IF4G3_HUMAN
ID IF4G3_HUMAN Reviewed; 1585 AA.
AC O43432; B9EGQ7; Q15597; Q504Z1; Q5SWC3; Q8NEN1;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 3;
DE Short=eIF-4-gamma 3;
DE Short=eIF-4G 3;
DE Short=eIF4G 3;
DE AltName: Full=eIF-4-gamma II;
DE Short=eIF4GII;
GN Name=EIF4G3;
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 [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP EIF4A; EIF4E AND EIF3.
RX PubMed=9418880; DOI=10.1128/mcb.18.1.334;
RA Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S.,
RA Sonenberg N.;
RT "A novel functional human eukaryotic translation initiation factor 4G.";
RL Mol. Cell. Biol. 18:334-342(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=PNS, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 887-1585 (ISOFORM 1).
RC TISSUE=Ovary;
RA Klaudiny J.J., von der Kammer H.H., Scheit K.K.;
RT "Characterization of secretory proteins of human ovarian follicle cells by
RT cDNA cloning.";
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH PABPC1.
RX PubMed=9857202; DOI=10.1093/emboj/17.24.7480;
RA Imataka H., Gradi A., Sonenberg N.;
RT "A newly identified N-terminal amino acid sequence of human eIF4G binds
RT poly(A)-binding protein and functions in poly(A)-dependent translation.";
RL EMBO J. 17:7480-7489(1998).
RN [7]
RP PHOSPHORYLATION AT SER-1156 BY CAMK1.
RX PubMed=14507913; DOI=10.1074/jbc.m308781200;
RA Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.;
RT "Phosphorylation screening identifies translational initiation factor 4GII
RT as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase
RT I.";
RL J. Biol. Chem. 278:48570-48579(2003).
RN [8]
RP CLEAVAGE BY RHINOVIRUS PROTEASE.
RX PubMed=12663812; DOI=10.1128/jvi.77.8.5026-5029.2003;
RA Gradi A., Svitkin Y.V., Sommergruber W., Imataka H., Morino S., Skern T.,
RA Sonenberg N.;
RT "Human rhin4ovirus 2A proteinase cleavage sites in eukaryotic initiation
RT factors (eIF) 4GI and eIF4GII are different.";
RL J. Virol. 77:5026-5029(2003).
RN [9]
RP CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS PROTEASE.
RX PubMed=15016848; DOI=10.1128/jvi.78.7.3271-3278.2004;
RA Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T.,
RA Belsham G.J.;
RT "Cleavage of eukaryotic translation initiation factor 4GII within foot-and-
RT mouth disease virus-infected cells: identification of the L-protease
RT cleavage site in vitro.";
RL J. Virol. 78:3271-3278(2004).
RN [10]
RP REVIEW.
RX PubMed=10872469; DOI=10.1146/annurev.biochem.68.1.913;
RA Gingras A.-C., Raught B., Sonenberg N.;
RT "eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and
RT regulators of translation.";
RL Annu. Rev. Biochem. 68:913-963(1999).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT network: indicating the involvement of ribonucleoside-diphosphate reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND IDENTIFICATION BY
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND SER-495, AND
RP IDENTIFICATION BY 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND SER-495, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232; SER-495;
RP SER-1218 AND SER-1409, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-267 AND SER-495, AND
RP IDENTIFICATION BY 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 [22]
RP STRUCTURE BY NMR OF 621-637 IN COMPLEX WITH EIF4E.
RX PubMed=12975586; DOI=10.1023/a:1025442322316;
RA Miura T., Shiratori Y., Shimma N.;
RT "Backbone resonance assignment of human eukaryotic translation initiation
RT factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and
RT a 17-amino acid peptide derived from human eIF4GII.";
RL J. Biomol. NMR 27:279-280(2003).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 745-986, AND MUTAGENESIS OF
RP ARG-756; ARG-759; LYS-764; ARG-814; LYS-820 AND 834-ARG-LYS-835.
RX PubMed=11172724; DOI=10.1016/s1097-2765(01)00167-8;
RA Marcotrigiano J., Lomakin I.B., Sonenberg N., Pestova T.V., Hellen C.U.T.,
RA Burley S.K.;
RT "A conserved HEAT domain within eIF4G directs assembly of the translation
RT initiation machinery.";
RL Mol. Cell 7:193-203(2001).
CC -!- FUNCTION: Probable component of the protein complex eIF4F, which is
CC involved in the recognition of the mRNA cap, ATP-dependent unwinding of
CC 5'-terminal secondary structure and recruitment of mRNA to the
CC ribosome. Thought to be a functional homolog of EIF4G1.
CC {ECO:0000269|PubMed:9418880}.
CC -!- SUBUNIT: Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a
CC complex with EIF4E. eIF4F is a multi-subunit complex, the composition
CC of which varies with external and internal environmental conditions. It
CC is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3
CC interacts through its C-terminus with the serine/threonine kinases
CC MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding
CC these enzymes in place to phosphorylate eIF4E. Non-phosphorylated
CC EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin
CC stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1
CC causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and
CC consequent initiation of translation. EIF4G1/EIF4G3 interacts with
CC PABPC1 to bring about circularization of the mRNA (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O43432; P06730: EIF4E; NbExp=3; IntAct=EBI-464766, EBI-73440;
CC O43432-1; P06730: EIF4E; NbExp=2; IntAct=EBI-15841003, EBI-73440;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O43432-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43432-2; Sequence=VSP_010487, VSP_010488, VSP_010489;
CC Name=3;
CC IsoId=O43432-3; Sequence=VSP_043447, VSP_043448;
CC Name=4;
CC IsoId=O43432-4; Sequence=VSP_054502;
CC -!- PTM: Following infection by certain enteroviruses, rhinoviruses and
CC aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the
CC leader protease in the case of aphthoviruses. This shuts down the
CC capped cellular mRNA transcription. {ECO:0000269|PubMed:12663812,
CC ECO:0000269|PubMed:15016848}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
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DR EMBL; AF012072; AAC02903.2; -; mRNA.
DR EMBL; AL031005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471134; EAW94956.1; -; Genomic_DNA.
DR EMBL; BC030578; AAH30578.1; -; mRNA.
DR EMBL; BC094683; AAH94683.1; -; mRNA.
DR EMBL; BC136643; AAI36644.1; -; mRNA.
DR EMBL; Z34918; CAA84397.1; -; mRNA.
DR CCDS; CCDS214.1; -. [O43432-1]
DR CCDS; CCDS55580.1; -. [O43432-3]
DR CCDS; CCDS59192.1; -. [O43432-2]
DR PIR; S49172; S49172.
DR RefSeq; NP_001185730.1; NM_001198801.1.
DR RefSeq; NP_001185731.1; NM_001198802.1. [O43432-3]
DR RefSeq; NP_001185732.1; NM_001198803.2. [O43432-2]
DR RefSeq; NP_003751.2; NM_003760.4. [O43432-1]
DR RefSeq; XP_016858189.1; XM_017002700.1. [O43432-1]
DR RefSeq; XP_016858197.1; XM_017002708.1. [O43432-4]
DR RefSeq; XP_016858201.1; XM_017002712.1.
DR PDB; 1HU3; X-ray; 2.37 A; A=745-1003.
DR PDBsum; 1HU3; -.
DR AlphaFoldDB; O43432; -.
DR BMRB; O43432; -.
DR SMR; O43432; -.
DR BioGRID; 114220; 112.
DR ComplexPortal; CPX-5635; Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G3 variant.
DR ComplexPortal; CPX-5636; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant.
DR DIP; DIP-33245N; -.
DR ELM; O43432; -.
DR IntAct; O43432; 40.
DR MINT; O43432; -.
DR STRING; 9606.ENSP00000383274; -.
DR GlyGen; O43432; 8 sites, 2 O-linked glycans (8 sites).
DR iPTMnet; O43432; -.
DR MetOSite; O43432; -.
DR PhosphoSitePlus; O43432; -.
DR BioMuta; EIF4G3; -.
DR EPD; O43432; -.
DR jPOST; O43432; -.
DR MassIVE; O43432; -.
DR MaxQB; O43432; -.
DR PaxDb; O43432; -.
DR PeptideAtlas; O43432; -.
DR PRIDE; O43432; -.
DR ProteomicsDB; 48943; -. [O43432-1]
DR ProteomicsDB; 48944; -. [O43432-2]
DR ProteomicsDB; 48945; -. [O43432-3]
DR ProteomicsDB; 62418; -.
DR Antibodypedia; 15146; 157 antibodies from 24 providers.
DR DNASU; 8672; -.
DR Ensembl; ENST00000264211.13; ENSP00000264211.7; ENSG00000075151.24. [O43432-1]
DR Ensembl; ENST00000356916.7; ENSP00000349386.3; ENSG00000075151.24. [O43432-2]
DR Ensembl; ENST00000374935.7; ENSP00000364071.3; ENSG00000075151.24. [O43432-4]
DR Ensembl; ENST00000682284.1; ENSP00000507819.1; ENSG00000075151.24. [O43432-2]
DR Ensembl; ENST00000686579.1; ENSP00000509941.1; ENSG00000075151.24. [O43432-3]
DR GeneID; 8672; -.
DR KEGG; hsa:8672; -.
DR UCSC; uc001bee.4; human. [O43432-1]
DR CTD; 8672; -.
DR DisGeNET; 8672; -.
DR GeneCards; EIF4G3; -.
DR HGNC; HGNC:3298; EIF4G3.
DR HPA; ENSG00000075151; Low tissue specificity.
DR MIM; 603929; gene.
DR neXtProt; NX_O43432; -.
DR OpenTargets; ENSG00000075151; -.
DR PharmGKB; PA27724; -.
DR VEuPathDB; HostDB:ENSG00000075151; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000156454; -.
DR HOGENOM; CLU_001519_2_0_1; -.
DR InParanoid; O43432; -.
DR OrthoDB; 594395at2759; -.
DR PhylomeDB; O43432; -.
DR TreeFam; TF101527; -.
DR PathwayCommons; O43432; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR SignaLink; O43432; -.
DR SIGNOR; O43432; -.
DR BioGRID-ORCS; 8672; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; EIF4G3; human.
DR EvolutionaryTrace; O43432; -.
DR GeneWiki; EIF4G3; -.
DR GenomeRNAi; 8672; -.
DR Pharos; O43432; Tbio.
DR PRO; PR:O43432; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O43432; protein.
DR Bgee; ENSG00000075151; Expressed in sperm and 199 other tissues.
DR ExpressionAtlas; O43432; baseline and differential.
DR Genevisible; O43432; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000339; F:RNA cap binding; TAS:ProtInc.
DR GO; GO:0008135; F:translation factor activity, RNA binding; TAS:ProtInc.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR037585; EIF4G3.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; PTHR23253; 1.
DR PANTHER; PTHR23253:SF23; PTHR23253:SF23; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 3.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Initiation factor;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding; Translation regulation.
FT CHAIN 1..1585
FT /note="Eukaryotic translation initiation factor 4 gamma 3"
FT /id="PRO_0000213329"
FT REPEAT 745..783
FT /note="HEAT 1"
FT DOMAIN 755..983
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REPEAT 784..831
FT /note="HEAT 2"
FT REPEAT 832..905
FT /note="HEAT 3"
FT REPEAT 906..944
FT /note="HEAT 4"
FT REPEAT 945..984
FT /note="HEAT 5"
FT DOMAIN 1221..1343
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 1416..1585
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..162
FT /note="PABPC1-binding"
FT REGION 208..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..630
FT /note="EIF4E-binding"
FT /evidence="ECO:0000250"
FT REGION 686..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..1019
FT /note="eIF3/EIF4A-binding"
FT /evidence="ECO:0000250"
FT REGION 729..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1585
FT /note="EIF4A-binding"
FT /evidence="ECO:0000250"
FT REGION 1571..1585
FT /note="Necessary but not sufficient for MKNK1-binding"
FT /evidence="ECO:0000250"
FT COILED 447..475
FT /evidence="ECO:0000255"
FT COILED 994..1023
FT /evidence="ECO:0000255"
FT COMPBIAS 136..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..187
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 699..700
FT /note="Cleavage; by enterovirus/rhinovirus protease 2A"
FT SITE 700..701
FT /note="Cleavage; by foot-and-mouth disease virus leader
FT protease"
FT MOD_RES 168
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q80XI3"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80XI3"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1156
FT /note="Phosphoserine; by CaMK1"
FT /evidence="ECO:0000269|PubMed:14507913"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 10
FT /note="P -> PGGFRPIQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043447"
FT VAR_SEQ 11
FT /note="F -> FAAGPRPPHHQF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010487"
FT VAR_SEQ 182
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043448"
FT VAR_SEQ 219..498
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054502"
FT VAR_SEQ 499..504
FT /note="AQIAIT -> ETSNEC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010488"
FT VAR_SEQ 505..1585
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010489"
FT VARIANT 378
FT /note="Q -> R (in dbSNP:rs35731992)"
FT /id="VAR_048924"
FT VARIANT 496
FT /note="P -> A (in dbSNP:rs35176330)"
FT /id="VAR_034009"
FT VARIANT 1185
FT /note="D -> E (in dbSNP:rs2230572)"
FT /id="VAR_048925"
FT MUTAGEN 756
FT /note="R->D: Reduces binding to EIF4A; when associated with
FT D-759 and D-764."
FT /evidence="ECO:0000269|PubMed:11172724"
FT MUTAGEN 759
FT /note="R->D: Reduces binding to EIF4A; when associated with
FT D-756 and D-764."
FT /evidence="ECO:0000269|PubMed:11172724"
FT MUTAGEN 764
FT /note="K->D: Reduces binding to EIF4A; when associated with
FT D-756 and D-759."
FT /evidence="ECO:0000269|PubMed:11172724"
FT MUTAGEN 814
FT /note="R->D: Reduces binding to EIF4A; when associated with
FT D-820."
FT /evidence="ECO:0000269|PubMed:11172724"
FT MUTAGEN 820
FT /note="K->D: Reduces binding to EIF4A; when associated with
FT D-814."
FT /evidence="ECO:0000269|PubMed:11172724"
FT MUTAGEN 834..835
FT /note="RK->DD: Reduces binding to IRES."
FT /evidence="ECO:0000269|PubMed:11172724"
FT CONFLICT 159
FT /note="M -> I (in Ref. 4; AAH30578)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="D -> G (in Ref. 4; AAH30578)"
FT /evidence="ECO:0000305"
FT HELIX 746..762
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 770..777
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 785..801
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 806..816
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 833..848
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 885..900
FT /evidence="ECO:0007829|PDB:1HU3"
FT TURN 901..903
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 907..919
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 923..940
FT /evidence="ECO:0007829|PDB:1HU3"
FT TURN 943..945
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 946..961
FT /evidence="ECO:0007829|PDB:1HU3"
FT HELIX 967..981
FT /evidence="ECO:0007829|PDB:1HU3"
FT TURN 982..984
FT /evidence="ECO:0007829|PDB:1HU3"
SQ SEQUENCE 1585 AA; 176652 MW; EA483139373DCA5C CRC64;
MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM VNHLPMPYPV
PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFPNAYGT PFYPSQPVYQ
SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPTSTPTP
PQQLPSQVPE HSPVVYGTVE SAHLAASTPV TAASDQKQEE KPKPDPVLKS PSPVLRLVLS
GEKKEQEGQT SETTAIVSIA ELPLPPSPTT VSSVARSTIA APTSSALSSQ PIFTTAIDDR
CELSSPREDT IPIPSLTSCT ETSDPLPTNE NDDDICKKPC SVAPNDIPLV SSTNLINEIN
GVSEKLSATE SIVEIVKQEV LPLTLELEIL ENPPEEMKLE CIPAPITPST VPSFPPTPPT
PPASPPHTPV IVPAAATTVS SPSAAITVQR VLEEDESIRT CLSEDAKEIQ NKIEVEADGQ
TEEILDSQNL NSRRSPVPAQ IAITVPKTWK KPKDRTRTTE EMLEAELELK AEEELSIDKV
LESEQDKMSQ GFHPERDPSD LKKVKAVEEN GEEAEPVRNG AESVSEGEGI DANSGSTDSS
GDGVTFPFKP ESWKPTDTEG KKQYDREFLL DFQFMPACIQ KPEGLPPISD VVLDKINQPK
LPMRTLDPRI LPRGPDFTPA FADFGRQTPG GRGVPLLNVG SRRSQPGQRR EPRKIITVSV
KEDVHLKKAE NAWKPSQKRD SQADDPENIK TQELFRKVRS ILNKLTPQMF NQLMKQVSGL
TVDTEERLKG VIDLVFEKAI DEPSFSVAYA NMCRCLVTLK VPMADKPGNT VNFRKLLLNR
CQKEFEKDKA DDDVFEKKQK ELEAASAPEE RTRLHDELEE AKDKARRRSI GNIKFIGELF
KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD QYFNQMEKIV
KERKTSSRIR FMLQDVIDLR LCNWVSRRAD QGPKTIEQIH KEAKIEEQEE QRKVQQLMTK
EKRRPGVQRV DEGGWNTVQG AKNSRVLDPS KFLKITKPTI DEKIQLVPKA QLGSWGKGSS
GGAKASETDA LRSSASSLNR FSALQPPAPS GSTPSTPVEF DSRRTLTSRG SMGREKNDKP
LPSATARPNT FMRGGSSKDL LDNQSQEEQR REMLETVKQL TGGVDVERNS TEAERNKTRE
SAKPEISAMS AHDKAALSEE ELERKSKSII DEFLHINDFK EAMQCVEELN AQGLLHVFVR
VGVESTLERS QITRDHMGQL LYQLVQSEKL SKQDFFKGFS ETLELADDMA IDIPHIWLYL
AELVTPMLKE GGISMRELTI EFSKPLLPVG RAGVLLSEIL HLLCKQMSHK KVGALWREAD
LSWKDFLPEG EDVHNFLLEQ KLDFIESDSP CSSEALSKKE LSAEELYKRL EKLIIEDKAN
DEQIFDWVEA NLDEIQMSSP TFLRALMTAV CKAAIIADSS TFRVDTAVIK QRVPILLKYL
DSDTEKELQA LYALQASIVK LDQPANLLRM FFDCLYDEEV ISEDAFYKWE SSKDPAEQNG
KGVALKSVTA FFTWLREAEE ESEDN
