IF5A_SPOEX
ID IF5A_SPOEX Reviewed; 160 AA.
AC P62924; Q9TVJ8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Eukaryotic translation initiation factor 5A;
DE Short=eIF-5A;
GN Name=eIF-5A; Synonyms=eIF5A;
OS Spodoptera exigua (Beet armyworm) (Noctua fulgens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7107;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Midgut, and Ovary;
RX PubMed=10620048; DOI=10.1046/j.1365-2583.1999.00148.x;
RA van Oers M.M., van Marwijk M., Kwa M.S.G., Vlak J.M., Thomas A.A.M.;
RT "Cloning and analysis of cDNAs encoding the hypusine-containing protein
RT eIF5A of two lepidopteran insect species.";
RL Insect Mol. Biol. 8:531-538(1999).
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). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Lys-52 undergoes hypusination, a unique post-translational
CC modification that consists in the addition of a butylamino group from
CC spermidine to lysine side chain, leading to the formation of the
CC unusual amino acid hypusine. eIF-5As are the only known proteins to
CC undergo this modification, which is essential for their function.
CC {ECO:0000250|UniProtKB:P63241}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; AF109730; AAF13315.1; -; mRNA.
DR AlphaFoldDB; P62924; -.
DR SMR; P62924; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro.
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; RNA-binding.
FT CHAIN 1..160
FT /note="Eukaryotic translation initiation factor 5A"
FT /id="PRO_0000142461"
FT MOD_RES 52
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
SQ SEQUENCE 160 AA; 17525 MW; D3CE1E65CEA21732 CRC64;
MADIEDTHFE TGDSGASATF PMQCSALRKN GFVMLKGRPC KIVEMSTSKT GKHGHAKVHL
VGIDIFNGKK YEDICPSTHN MDVPHVKRED YQLTDISDDG YLTLMADNGD LREDLKIPDG
DLGTQLRSDF DSGKELLCTV LKSCGEECVI AVKANTALDK
