ID   IF2B_CAEEL              Reviewed;         250 AA.
AC   Q21230; Q18855;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 4.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE   AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE            Short=eIF-2-beta;
GN   Name=eif-2beta {ECO:0000312|WormBase:K04G2.1};
GN   Synonyms=iftb-1 {ECO:0000312|WormBase:K04G2.1};
GN   ORFNames=K04G2.1 {ECO:0000312|WormBase:K04G2.1};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18635357; DOI=10.1016/j.cub.2008.06.065;
RA   Chen L., McCloskey T., Joshi P.M., Rothman J.H.;
RT   "ced-4 and proto-oncogene tfg-1 antagonistically regulate cell size and
RT   apoptosis in C. elegans.";
RL   Curr. Biol. 18:1025-1033(2008).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a reduced body
CC       length (PubMed:18635357). This phenotype in suppressed in a ced-4 n1162
CC       mutant background (PubMed:18635357). {ECO:0000269|PubMed:18635357}.
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR   EMBL; BX284601; CAB00049.1; -; Genomic_DNA.
DR   EMBL; Z75533; CAB00049.1; JOINED; Genomic_DNA.
DR   PIR; T20242; T20242.
DR   RefSeq; NP_492209.1; NM_059808.3.
DR   AlphaFoldDB; Q21230; -.
DR   SMR; Q21230; -.
DR   BioGRID; 38019; 15.
DR   STRING; 6239.K04G2.1.1; -.
DR   EPD; Q21230; -.
DR   PaxDb; Q21230; -.
DR   PeptideAtlas; Q21230; -.
DR   EnsemblMetazoa; K04G2.1.1; K04G2.1.1; WBGene00010560.
DR   EnsemblMetazoa; K04G2.1.2; K04G2.1.2; WBGene00010560.
DR   GeneID; 172584; -.
DR   KEGG; cel:CELE_K04G2.1; -.
DR   CTD; 172584; -.
DR   WormBase; K04G2.1; CE16227; WBGene00010560; eif-2beta.
DR   eggNOG; KOG2768; Eukaryota.
DR   GeneTree; ENSGT00940000167018; -.
DR   HOGENOM; CLU_026663_0_1_1; -.
DR   InParanoid; Q21230; -.
DR   OMA; WPDYTYE; -.
DR   OrthoDB; 1178655at2759; -.
DR   PhylomeDB; Q21230; -.
DR   Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-CEL-381042; PERK regulates gene expression.
DR   Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR   Reactome; R-CEL-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-CEL-72731; Recycling of eIF2:GDP.
DR   PRO; PR:Q21230; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00010560; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR   GO; GO:0006412; P:translation; IMP:UniProtKB.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   PANTHER; PTHR23001; PTHR23001; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SUPFAM; SSF100966; SSF100966; 1.
DR   SUPFAM; SSF75689; SSF75689; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Metal-binding; Protein biosynthesis; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..250
FT                   /note="Eukaryotic translation initiation factor 2 subunit
FT                   2"
FT                   /id="PRO_0000137410"
FT   ZN_FING         193..217
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   250 AA;  27580 MW;  3EAC2C70946986C4 CRC64;
     MADDLGLDLG KKKKSKKVIK IDGDDAPVET GVEAVEDGLG ELNLGAKKKK KTPKTAGEEV
     VEEKVPTLEI GIGAQNLIDA KGAWPDYTYE EALTLVYQVM KDKNPDFAGD KKKFAIKLPE
     VARAGSKKTA FSNFLEICRL MKRQDKHVLQ FLLAELGTTG SIDGSNCLIV KGRWQQKQFE
     SVLRKYIKEY VMCHTCKSPE TQLTKDTRLF FLQCTNCGSR CSVTAIKSGF KAVVGKRAAI
     RRAEEATAGK