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Database: UniProt
Entry: A0A0J9YUS5_MOUSE
LinkDB: A0A0J9YUS5_MOUSE
Original site: A0A0J9YUS5_MOUSE 
ID   A0A0J9YUS5_MOUSE        Unreviewed;      1303 AA.
AC   A0A0J9YUS5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Eukaryotic translation initiation factor 4, gamma 1 {ECO:0000313|Ensembl:ENSMUSP00000144320.2};
GN   Name=Eif4g1 {ECO:0000313|Ensembl:ENSMUSP00000144320.2,
GN   ECO:0000313|MGI:MGI:2384784};
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 {ECO:0000313|Ensembl:ENSMUSP00000144320.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:17242355}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [2] {ECO:0007829|PubMed:18630941}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [3] {ECO:0007829|PubMed:19144319}
RP   IDENTIFICATION BY 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   [4] {ECO:0007829|PubMed:19131326}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [5] {ECO:0000313|Ensembl:ENSMUSP00000144320.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144320.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [7] {ECO:0007829|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [8] {ECO:0007829|PubMed:24129315}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24129315;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [9] {ECO:0000313|Ensembl:ENSMUSP00000144320.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144320.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000256|ARBA:ARBA00005775}.
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DR   RefSeq; XP_017172409.1; XM_017316920.1.
DR   SMR; A0A0J9YUS5; -.
DR   jPOST; A0A0J9YUS5; -.
DR   ProteomicsDB; 345565; -.
DR   Antibodypedia; 3406; 709 antibodies from 37 providers.
DR   Ensembl; ENSMUST00000143939.8; ENSMUSP00000144320.2; ENSMUSG00000045983.17.
DR   AGR; MGI:2384784; -.
DR   MGI; MGI:2384784; Eif4g1.
DR   VEuPathDB; HostDB:ENSMUSG00000045983; -.
DR   GeneTree; ENSGT00940000154648; -.
DR   BioGRID-ORCS; 208643; 7 hits in 65 CRISPR screens.
DR   ChiTaRS; Eif4g1; mouse.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000045983; Expressed in lacrimal gland and 257 other cell types or tissues.
DR   ExpressionAtlas; A0A0J9YUS5; baseline and differential.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd11559; W2_eIF4G1_like; 1.
DR   Gene3D; 1.25.40.180; -; 3.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF10; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 1; 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; ARM repeat; 3.
DR   PROSITE; PS51366; MI; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   Proteomics identification {ECO:0007829|EPD:A0A0J9YUS5,
KW   ECO:0007829|MaxQB:A0A0J9YUS5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          944..1066
FT                   /note="MI"
FT                   /evidence="ECO:0000259|PROSITE:PS51366"
FT   DOMAIN          1132..1302
FT                   /note="W2"
FT                   /evidence="ECO:0000259|PROSITE:PS51363"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          68..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..820
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          832..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..184
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..846
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..926
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1303 AA;  145313 MW;  93B67E43C9D8FAD2 CRC64;
     MTTGMIPMSV EESTPISCET GEPYCLSPEP TLAEPILEVE VTLSKPIPES EFSSSPLQVS
     TALVPHKVET HEPNGVIPSE DLEPEVESST EPAPPPLSPC ASESLVPIAP TAQPEELLNG
     APSPPAVDLS PVSEPEEQAK KVSSAALASI LSPAPPVAPS DTSPAQEEEM EEDDDDEEGG
     EAESEKGGED VPLDSTPVPA QLSQNLEVAA ATQVAVSVPK RRRKIKELNK KEAVGDLLDA
     FKEVDPAVPE VENQPPTGSN PSPESEGSMV PTQPEETEET WDSKEDKIHN AENIQPGEQK
     YEYKSDQWKP LNLEEKKRYD REFLLGFQFI FASMQKPEGL PHITDVVLDK ANKTPLRQLD
     PSRLPGINCG PDFTPSFANL GRPALSNRGP PRGGPGGELP RGPAGLGPRR SQQGPRKETR
     KIISSVIMTE DIKLNKAEKA WKPSSKRTAA DKDRGEEDAD GSKTQDLFRR VRSILNKLTP
     QMFQQLMKQV TQLAIDTEER LKGVIDLIFE KAISEPNFSV AYANMCRCLM ALKVPTTEKP
     TVTVNFRKLL LNRCQKEFEK DKDDDEVFEK KQKEMDEAAT AEERGRLKEE LEEARDIARR
     RSLGNIKFIG ELFKLKMLTE AIMHDCVVKL LKNHDEESLE CLCRLLTTIG KDLDFAKAKP
     RMDQYFNQME KIIKEKKTSS RIRFMLQDVL DLRQSNWVPR RGDQGPKTID QIHKEAEMEE
     HREHIKVQQL MAKGSDKRRG GPPGPPINRG LPLVDDGGWN TVPISKGSRP IDTSRLTKIT
     KPGSIDSNNQ LFAPGGRLSW GKGSSGGSGA KPSDTASEAT RPATLNRFSA LQQTLPAENT
     DNRRVVQRSS LSRERGEKAG DRGDRLERSE RGGDRGDRLD RARTPATKRS FSKEVEERSR
     ERPSQPEGLR KAASLTEDRG RDPVKREATL PPVSPPKAAL SVDEVEKKSK AIIEEYLHLN
     DMKEAVQCVQ ELASPSLLFI FVRLGIESTL ERSTIAREHM GRLLHQLLCA GHLSTAQYYQ
     GLYETLELAE DMEIDIPHVW LYLAELITPI LQEDGVPMGE LFREITKPLR PMGKATSLLL
     EILGLLCKSM GPKKVGMLWR EAGLSWREFL AEGQDVGSFV AEKKVEYTLG EESEAPGQRT
     LAFEELRRQL EKLLKDGGSN QRVFDWIDAN LNEQQIASNT LVRALMTTVC YSAIIFETPL
     RVDVQVLKVR ARLLQKYLCD EQKELQALYA LQALVVTLEQ PANLLRMFFD ALYDEDVVKE
     DAFYSWESSK DPAEQQGKGV ALKSVTAFFN WLREAEDEES DHN
//
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