRPSNVAGD DRWTKNQGSL PAGYGGNVGF RPGQGGNSGV
LRNPRMQGPI ISRPMQPVGP MGGMGRNTPD LERWQRGSNF QQKGLFPSPH TPMQVMHKAE
RKYQVGTIAD EEQAKQRQLK SILNKLTPQN FEKLFEQVKS VNIDNAVTLS GVISQIFDKA
LMEPTFCEMY ADFCFHLSGA LPDFNENGEK ITFKRLLLNK CQEEFERGEK EEEEASRVAE
EGQVEQTEEE REEKRLQVRR RMLGNIRLIG ELYKKRMLTE KIMHACIQKL LGYNQDPHEE
NIEALCKLMS TIGVMIDHNK AKFQMDGYFE KMKMLSCKQE LSSRVRFMLI NAIDLRKNKW
QERMKVEGPK KIEEVHRDAA QERQTQANRL SRGPSMNSSG RRGHMEFSSP RGGGGMLSPP
AAQMGSYHGP PQGRGFSNQD IRFDDRPSYE PRMVPMPQRS VCEEPITLGP QGGLGQGMSI
RRPAVASNTY QSDATQAGGG DSRRPAGGLN GFGSHRPASP VTHGRSSPQE RGTAYVHREF
ASLSRASDLS PEVSSARQVL QGPSATVNSP RENALSEEQL ENLSLSAIKE YYSARDENEI
GMCMKDMNSP AYHPTMISLW VTDSFERKDK ERDLLAKLLV NLVKSADNAL NEVQLVKGFE
SVLKTLEDAV NDAPKAAEFL GRIFGKSVTE KVVTLTEIGR LIQEGGEEPG SLIEFGLGGD
VLGSVLEMIK TEAGEETLVE IRRSSGLRIE NFKPHAPNRS KILEKFT
