ID EF1G_HORSE Reviewed; 437 AA.
AC A2Q127;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
GN Name=EEF1G;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Thoroughbred; TISSUE=Tendon;
RA Hasegawa T., Hayashi K., Kagawa Y., Akiyama Y., Suzuki Y., Sugano S.,
RA Ishida N.;
RT "Cloning of genes expressed in equine tendon.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000250}.
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DR EMBL; AB292250; BAF46268.1; -; mRNA.
DR RefSeq; NP_001075254.1; NM_001081785.1.
DR AlphaFoldDB; A2Q127; -.
DR BMRB; A2Q127; -.
DR SMR; A2Q127; -.
DR STRING; 9796.ENSECAP00000012558; -.
DR PaxDb; 9796-ENSECAP00000012558; -.
DR PeptideAtlas; A2Q127; -.
DR GeneID; 100009686; -.
DR KEGG; ecb:100009686; -.
DR CTD; 1937; -.
DR HOGENOM; CLU_011226_3_1_1; -.
DR InParanoid; A2Q127; -.
DR OrthoDB; 159792at2759; -.
DR TreeFam; TF314343; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 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 PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR PANTHER; PTHR43986:SF12; ELONGATION FACTOR 1-GAMMA; 1.
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 SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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_0000286045"
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; 50049 MW; DC9F0CDF139E68C2 CRC64;
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
MHHNKQATEN AKEEVRRILG LLDAHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEEAQ TLVREYFSWE
GAFQHVGKAF NQGKIFK
//
