IF5A1_RABIT
ID IF5A1_RABIT Reviewed; 154 AA.
AC P10160;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Eukaryotic translation initiation factor 5A-1;
DE Short=eIF-5A-1;
DE Short=eIF-5A1;
DE AltName: Full=Eukaryotic initiation factor 5A isoform 1;
DE Short=eIF-5A;
DE AltName: Full=eIF-4D;
GN Name=EIF5A;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 2-154, HYPUSINE AT LYS-50, AND BLOCKED N-TERMINUS.
RX PubMed=2492279; DOI=10.1016/s0021-9258(18)94226-2;
RA Smit-Mcbride Z., Dever T.E., Hershey J.W.B., Merrick W.C.;
RT "Sequence determination and cDNA cloning of eukaryotic initiation factor
RT 4D, the hypusine-containing protein.";
RL J. Biol. Chem. 264:1578-1583(1989).
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 Involved in actin dynamics and cell cycle progression, mRNA decay and
CC probably in a pathway involved in stress response and maintenance of
CC cell wall integrity. With syntenin SDCBP, functions as a regulator of
CC p53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-
CC mediated apoptosis. Mediates effects of polyamines on neuronal process
CC extension and survival (By similarity). May play an important role in
CC brain development and function, and in skeletal muscle stem cell
CC differentiation (By similarity). {ECO:0000250|UniProtKB:P63241,
CC ECO:0000250|UniProtKB:Q3T1J1}.
CC -!- SUBUNIT: Interacts with DHPS, with SDCBP and DOHH. Found in a complex
CC with Ran and XPO4; the hypusine modification increases the interaction
CC with XPO4. {ECO:0000250|UniProtKB:P63241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63241}. Nucleus
CC {ECO:0000250|UniProtKB:P63241}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P63241}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P63241}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P63241}. Note=Hypusine modification promotes the
CC nuclear export and cytoplasmic localization and there was a dynamic
CC shift in the localization from predominantly cytoplasmic to primarily
CC nuclear under apoptotic inducing conditions. Nuclear export of
CC hypusinated protein is mediated by XPO4.
CC {ECO:0000250|UniProtKB:P63241}.
CC -!- PTM: Acetylated by PCAF/KAT2B, regulating its subcellular localization
CC (By similarity). Deacetylated by SIRT2 (By similarity).
CC {ECO:0000250|UniProtKB:P63241}.
CC -!- PTM: Lys-50 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:0000269|PubMed:2492279}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:2492279}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR PIR; A31486; A31486.
DR AlphaFoldDB; P10160; -.
DR BMRB; P10160; -.
DR SMR; P10160; -.
DR STRING; 9986.ENSOCUP00000013104; -.
DR PRIDE; P10160; -.
DR eggNOG; KOG3271; Eukaryota.
DR InParanoid; P10160; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0045727; P:positive regulation of translation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Elongation factor;
KW Endoplasmic reticulum; Hypusine; Membrane; Nucleus; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2492279"
FT CHAIN 2..154
FT /note="Eukaryotic translation initiation factor 5A-1"
FT /id="PRO_0000142453"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
FT MOD_RES 50
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:2492279"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63242"
FT UNSURE 2..8
SQ SEQUENCE 154 AA; 16816 MW; 07FE052C7DEA3091 CRC64;
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG
KEIEQKYDSG EEILITVLSA MTEEAAVAIK AMAK
