IF5A1_CAEEL
ID IF5A1_CAEEL Reviewed; 161 AA.
AC P34563;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Eukaryotic translation initiation factor 5A-1;
DE Short=eIF-5A-1;
DE AltName: Full=Initiation factor five protein 1;
GN Name=iff-1; ORFNames=T05G5.10;
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=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
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 [3]
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). Required for mitotic germ cell
CC proliferation, gametogenesis after entry into meiosis, and localization
CC of the P granule component pgl-1 on P granules. {ECO:0000250,
CC ECO:0000250|UniProtKB:P63241, ECO:0000269|PubMed:15003625}.
CC -!- INTERACTION:
CC P34563; Q9XXJ0: dhps-1; NbExp=3; IntAct=EBI-327278, EBI-322139;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in the germline in the
CC distal region of gonads where germ cells actively proliferate.
CC {ECO:0000269|PubMed:15003625}.
CC -!- DEVELOPMENTAL STAGE: Present at late larval stages and adults.
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, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA81597.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z27079; CAA81597.2; ALT_INIT; Genomic_DNA.
DR PIR; S41010; S41010.
DR RefSeq; NP_001255020.1; NM_001268091.1.
DR RefSeq; NP_001255021.1; NM_001268092.1.
DR AlphaFoldDB; P34563; -.
DR SMR; P34563; -.
DR BioGRID; 41568; 14.
DR DIP; DIP-25111N; -.
DR IntAct; P34563; 7.
DR STRING; 6239.T05G5.10a; -.
DR EPD; P34563; -.
DR PaxDb; P34563; -.
DR EnsemblMetazoa; T05G5.10a.1; T05G5.10a.1; WBGene00002064.
DR GeneID; 176373; -.
DR KEGG; cel:CELE_T05G5.10; -.
DR UCSC; T05G5.10; c. elegans.
DR CTD; 176373; -.
DR WormBase; T05G5.10a; CE37787; WBGene00002064; iff-1.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; P34563; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; P34563; -.
DR Reactome; R-CEL-204626; Hypusine synthesis from eIF5A-lysine.
DR PRO; PR:P34563; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002064; Expressed in germ line (C elegans) and 5 other tissues.
DR ExpressionAtlas; P34563; baseline and differential.
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:0045901; P:positive regulation of translational elongation; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
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 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; Hypusine; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..161
FT /note="Eukaryotic translation initiation factor 5A-1"
FT /id="PRO_0000142456"
FT MOD_RES 54
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
SQ SEQUENCE 161 AA; 17867 MW; 7BD03FAE52D6387C CRC64;
MSEDHHDEEQ FDSAESGAAA TFPKQCSALR KNEHVMIRGR PCKIVEMSTS KTGKHGHAKV
HMVAIDIFTT KKLEDICPST HNMDVPVVKR REYILMSIED GFCSLMDPES CELKDDLKMP
EGDLGNTIRE ALEKDEGSVL VQVVAACGEE AILGYKISTK E
