IF5A2_CAEEL
ID IF5A2_CAEEL Reviewed; 161 AA.
AC Q20751;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Eukaryotic translation initiation factor 5A-2;
DE Short=eIF-5A-2;
DE AltName: Full=Initiation factor five protein 2;
GN Name=iff-2; ORFNames=F54C9.1;
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 FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15003625; DOI=10.1016/j.mod.2004.02.001;
RA Hanazawa M., Kawasaki I., Kunitomo H., Gengyo-Ando K., Bennett K.L.,
RA Mitani S., Iino Y.;
RT "The Caenorhabditis elegans eukaryotic initiation factor 5A homologue, IFF-
RT 1, is required for germ cell proliferation, gametogenesis and localization
RT of the P-granule component PGL-1.";
RL Mech. Dev. 121:213-224(2004).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC an important function at the level of mRNA turnover, probably acting
CC downstream of decapping. Critical for the efficient synthesis of
CC peptide bonds between consecutive proline residues. Can resolve
CC ribosomal stalling caused by consecutive prolines during translation
CC (By similarity). Involved in actin dynamics and cell cycle progression,
CC mRNA decay and probably in a pathway involved in stress response and
CC maintenance of cell wall integrity. Functions as a regulator of
CC apoptosis (By similarity). Acts in somatic tissues and its function in
CC the soma is essential for normal growth and reproduction. {ECO:0000250,
CC ECO:0000250|UniProtKB:P63241, ECO:0000269|PubMed:15003625}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the somatic tissues.
CC {ECO:0000269|PubMed:15003625}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:15003625}.
CC -!- PTM: Lys-54 undergoes hypusination, a unique post-translational
CC modification that consists in the addition of a butylamino group from
CC spermidine to lysine side chain and leads to the formation of a
CC hypusine residue. eIF-5As are the only known proteins to undergo this
CC modification, which is essential for their function.
CC {ECO:0000250|UniProtKB:Q9GZV4}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; Z49967; CAA90247.1; -; Genomic_DNA.
DR PIR; T22628; T22628.
DR RefSeq; NP_495807.1; NM_063406.6.
DR AlphaFoldDB; Q20751; -.
DR SMR; Q20751; -.
DR BioGRID; 39695; 52.
DR STRING; 6239.F54C9.1.1; -.
DR EPD; Q20751; -.
DR PaxDb; Q20751; -.
DR PeptideAtlas; Q20751; -.
DR EnsemblMetazoa; F54C9.1.1; F54C9.1.1; WBGene00002065.
DR EnsemblMetazoa; F54C9.1.2; F54C9.1.2; WBGene00002065.
DR UCSC; F54C9.1.1; c. elegans.
DR WormBase; F54C9.1; CE02249; WBGene00002065; iff-2.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; Q20751; -.
DR OMA; VTYPQQC; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q20751; -.
DR Reactome; R-CEL-204626; Hypusine synthesis from eIF5A-lysine.
DR PRO; PR:Q20751; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00002065; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0007276; P:gamete generation; IMP:WormBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR InterPro; IPR020189; Transl_elong_IF5A_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR PIRSF; PIRSF003025; eIF5A; 1.
DR SMART; SM01376; eIF-5a; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00037; eIF_5A; 1.
DR PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Elongation factor; Hypusine; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..161
FT /note="Eukaryotic translation initiation factor 5A-2"
FT /id="PRO_0000142457"
FT MOD_RES 54
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZV4"
SQ SEQUENCE 161 AA; 17953 MW; E497AFDE6580E53B CRC64;
MSDDHHDDEH FHTGDSGAAA TFPKQCSALR KNEHVMIKGR PCKIVEMSTS KTGKHGHAKV
HMVAIDIFTS KKLEDICPST HNMDVPVVKR REYLLMAIDD GYCSLMDPES CEQKDDLKLP
DTELGQQIRD AYEKDEGSVL VQVVSAIGEE AILGWKVSTK E
