IF5_CAEEL
ID IF5_CAEEL Reviewed; 436 AA.
AC Q22918; Q95Q70;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN ORFNames=C37C3.2;
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], AND ALTERNATIVE SPLICING.
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=23076791; DOI=10.1152/ajpcell.00294.2012;
RA Lee E.C., Strange K.;
RT "GCN-2 dependent inhibition of protein synthesis activates osmosensitive
RT gene transcription via WNK and Ste20 kinase signaling.";
RL Am. J. Physiol. 303:C1269-1277(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q22918-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q22918-2; Sequence=VSP_001438;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in a decrease in
CC protein synthesis and an increase in the expression of gpdh-1
CC independent of hypertonic stress. {ECO:0000269|PubMed:23076791}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; FO080808; CCD66940.1; -; Genomic_DNA.
DR EMBL; FO080808; CCD66941.1; -; Genomic_DNA.
DR PIR; T34401; T34401.
DR RefSeq; NP_001334195.1; NM_001347267.1.
DR RefSeq; NP_741572.1; NM_171488.4.
DR AlphaFoldDB; Q22918; -.
DR SMR; Q22918; -.
DR BioGRID; 44208; 4.
DR STRING; 6239.C37C3.2a.1; -.
DR iPTMnet; Q22918; -.
DR EPD; Q22918; -.
DR PaxDb; Q22918; -.
DR PeptideAtlas; Q22918; -.
DR PRIDE; Q22918; -.
DR EnsemblMetazoa; C37C3.18a.1; C37C3.18a.1; WBGene00303000.
DR EnsemblMetazoa; C37C3.2.1; C37C3.2.1; WBGene00016496. [Q22918-1]
DR UCSC; C37C3.2b.3; c. elegans. [Q22918-1]
DR WormBase; C37C3.2a; CE27367; WBGene00016496; -. [Q22918-1]
DR WormBase; C37C3.2b; CE51823; WBGene00016496; -.
DR eggNOG; KOG2767; Eukaryota.
DR GeneTree; ENSGT00390000016478; -.
DR InParanoid; Q22918; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 979826at2759; -.
DR PhylomeDB; Q22918; -.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q22918; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00016496; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q22918; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
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:0006412; P:translation; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
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 InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..436
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212519"
FT DOMAIN 216..379
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 177..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 272..305
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_001438"
SQ SEQUENCE 436 AA; 48787 MW; A89468A5AA48B211 CRC64;
MALNVNRAVA DPFYRYKMPK LSAKVEGKGN GIKTVISNMS EIAKALERPP MYPTKYFGCE
LGAQTNFDAK NERYIVNGEH DANKLQDILD GFIKKFVLCK SCENPETQLF VRKNNIKSKC
KACGCSFDID LKHKLSTFIM KNPPKIDVDF SKAEQKNGKK TSGADAAAAV AADIIHNSDK
GSSNDDDDDD WEPEPVEPNG MLSAGMGKLV LDKDLEKSEE QRLDMLHTFF LKAKEEDRIS
DAKGQTALRD EAERLELKQK ASLLLANVFL DEKVITDKQI SKHRNLLLRF TLNDKKAQRY
LLGGVEQVIH KHEAELLSKS AHIIKSLYDE DVCEEDSLIS WGEKPSSKYV SKSFAKKIIE
NSQPVLNWLK EAEEETEEES DDEIAFGGDV KESEFLRQQK EKAAREAQQK SAKATNGNAA
AASGANDEED LDIDDI
