ID G3NLT9_GASAC Unreviewed; 566 AA.
AC G3NLT9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Eukaryotic translation initiation factor 2A {ECO:0000256|ARBA:ARBA00013819, ECO:0000256|PIRNR:PIRNR017222};
DE Short=eIF-2A {ECO:0000256|PIRNR:PIRNR017222};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000006302.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000006302.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000006302.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. {ECO:0000256|ARBA:ARBA00003993,
CC ECO:0000256|PIRNR:PIRNR017222}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family.
CC {ECO:0000256|ARBA:ARBA00009573, ECO:0000256|PIRNR:PIRNR017222}.
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DR AlphaFoldDB; G3NLT9; -.
DR Ensembl; ENSGACT00000006319.1; ENSGACP00000006302.1; ENSGACG00000004748.1.
DR GeneTree; ENSGT00730000111053; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000004748; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13227; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR PANTHER; PTHR13227:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2A; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|PIRNR:PIRNR017222};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|PIRNR:PIRNR017222};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845,
KW ECO:0000256|PIRNR:PIRNR017222}; WD repeat {ECO:0000256|ARBA:ARBA00022574}.
FT DOMAIN 216..403
FT /note="Translation initiation factor beta propellor-like"
FT /evidence="ECO:0000259|Pfam:PF08662"
FT REGION 485..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 62685 MW; B7BB7139C89E634C CRC64;
MAPTIPLLAV RGSDGTSLLS GPPSCEQHSS FQRDARPSRC VSFSRDGTLF GWCNGLNVSV
VKSSDGSLVS TFDLPKATLL DFSPLNNILV TWQPYSKAKD GAQGEANLQL WDLQSGQLIK
ALYQKKLDSW WCPSWSEDEK ISVRSVNNEL HFYENNDFNL IANKLHMQKV SDFVVSPGGQ
PSKVAVYVPG SKGAPSFVRL YQYPVLGGPT AALANKSFFK ADRVSMQWNK KGSAVLVTSS
TEVDKSGASY YGEQTLHFLS VSGETSLVQL QKSGPIYDVV WSPGSAEFCV VYGFMPAKTT
VYSLKCEPLF DFGTGPRNAA YYSPQGHILV LAGFGNLRGQ MEVWDAKKYK QVSKPEAPDA
THFSWCPDGE HVVTATCSPR LRVNNGFKIW HYTGSVLHKQ EAEPGCQLWE VRWQPAPEGS
FPGRPVRYQA APSQLGTTQA TPTQAYRPPA LRHLPATPSS KLVSRRPWTG FPSITLLTYQ
WESSKELKPK TEPPSDPAHI ITSQLEPSCG DPETDKKIKN VKKKLKAIEE LKDQRASGKV
LQNNQLEKLQ KEDQLLKELE ELQIEP
//