ID E9Q9E1_MOUSE Unreviewed; 1593 AA.
AC E9Q9E1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Eukaryotic translation initiation factor 4, gamma 1 {ECO:0000313|Ensembl:ENSMUSP00000073506.6};
GN Name=Eif4g1 {ECO:0000313|Ensembl:ENSMUSP00000073506.6,
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:ENSMUSP00000073506.6, 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:ENSMUSP00000073506.6, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000073506.6,
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:ENSMUSP00000073506.6}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000073506.6};
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_006522003.1; XM_006521940.3.
DR SMR; E9Q9E1; -.
DR SwissPalm; E9Q9E1; -.
DR jPOST; E9Q9E1; -.
DR MaxQB; E9Q9E1; -.
DR PeptideAtlas; E9Q9E1; -.
DR ProteomicsDB; 347332; -.
DR Antibodypedia; 3406; 709 antibodies from 37 providers.
DR DNASU; 208643; -.
DR Ensembl; ENSMUST00000073840.12; ENSMUSP00000073506.6; ENSMUSG00000045983.17.
DR GeneID; 208643; -.
DR UCSC; uc007yqw.2; mouse.
DR AGR; MGI:2384784; -.
DR CTD; 1981; -.
DR MGI; MGI:2384784; Eif4g1.
DR VEuPathDB; HostDB:ENSMUSG00000045983; -.
DR GeneTree; ENSGT00940000154648; -.
DR OrthoDB; 92033at2759; -.
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; E9Q9E1; baseline and differential.
DR Genevisible; E9Q9E1; MM.
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:E9Q9E1,
KW ECO:0007829|MaxQB:E9Q9E1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 1234..1356
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT DOMAIN 1422..1592
FT /note="W2"
FT /evidence="ECO:0000259|PROSITE:PS51363"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..274
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1593 AA; 175331 MW; 9704D7543ED4972C CRC64;
MNKAPQPTGP PPARSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH FYPSRAQPPS
SAASRVQSAA PARPGPAPHV YPAGSQVMMI PSQISYSASQ GAYYIPGQGR STYVVPTQQY
PVQPGAPGFY PGASPTEFGT YAGAYYPAQG VQQFPASVAP APVLMNQPPQ IAPKRERKTI
RIRDPNQGGK DITEEIMSGA RTASTPTPPQ TGGSLEPQPN GESPQVAVII RPDDRSQGAA
IGGRPGLPGP EHSPGTESQP SSPSPTPSPP PILEPGSESN LGVLSIPGDT 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
//
