IF4E2_MOUSE
ID IF4E2_MOUSE Reviewed; 245 AA.
AC Q8BMB3; O88503; Q3UCK2;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Eukaryotic translation initiation factor 4E type 2 {ECO:0000303|PubMed:15153109};
DE Short=eIF-4E type 2 {ECO:0000303|PubMed:15153109};
DE Short=eIF4E type 2 {ECO:0000303|PubMed:15153109};
DE Short=eIF4E-2 {ECO:0000303|PubMed:15153109};
DE Short=mRNA cap-binding protein type 2 {ECO:0000303|PubMed:15153109};
DE AltName: Full=Eukaryotic translation initiation factor 4E-like 3;
DE AltName: Full=eIF4E-like protein 4E-LP {ECO:0000303|PubMed:15153109};
GN Name=Eif4e2 {ECO:0000303|PubMed:15153109, ECO:0000312|MGI:MGI:1914440};
GN Synonyms=Eif4el3;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF4EBP1; EIF4EBP2
RP AND EIF4EBP3, AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss;
RX PubMed=15153109; DOI=10.1111/j.1432-1033.2004.04149.x;
RA Joshi B., Cameron A., Jagus R.;
RT "Characterization of mammalian eIF4E-family members.";
RL Eur. J. Biochem. 271:2189-2203(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Mesonephros;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=22751931; DOI=10.1128/mcb.00455-12;
RA Morita M., Ler L.W., Fabian M.R., Siddiqui N., Mullin M., Henderson V.C.,
RA Alain T., Fonseca B.D., Karashchuk G., Bennett C.F., Kabuta T., Higashi S.,
RA Larsson O., Topisirovic I., Smith R.J., Gingras A.C., Sonenberg N.;
RT "A novel 4EHP-GIGYF2 translational repressor complex is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 32:3585-3593(2012).
CC -!- FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation (PubMed:15153109). Acts as a
CC repressor of translation initiation (By similarity). In contrast to
CC EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3),
CC suggesting that it acts by competing with EIF4E and block assembly of
CC eIF4F at the cap (PubMed:15153109). In P-bodies, component of a complex
CC that promotes miRNA-mediated translational repression (By similarity).
CC {ECO:0000250|UniProtKB:O60573, ECO:0000269|PubMed:15153109}.
CC -!- SUBUNIT: Interacts with EIF4EBP1, EIF4EBP2 and EIF4EBP3
CC (PubMed:15153109). Does not interact with eIF4G (EIF4G1, EIF4G2 or
CC EIF4G3) (PubMed:15153109). Component of the 4EHP-GYF2 complex, at least
CC composed of EIF4E2, GIGYF2 and ZNF598 (By similarity). Interacts with
CC GIGYF2 (via the 4EHP-binding motif); the interaction is direct (By
CC similarity). Interacts with EIF4ENIF1/4E-T (via YXXXXLphi motif);
CC increasing affinity for the 7-methylguanosine-containing mRNA cap (By
CC similarity). {ECO:0000250|UniProtKB:O60573,
CC ECO:0000269|PubMed:15153109}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60573}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:O60573}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis,
CC kidney and liver. {ECO:0000269|PubMed:15153109}.
CC -!- PTM: Ubiquitinated by ARIH1. The consequences of ubiquitination are
CC however unclear: according to a report, EIF4E2 ubiquitination leads to
CC promote EIF4E2 cap-binding and protein translation arrest. According to
CC another report ubiquitination leads to its subsequent degradation.
CC {ECO:0000250|UniProtKB:O60573}.
CC -!- PTM: ISGylation enhances its cap structure-binding activity and
CC translation-inhibition activity. {ECO:0000250|UniProtKB:O60573}.
CC -!- DISRUPTION PHENOTYPE: Lethality; mice die just before birth.
CC {ECO:0000269|PubMed:22751931}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AF068116; AAC19373.1; -; mRNA.
DR EMBL; AK032965; BAC28102.1; -; mRNA.
DR EMBL; AK150495; BAE29610.1; -; mRNA.
DR EMBL; BC045153; AAH45153.1; -; mRNA.
DR CCDS; CCDS35652.1; -.
DR RefSeq; NP_001034259.1; NM_001039170.1.
DR RefSeq; NP_075803.2; NM_023314.3.
DR AlphaFoldDB; Q8BMB3; -.
DR SMR; Q8BMB3; -.
DR BioGRID; 205093; 2.
DR IntAct; Q8BMB3; 3.
DR MINT; Q8BMB3; -.
DR STRING; 10090.ENSMUSP00000108859; -.
DR iPTMnet; Q8BMB3; -.
DR PhosphoSitePlus; Q8BMB3; -.
DR EPD; Q8BMB3; -.
DR MaxQB; Q8BMB3; -.
DR PaxDb; Q8BMB3; -.
DR PeptideAtlas; Q8BMB3; -.
DR PRIDE; Q8BMB3; -.
DR ProteomicsDB; 266946; -.
DR Antibodypedia; 20222; 431 antibodies from 30 providers.
DR DNASU; 26987; -.
DR Ensembl; ENSMUST00000113233; ENSMUSP00000108859; ENSMUSG00000026254.
DR GeneID; 26987; -.
DR KEGG; mmu:26987; -.
DR UCSC; uc007bwk.1; mouse.
DR CTD; 9470; -.
DR MGI; MGI:1914440; Eif4e2.
DR VEuPathDB; HostDB:ENSMUSG00000026254; -.
DR eggNOG; KOG1669; Eukaryota.
DR GeneTree; ENSGT00940000154694; -.
DR InParanoid; Q8BMB3; -.
DR TreeFam; TF101529; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR BioGRID-ORCS; 26987; 16 hits in 71 CRISPR screens.
DR ChiTaRS; Eif4e2; mouse.
DR PRO; PR:Q8BMB3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BMB3; protein.
DR Bgee; ENSMUSG00000026254; Expressed in internal carotid artery and 261 other tissues.
DR ExpressionAtlas; Q8BMB3; baseline and differential.
DR Genevisible; Q8BMB3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Translation regulation; Ubl conjugation.
FT CHAIN 1..245
FT /note="Eukaryotic translation initiation factor 4E type 2"
FT /id="PRO_0000193665"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..57
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT REGION 95..99
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT REGION 150..157
FT /note="EIF4EBP1/2/3 binding"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT COMPBIAS 1..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..79
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT BINDING 110
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT BINDING 124..125
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT BINDING 174..179
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT BINDING 222..224
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P06730"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT MOD_RES 134
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15); alternate"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:O60573"
FT CONFLICT 200
FT /note="L -> F (in Ref. 1; AAC19373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 28263 MW; AA722843721A01CC CRC64;
MNNKFDALKD DDSGDHDQNE ENSTQKDGEK EKTDRDKSQS SGKRKAVVPG PAEHPLQYNY
TFWYSRRTPG RPTSSQSYEQ NIKQIGTFAS VEQFWKFYSH MVRPGDLTGH SDFHLFKEGI
KPMWEDDANK NGGKWIIRLR KGLASRCWEN LILAMLGEQF MVGEEICGAV VSVRFQEDII
SIWNKTASDQ ATTARIRDTL RRVLNLPPNT IMEYKTHTDS IKMPGRLGPQ RLLFQNLWKP
RLNVP
