IF5A2_CHICK
ID IF5A2_CHICK Reviewed; 153 AA.
AC Q07460;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Eukaryotic translation initiation factor 5A-2;
DE Short=eIF-5A-2;
DE Short=eIF-5A2;
DE AltName: Full=Eukaryotic initiation factor 5A isoform 2;
DE AltName: Full=eIF-4D;
GN Name=EIF5A2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=7916728; DOI=10.1016/0378-1119(93)90025-x;
RA Rinaudo M.S., Joe Y.A., Park M.H.;
RT "Cloning and sequencing of a chick embryo cDNA encoding the 20-kDa
RT hypusine-containing protein, eIF-5A.";
RL Gene 137:303-307(1993).
RN [2]
RP PROTEIN SEQUENCE OF 7-121, HYPUSINE AT LYS-50, AND BLOCKED N-TERMINUS.
RC STRAIN=Leghorn; TISSUE=Embryo;
RX PubMed=1556119; DOI=10.1016/s0021-9258(18)42668-3;
RA Wolff E.C., Kinzy T.G., Merrick W.C., Park M.H.;
RT "Two isoforms of eIF-5A in chick embryo. Isolation, activity, and
RT comparison of sequences of the hypusine-containing proteins.";
RL J. Biol. Chem. 267:6107-6113(1992).
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. Mediates effects of polyamines on neuronal process extension
CC and survival. May play an important role in brain development and
CC function, and in skeletal muscle stem cell differentiation (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus, nuclear
CC pore complex {ECO:0000250}. 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. {ECO:0000250}.
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 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:0000269|PubMed:1556119}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; M99499; AAA17444.1; -; mRNA.
DR PIR; I50227; A42156.
DR RefSeq; NP_990863.1; NM_205532.1.
DR RefSeq; XP_015147137.1; XM_015291651.1.
DR AlphaFoldDB; Q07460; -.
DR SMR; Q07460; -.
DR STRING; 9031.ENSGALP00000038570; -.
DR PaxDb; Q07460; -.
DR Ensembl; ENSGALT00000039360; ENSGALP00000038570; ENSGALG00000009309.
DR GeneID; 396545; -.
DR KEGG; gga:396545; -.
DR CTD; 56648; -.
DR VEuPathDB; HostDB:geneid_396545; -.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; Q07460; -.
DR OMA; TIMINIQ; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q07460; -.
DR TreeFam; TF101534; -.
DR Reactome; R-GGA-204626; Hypusine synthesis from eIF5A-lysine.
DR PRO; PR:Q07460; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000009309; Expressed in spermatocyte and 14 other tissues.
DR ExpressionAtlas; Q07460; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; 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:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein biosynthesis; Protein transport;
KW Reference proteome; RNA-binding; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..153
FT /note="Eukaryotic translation initiation factor 5A-2"
FT /id="PRO_0000142454"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZV4"
FT MOD_RES 50
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:1556119"
SQ SEQUENCE 153 AA; 16720 MW; 8FAAE80D68538E55 CRC64;
MADELDFTTG DAGASSTYPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFNGKKYE DICPSTHNMD VPNIKRNDYQ LIGIQDGYLS LLTESGEVRE DLKLPEGDLG
KEIEGKFNAN EDVQISVISA MNEECAVAIK PCK
