IF4E3_MOUSE
ID IF4E3_MOUSE Reviewed; 207 AA.
AC Q9DBB5; Q9D983;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Eukaryotic translation initiation factor 4E type 3;
DE Short=eIF-4E type 3;
DE Short=eIF-4E3;
DE Short=eIF4E type 3;
DE Short=eIF4E-3;
GN Name=Eif4e3;
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, TISSUE SPECIFICITY, AND INTERACTION
RP WITH EIF4G1.
RC STRAIN=Czech II; TISSUE=Lung tumor;
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=Liver, and Testis;
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 tumor;
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=Lung;
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: Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis. May
CC act as an inhibitor of EIF4E1 activity. {ECO:0000269|PubMed:15153109}.
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 (By similarity). EIF4E3
CC interacts with EIF4G1, but not with EIF4EBP1, EIF4EBP2 and EIF4EBP3.
CC {ECO:0000250, ECO:0000269|PubMed:15153109}.
CC -!- TISSUE SPECIFICITY: Only expressed in heart, skeletal muscle, lung and
CC spleen. {ECO:0000269|PubMed:15153109}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AY628329; AAT45741.1; -; mRNA.
DR EMBL; AK005054; BAB23780.1; -; mRNA.
DR EMBL; AK007268; BAB24928.1; -; mRNA.
DR EMBL; BC027014; AAH27014.1; -; mRNA.
DR CCDS; CCDS20386.1; -.
DR RefSeq; NP_080105.1; NM_025829.4.
DR PDB; 4B6U; NMR; -; A=1-207.
DR PDB; 4B6V; NMR; -; A=1-207.
DR PDBsum; 4B6U; -.
DR PDBsum; 4B6V; -.
DR AlphaFoldDB; Q9DBB5; -.
DR BMRB; Q9DBB5; -.
DR SMR; Q9DBB5; -.
DR BioGRID; 211792; 2.
DR STRING; 10090.ENSMUSP00000032151; -.
DR iPTMnet; Q9DBB5; -.
DR PhosphoSitePlus; Q9DBB5; -.
DR REPRODUCTION-2DPAGE; Q9DBB5; -.
DR EPD; Q9DBB5; -.
DR MaxQB; Q9DBB5; -.
DR PaxDb; Q9DBB5; -.
DR PeptideAtlas; Q9DBB5; -.
DR PRIDE; Q9DBB5; -.
DR ProteomicsDB; 269376; -.
DR Antibodypedia; 31921; 109 antibodies from 25 providers.
DR DNASU; 66892; -.
DR Ensembl; ENSMUST00000032151; ENSMUSP00000032151; ENSMUSG00000093661.
DR GeneID; 66892; -.
DR KEGG; mmu:66892; -.
DR UCSC; uc009dbr.1; mouse.
DR CTD; 317649; -.
DR MGI; MGI:1914142; Eif4e3.
DR VEuPathDB; HostDB:ENSMUSG00000093661; -.
DR eggNOG; ENOG502QPP4; Eukaryota.
DR GeneTree; ENSGT00940000155865; -.
DR HOGENOM; CLU_043552_5_1_1; -.
DR InParanoid; Q9DBB5; -.
DR OMA; SYFYKRH; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; Q9DBB5; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR BioGRID-ORCS; 66892; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Eif4e3; mouse.
DR PRO; PR:Q9DBB5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9DBB5; protein.
DR Bgee; ENSMUSG00000093661; Expressed in primary oocyte and 241 other tissues.
DR Genevisible; Q9DBB5; MM.
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:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome;
KW RNA-binding; Translation regulation.
FT CHAIN 1..207
FT /note="Eukaryotic translation initiation factor 4E type 3"
FT /id="PRO_0000287698"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..99
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"
FT BINDING 152..157
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"
FT CONFLICT 122
FT /note="W -> G (in Ref. 2; BAB24928)"
FT /evidence="ECO:0000305"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:4B6V"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 31..41
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4B6U"
FT TURN 101..105
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4B6U"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:4B6U"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:4B6U"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4B6U"
FT HELIX 173..180
FT /evidence="ECO:0007829|PDB:4B6U"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:4B6U"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4B6U"
SQ SEQUENCE 207 AA; 22836 MW; 0263A317BFD0A4C1 CRC64;
MALPPAAAPP GANEPLDKAL SALPPEPGGV PLHSPWTFWL DRSLPGATAA ECASNLKKIY
TVQTVQIFWS VYNNIPPVTS LPLRCSYHLM RGERRPLWEE ESNAKGGVWK MKVPKDSTST
VWKELLLATI GEQFTDCAAA DDEIIGVSVS VRDREDVVQV WNVNASLVGE ATVLEKIHQL
LPHIAFKAVF YKPHEEHHAF EGGRGKH
