EFGM_MOUSE
ID EFGM_MOUSE Reviewed; 751 AA.
AC Q8K0D5; Q921D6; Q924I0;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Elongation factor G, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=EF-Gmt {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03061};
DE Short=mEF-G 1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE AltName: Full=Elongation factor G1 {ECO:0000255|HAMAP-Rule:MF_03061};
DE Flags: Precursor;
GN Name=Gfm1; Synonyms=Efg, Efg1, Gfm;
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].
RX PubMed=11374907; DOI=10.1006/geno.2001.6536;
RA Gao J., Yu L., Zhang P., Jiang J., Chen J., Peng J., Wei Y., Zhao S.;
RT "Cloning and characterization of human and mouse mitochondrial elongation
RT factor G, GFM and gfm, and mapping of GFM to human chromosome 3q25.1-
RT q26.2.";
RL Genomics 74:109-114(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Mitochondrial GTPase that catalyzes the GTP-dependent
CC ribosomal translocation step during translation elongation. During this
CC step, the ribosome changes from the pre-translocational (PRE) to the
CC post-translocational (POST) state as the newly formed A-site-bound
CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E
CC sites, respectively. Catalyzes the coordinated movement of the two tRNA
CC molecules, the mRNA and conformational changes in the ribosome. Does
CC not mediate the disassembly of ribosomes from messenger RNA at the
CC termination of mitochondrial protein biosynthesis. {ECO:0000255|HAMAP-
CC Rule:MF_03061}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_03061}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000305}.
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DR EMBL; AF315511; AAK58878.1; -; mRNA.
DR EMBL; BC013093; AAH13093.1; -; mRNA.
DR EMBL; BC031772; AAH31772.1; -; mRNA.
DR CCDS; CCDS38449.1; -.
DR RefSeq; NP_613057.2; NM_138591.2.
DR AlphaFoldDB; Q8K0D5; -.
DR SMR; Q8K0D5; -.
DR BioGRID; 205725; 5.
DR IntAct; Q8K0D5; 1.
DR STRING; 10090.ENSMUSP00000076503; -.
DR iPTMnet; Q8K0D5; -.
DR PhosphoSitePlus; Q8K0D5; -.
DR SwissPalm; Q8K0D5; -.
DR EPD; Q8K0D5; -.
DR jPOST; Q8K0D5; -.
DR MaxQB; Q8K0D5; -.
DR PaxDb; Q8K0D5; -.
DR PeptideAtlas; Q8K0D5; -.
DR PRIDE; Q8K0D5; -.
DR ProteomicsDB; 277799; -.
DR Antibodypedia; 46773; 191 antibodies from 28 providers.
DR Ensembl; ENSMUST00000077271; ENSMUSP00000076503; ENSMUSG00000027774.
DR GeneID; 28030; -.
DR KEGG; mmu:28030; -.
DR UCSC; uc008plm.2; mouse.
DR CTD; 85476; -.
DR MGI; MGI:107339; Gfm1.
DR VEuPathDB; HostDB:ENSMUSG00000027774; -.
DR eggNOG; KOG0465; Eukaryota.
DR GeneTree; ENSGT00550000074911; -.
DR HOGENOM; CLU_002794_4_1_1; -.
DR InParanoid; Q8K0D5; -.
DR OMA; AATTCHW; -.
DR OrthoDB; 637899at2759; -.
DR PhylomeDB; Q8K0D5; -.
DR TreeFam; TF105631; -.
DR Reactome; R-MMU-5389840; Mitochondrial translation elongation.
DR UniPathway; UPA00345; -.
DR BioGRID-ORCS; 28030; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Gfm1; mouse.
DR PRO; PR:Q8K0D5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8K0D5; protein.
DR Bgee; ENSMUSG00000027774; Expressed in myocardium of ventricle and 261 other tissues.
DR Genevisible; Q8K0D5; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
DR GO; GO:0070125; P:mitochondrial translational elongation; ISS:UniProtKB.
DR CDD; cd16262; EFG_III; 1.
DR CDD; cd01434; EFG_mtEFG1_IV; 1.
DR CDD; cd04097; mtEFG1_C; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR InterPro; IPR045044; EFG1-like.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR009022; EFG_III.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR035649; EFG_V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR004540; Transl_elong_EFG/EF2.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR43636; PTHR43636; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00484; EF-G; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Elongation factor; GTP-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT CHAIN 38..751
FT /note="Elongation factor G, mitochondrial"
FT /id="PRO_0000007441"
FT DOMAIN 45..322
FT /note="tr-type G"
FT BINDING 54..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 121..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT BINDING 175..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03061"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RP9"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96RP9"
FT CONFLICT 120
FT /note="I -> M (in Ref. 1; AAK58878)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="G -> R (in Ref. 1; AAK58878)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="K -> E (in Ref. 1; AAK58878)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="P -> S (in Ref. 2; AAH13093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 83550 MW; 75A3FB52ECAC3A42 CRC64;
MRLLRVAAAL GRGPFPRVPA VLGWQGKQAD WKTRRWCSSG PVPNEKIRNI GISAHIDSGK
TTLTERVLYY TGRIATMHEV KGKDGVGAVM DSMELERQRG ITIQSAATYT MWKDININII
DTPGHVDFTI EVERALRVLD GAVLVLCAVG GVQCQTMTVS RQMKRYNVPF LTFINKLDRM
GSNPSRALQQ MRSKLNHNAA FVQIPIGLEG DFKGIIDLIE ERAIYFDGDF GQIVRYDEIP
AGLRAAAADH RQELIECVAN SDEQLGELFL EEKIPSVSDL KRAIRRATLS RSFTPVFLGS
ALKNKGVQPL LDAVLEYLPN PSEVQNYAIL NQNDSKEKTK ILMNPQRDDS HPFVGLAFKL
EAGRFGQLTY VRNYQGELKK GSTIYNTRTG KKVRVQRLVR MHADMMEDVE EVYAGDICAL
FGIDCASGDT FTNKDNSDLS MESIHVPEPV ISIAMRPSNK NDLEKFSKGI GRFTREDPTF
KVHFDPESKE TIVSGMGELH LEIYAQRMER EYGCPCITGK PKVAFRETIV APVPFDFTHK
KQSGGAGQFG KVIGVLEPLP PEDYTKLEFS DETFGSNVPK QFVPAVEKGF LDACEKGPLS
GHKLSGLRFV LQDGAHHMVD SNEISFIRAG EGALKQALAN GTLCIIEPIM SVEVIAPNEF
QGTVFAGINR RHGVITGQDG IEDYFTLYAD VPLNNMFGYS TELRSCTEGK GEYTMEYCRY
QPCSPSTQEE LINKYLEATG QLPVKKGKAK N
