IF4G2_MOUSE
ID IF4G2_MOUSE Reviewed; 906 AA.
AC Q62448; P97867; Q0VGZ3; Q3UNC1; Q5XKD8; Q6P1Z0; Q921U3;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Eukaryotic translation initiation factor 4 gamma 2;
DE Short=eIF-4-gamma 2;
DE Short=eIF-4G 2;
DE Short=eIF4G 2;
DE AltName: Full=Novel APOBEC-1 target 1;
DE AltName: Full=Translation repressor NAT1;
DE AltName: Full=p97;
GN Name=Eif4g2 {ECO:0000312|MGI:MGI:109207};
GN Synonyms=Nat1 {ECO:0000312|MGI:MGI:109207};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=9030685; DOI=10.1101/gad.11.3.321;
RA Yamanaka S., Poksay K.S., Arnold K.S., Innerarity T.L.;
RT "A novel translational repressor mRNA is edited extensively in livers
RT containing tumors caused by the transgene expression of the apoB mRNA-
RT editing enzyme.";
RL Genes Dev. 11:321-333(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:9027506};
RX PubMed=9027506; DOI=10.1006/geno.1996.4502;
RA Shaughnessy J.D. Jr., Jenkins N.A., Copeland N.G.;
RT "cDNA cloning, expression analysis, and chromosomal localization of a gene
RT with high homology to wheat eIF-(iso)4F and mammalian eIF-4G.";
RL Genomics 39:192-197(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000269|PubMed:15489334}, and Czech II;
RC TISSUE=Embryonic brain, Eye, and
RC Mammary gland {ECO:0000269|PubMed:15489334};
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Appears to play a role in the switch from cap-dependent to
CC IRES-mediated translation during mitosis, apoptosis and viral
CC infection. Cleaved by some caspases and viral proteases.
CC {ECO:0000250|UniProtKB:P78344, ECO:0000269|PubMed:9030685}.
CC -!- SUBUNIT: Interacts with the serine/threonine protein kinases MKNK1 and
CC MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q62448; Q61823: Pdcd4; NbExp=2; IntAct=EBI-296494, EBI-296473;
CC Q62448; P26450: Pik3r1; NbExp=3; IntAct=EBI-296494, EBI-641764;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62448-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62448-2; Sequence=VSP_021640;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues examined.
CC {ECO:0000269|PubMed:9027506}.
CC -!- PTM: Phosphorylation; hyperphosphorylated during mitosis.
CC {ECO:0000250|UniProtKB:P78344}.
CC -!- MISCELLANEOUS: This gene has been shown to be extensively edited in the
CC liver of APOBEC1 transgenic animals. Its aberrant editing could
CC contribute to the potent oncogenesis induced by overexpression of
CC APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a
CC fundamental translational repressor.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE25826.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; U76112; AAC53095.1; -; mRNA.
DR EMBL; U63323; AAC53030.1; -; mRNA.
DR EMBL; AK144309; BAE25826.1; ALT_INIT; mRNA.
DR EMBL; BC040391; AAH40391.2; -; mRNA.
DR EMBL; BC043034; AAH43034.2; -; mRNA.
DR EMBL; BC056387; AAH56387.1; -; mRNA.
DR EMBL; BC057673; AAH57673.2; -; mRNA.
DR EMBL; BC064810; AAH64810.2; -; mRNA.
DR EMBL; BC092521; AAH92521.1; -; mRNA.
DR CCDS; CCDS40087.1; -. [Q62448-2]
DR CCDS; CCDS40088.1; -. [Q62448-1]
DR RefSeq; NP_001035221.1; NM_001040131.2.
DR RefSeq; NP_038535.2; NM_013507.3.
DR AlphaFoldDB; Q62448; -.
DR SMR; Q62448; -.
DR BioGRID; 199423; 13.
DR IntAct; Q62448; 3.
DR MINT; Q62448; -.
DR STRING; 10090.ENSMUSP00000124551; -.
DR iPTMnet; Q62448; -.
DR PhosphoSitePlus; Q62448; -.
DR SwissPalm; Q62448; -.
DR EPD; Q62448; -.
DR jPOST; Q62448; -.
DR MaxQB; Q62448; -.
DR PaxDb; Q62448; -.
DR PeptideAtlas; Q62448; -.
DR PRIDE; Q62448; -.
DR ProteomicsDB; 266947; -. [Q62448-1]
DR ProteomicsDB; 266948; -. [Q62448-2]
DR DNASU; 13690; -.
DR GeneID; 13690; -.
DR KEGG; mmu:13690; -.
DR CTD; 1982; -.
DR MGI; MGI:109207; Eif4g2.
DR eggNOG; KOG0401; Eukaryota.
DR InParanoid; Q62448; -.
DR OrthoDB; 594395at2759; -.
DR PhylomeDB; Q62448; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR BioGRID-ORCS; 13690; 21 hits in 70 CRISPR screens.
DR ChiTaRS; Eif4g2; mouse.
DR PRO; PR:Q62448; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q62448; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0034645; P:cellular macromolecule biosynthetic process; ISO:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
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 InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23253; PTHR23253; 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 Acetylation; Alternative splicing; Initiation factor; Isopeptide bond;
KW Methylation; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Repressor; Translation regulation; Ubl conjugation.
FT CHAIN 1..906
FT /note="Eukaryotic translation initiation factor 4 gamma 2"
FT /id="PRO_0000213326"
FT DOMAIN 78..308
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 542..665
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 719..903
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 89
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 359
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 430
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 504
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 507
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT CROSSLNK 574
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P78344"
FT VAR_SEQ 433..470
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021640"
FT CONFLICT 1
FT /note="M -> V (in Ref. 3; BAE25826)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="S -> T (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="L -> G (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="K -> Q (in Ref. 1; AAC53095)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="RS -> MSR (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="S -> N (in Ref. 3; BAE25826 and 4; AAH40391/
FT AAH43034/AAH56387/AAH57673/AAH64810/AAH92521)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="F -> L (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="S -> P (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="L -> F (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="S -> R (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> D (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="K -> M (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="V -> G (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="D -> N (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="I -> S (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="K -> T (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 784
FT /note="S -> N (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 797..798
FT /note="SK -> PT (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="L -> V (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="L -> F (in Ref. 1; AAC53095)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="K -> Q (in Ref. 2; AAC53030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 906 AA; 102106 MW; EA73E717671562E4 CRC64;
MESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW IPARSTRRDD
NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL LNVGVESKLI LKGVILLIVD
KALEEPKYSS LYAQLCLRLA EDAPNFDGPA AEGQPGQKQS TTFRRLLISK LQDEFENRTR
NVDVYDKREN PLLPEEEEQR AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK
RVQLKDMGED LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD
TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGRSDFF LEGPFMPPRM
KMDRDPLGGL ADMFGQMPGS GIGTGPGVIQ DRFSPTMGRH RSNQLFNGHG GHIMPPTQSQ
FGEMGGKFMK SQGLSQLYHN QSQGLLSQLQ GQSKDMPPRF SKKGQLNADE ISLRPAQSFL
MNKNQVPKLQ PQITMIPPSA QPPRTQTPPL GQTPQLGLKT NPPLIQEKPA KTSKKPPPSK
EELLKLTEAV VTDYLNSGNA NDAVSGVREM RAPKHFLPEM LSKVIILSLD RSDEDKEKAS
SLISLLKQEG IATSDNFMQA FLNVLEQCPK LEVDIPLVKS YLAQFAARAI ISELVSISEL
AQPLESGTHF PLFLLCLQQL AKLQDREWLT ELFQQSKVNM QKMLPEIDQN KDRMLEILEG
KGLSFLFPLL KLEKELLKQI KLDPSPQTIY KWIKDNISPK LHVDKGFVNI LMTSFLQYIS
SEVSPPSDET DSSSAPSKEQ LEQEKQLLLS FKPVMQKFLH DHVDLQVSAL YALQVHCYNS
SFPKGMLLRF FVHFYDMEII EEEAFLAWKE DITQEFPGKG KALFQVNQWL TWLETAEEEE
SEEEAD
