IF2G_RABIT
ID IF2G_RABIT Reviewed; 152 AA.
AC P33887; Q9TRV8; Q9TRV9; Q9TRW0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE Short=eIF-2-gamma;
DE Flags: Fragments;
GN Name=EIF2S3; Synonyms=EIF2G;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 1-22.
RC TISSUE=Reticulocyte;
RX PubMed=3745199; DOI=10.1016/s0021-9258(18)67107-8;
RA Wettenhall R.E.H., Kudlicki W., Kramer G., Hardesty B.;
RT "The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic
RT initiation factor 2 and the phosphorylation site for the heme-regulated
RT eIF-2 alpha kinase.";
RL J. Biol. Chem. 261:12444-12447(1986).
RN [2]
RP PROTEIN SEQUENCE OF 1-15 AND 82-126.
RC TISSUE=Reticulocyte;
RX PubMed=1911855; DOI=10.1016/0167-4838(91)90074-a;
RA Bommer U.-A., Kraft R., Kurzchalia T.V., Price N.T., Proud C.G.;
RT "Amino acid sequence analysis of the beta- and gamma-subunits of eukaryotic
RT initiation factor eIF-2. Identification of regions interacting with GTP.";
RL Biochim. Biophys. Acta 1079:308-315(1991).
RN [3]
RP PROTEIN SEQUENCE OF 1-8.
RC TISSUE=Reticulocyte;
RX PubMed=3592677; DOI=10.1016/0003-9861(87)90401-2;
RA Schafer M.P., Fairwell T., Parker D.S., Knight M., Anderson W.F., Safer B.;
RT "The purification and characterization of subunits alpha, beta, and gamma
RT from the rabbit reticulocyte eukaryotic initiation factor 2.";
RL Arch. Biochem. Biophys. 255:337-346(1987).
RN [4]
RP PROTEIN SEQUENCE OF 23-99 AND 102-152.
RX PubMed=8417348; DOI=10.1128/mcb.13.1.506-520.1993;
RA Hannig E.M., Cigan A.M., Freeman B.A., Kinzy T.G.;
RT "GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit
RT of eIF-2 in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:506-520(1993).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This complex
CC binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC 43S preinitiation complex. Junction of the 60S ribosomal subunit to
CC form the 80S initiation complex is preceded by hydrolysis of the GTP
CC bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC eIF-2 to recycle and catalyze another round of initiation, the GDP
CC bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC eIF-2B.
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 EIF2S3).
CC {ECO:0000250|UniProtKB:P41091}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EIF2G
CC subfamily. {ECO:0000305}.
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DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; NAS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; NAS:UniProtKB.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; GTP-binding; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..>152
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 3"
FT /id="PRO_0000137442"
FT BINDING 51..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P41091"
FT UNSURE 20
FT CONFLICT 3
FT /note="G -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="Q -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_CONS 22..23
FT /evidence="ECO:0000305"
FT NON_CONS 29..30
FT /evidence="ECO:0000305"
FT NON_CONS 41..42
FT /evidence="ECO:0000305"
FT NON_CONS 81..82
FT /evidence="ECO:0000305"
FT NON_CONS 101..102
FT /evidence="ECO:0000305"
FT NON_CONS 137..138
FT /evidence="ECO:0000305"
FT NON_TER 152
SQ SEQUENCE 152 AA; 16014 MW; CA56E544FA684CA7 CRC64;
AGGEAGVTLG QPSLVEQDSH SGFKNELERD GGLLLIAGNE SKLKHILILG NKIDLVKESQ
AKEQYGQILA FVQETVAXGA TVGQVLGAVG ALPEIFTELX IVNIGSLSTG GQVSAVKADL
GKIVLTNPVX TEVGEEKSVE KHWRLIGWGQ IR
