IF2G_MOUSE
ID IF2G_MOUSE Reviewed; 472 AA.
AC Q9Z0N1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3, X-linked;
DE EC=3.6.5.3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma, X-linked;
DE Short=eIF-2-gamma X;
GN Name=Eif2s3x;
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], TISSUE SPECIFICITY, AND ESCAPE FROM
RP X-INACTIVATION.
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=9736774; DOI=10.1093/hmg/7.11.1725;
RA Ehrmann I.E., Ellis P.S., Mazeyrat S., Duthie S., Brockdorff N.,
RA Mattei M.-G., Gavin M.A., Affara N.A., Brown G.M., Simpson E.,
RA Mitchell M.J., Scott D.M.;
RT "Characterization of genes encoding translation initiation factor eIF-
RT 2gamma in mouse and human: sex chromosome localization, escape from X-
RT inactivation and evolution.";
RL Hum. Mol. Genet. 7:1725-1737(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=12023983; DOI=10.1093/hmg/11.12.1409;
RA Xu J., Burgoyne P.S., Arnold A.P.;
RT "Sex differences in sex chromosome gene expression in mouse brain.";
RL Hum. Mol. Genet. 11:1409-1419(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16325480; DOI=10.1016/j.modgep.2005.06.011;
RA Xu J., Watkins R., Arnold A.P.;
RT "Sexually dimorphic expression of the X-linked gene Eif2s3x mRNA but not
RT protein in mouse brain.";
RL Gene Expr. Patterns 6:146-155(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-16, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Pancreas, Spleen, and
RC 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 [7]
RP FUNCTION.
RX PubMed=26823431; DOI=10.1126/science.aad1795;
RA Yamauchi Y., Riel J.M., Ruthig V.A., Ortega E.A., Mitchell M.J., Ward M.A.;
RT "Two genes substitute for the mouse Y chromosome for spermatogenesis and
RT reproduction.";
RL Science 351:514-516(2016).
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC involved in the early steps of protein synthesis. In the presence of
CC GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC step that determines the rate of protein translation. The 43S PIC binds
CC to mRNA and scans downstream to the initiation codon, where it forms a
CC 48S initiation complex by codon-anticodon base pairing. This leads to
CC the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B (By similarity). Along with its paralog on
CC chromosome Y, may contribute to spermatogenesis up to the round
CC spermatid stage (PubMed:26823431). {ECO:0000250|UniProtKB:P32481,
CC ECO:0000269|PubMed:26823431}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: The eukaryotic translation initiation factor 2 complex/eIF2 is
CC a heterotrimer composed of an alpha subunit, also called subunit 1
CC (encoded by EIF2S1), a beta subunit, also called subunit 2 (encoded by
CC EIF2S2) and a gamma subunit, also called subunit 3 (encoded by 2
CC homologous genes Eif2s3x and Eif2s3y). {ECO:0000250|UniProtKB:P41091}.
CC -!- TISSUE SPECIFICITY: Widely expressed. In the brain, high mRNA levels
CC are observed in specific regions, including the habenula, anterodorsal
CC thalamic nucleus, hippocampus, hypothalamus, and cerebellum. Also
CC expressed in the embryonic brain. There is a differential expression
CC between males and females, wich is tissue-specific. Females tend to
CC have higher expression levels than males in the brain (cortex,
CC hippocampus and paraventricular nucleus, but not in the habenula), as
CC well as in other tissues. The up-regulation observed in females at the
CC mRNA level may be due to the presence of 2 active copies of the gene.
CC {ECO:0000269|PubMed:12023983, ECO:0000269|PubMed:16325480,
CC ECO:0000269|PubMed:9736774}.
CC -!- MISCELLANEOUS: Encoded by an chromosome X-linked gene which escapes
CC inactivation. Has a homolog on chromosome Y (Eif2s3y).
CC {ECO:0000269|PubMed:9736774}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; AJ006587; CAA07099.1; -; mRNA.
DR EMBL; BC063755; AAH63755.1; -; mRNA.
DR CCDS; CCDS30277.1; -.
DR RefSeq; NP_036140.1; NM_012010.3.
DR AlphaFoldDB; Q9Z0N1; -.
DR SMR; Q9Z0N1; -.
DR BioGRID; 205054; 29.
DR IntAct; Q9Z0N1; 1.
DR STRING; 10090.ENSMUSP00000059395; -.
DR iPTMnet; Q9Z0N1; -.
DR PhosphoSitePlus; Q9Z0N1; -.
DR SwissPalm; Q9Z0N1; -.
DR EPD; Q9Z0N1; -.
DR jPOST; Q9Z0N1; -.
DR MaxQB; Q9Z0N1; -.
DR PaxDb; Q9Z0N1; -.
DR PRIDE; Q9Z0N1; -.
DR ProteomicsDB; 267210; -.
DR Ensembl; ENSMUST00000050328; ENSMUSP00000059395; ENSMUSG00000035150.
DR GeneID; 26905; -.
DR KEGG; mmu:26905; -.
DR UCSC; uc009ttc.1; mouse.
DR CTD; 26905; -.
DR MGI; MGI:1349431; Eif2s3x.
DR VEuPathDB; HostDB:ENSMUSG00000035150; -.
DR eggNOG; KOG0466; Eukaryota.
DR GeneTree; ENSGT00550000074801; -.
DR HOGENOM; CLU_027154_0_1_1; -.
DR InParanoid; Q9Z0N1; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 903135at2759; -.
DR PhylomeDB; Q9Z0N1; -.
DR TreeFam; TF101513; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-381042; PERK regulates gene expression.
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 26905; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Eif2s3x; mouse.
DR PRO; PR:Q9Z0N1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9Z0N1; protein.
DR Bgee; ENSMUSG00000035150; Expressed in ectoplacental cone and 250 other tissues.
DR ExpressionAtlas; Q9Z0N1; baseline and differential.
DR Genevisible; Q9Z0N1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; GTP-binding; Hydrolase; Initiation factor; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..472
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 3, X-linked"
FT /id="PRO_0000137439"
FT DOMAIN 39..248
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 48..55
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 76..80
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 134..137
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 190..193
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 225..227
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 51..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 190..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 225..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
SQ SEQUENCE 472 AA; 51065 MW; 63CA694C06ED4CB9 CRC64;
MAGGEGGVTL GQPHLSRQDL ATLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA
ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE CYRSCGSSTP DEFPTDIPGT
KGNFKLVRHV SFVDCPGHDI LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM
KLKHILILQN KIDLVKESQA KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV
KKIPVPPRDF TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA DRMVGQVLGA
VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK NEVLMVNIGS LSTGGRVSAV
KADLGKIVLT NPVCTEVGEK IALSRRVEKH WRLIGWGQIR RGVTIKPTVD DD
