EF1G_RAT
ID EF1G_RAT Reviewed; 437 AA.
AC Q68FR6; Q4FZZ5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
GN Name=Eef1g;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen, and Testis;
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).
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma.
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DR EMBL; BC079398; AAH79398.1; -; mRNA.
DR EMBL; BC098895; AAH98895.1; -; mRNA.
DR RefSeq; NP_001004223.1; NM_001004223.2.
DR AlphaFoldDB; Q68FR6; -.
DR SMR; Q68FR6; -.
DR BioGRID; 254421; 5.
DR IntAct; Q68FR6; 4.
DR MINT; Q68FR6; -.
DR STRING; 10116.ENSRNOP00000027305; -.
DR iPTMnet; Q68FR6; -.
DR PhosphoSitePlus; Q68FR6; -.
DR SwissPalm; Q68FR6; -.
DR World-2DPAGE; 0004:Q68FR6; -.
DR jPOST; Q68FR6; -.
DR PaxDb; Q68FR6; -.
DR PRIDE; Q68FR6; -.
DR Ensembl; ENSRNOT00000027305; ENSRNOP00000027305; ENSRNOG00000020075.
DR GeneID; 293725; -.
DR KEGG; rno:293725; -.
DR UCSC; RGD:1302939; rat.
DR CTD; 1937; -.
DR RGD; 1302939; Eef1g.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00390000007552; -.
DR HOGENOM; CLU_011226_3_1_1; -.
DR InParanoid; Q68FR6; -.
DR OMA; TRWYETI; -.
DR OrthoDB; 1341490at2759; -.
DR PhylomeDB; Q68FR6; -.
DR TreeFam; TF314343; -.
DR Reactome; R-RNO-156842; Eukaryotic Translation Elongation.
DR PRO; PR:Q68FR6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020075; Expressed in spleen and 19 other tissues.
DR Genevisible; Q68FR6; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.70.1010; -; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF89942; SSF89942; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Elongation factor; Isopeptide bond; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT CHAIN 2..437
FT /note="Elongation factor 1-gamma"
FT /id="PRO_0000208817"
FT DOMAIN 2..87
FT /note="GST N-terminal"
FT DOMAIN 88..216
FT /note="GST C-terminal"
FT DOMAIN 276..437
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 221..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT MOD_RES 147
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT MOD_RES 212
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D8N0"
FT MOD_RES 434
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT MOD_RES 434
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P26641"
FT CROSSLNK 285
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26641"
SQ SEQUENCE 437 AA; 50061 MW; D1AF3BE9FADB2F3E CRC64;
MAAGTLYTYP ENWRAFKALI AAQYSGAQIR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
MHHNKQATEN AKEEVKRILG LLDTHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
RQAFPNTNRW FLTCINQPQF RAILGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE
KQKPQTERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
DTLSVALPYF WEHFDKDGWS LWYAEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
ILFGTNNSSS ISGVWVFRGQ DLAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE
GAFQHVGKAV NQGKIFK
