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Database: UniProt
Entry: IF4G_ARATH
LinkDB: IF4G_ARATH
Original site: 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   27-MAR-2024, entry version 130.
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; 3.
DR   STRING; 3702.Q76E23; -.
DR   iPTMnet; Q76E23; -.
DR   PaxDb; 3702-AT3G60240-4; -.
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; AT3G60240; EIF4G.
DR   eggNOG; KOG0401; Eukaryota.
DR   InParanoid; Q76E23; -.
DR   OMA; QFGGPNQ; -.
DR   OrthoDB; 1123866at2759; -.
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:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009615; P:response to virus; IMP:TAIR.
DR   Gene3D; 1.25.40.180; -; 2.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
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
//
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