IF5A1_CHICK
ID IF5A1_CHICK Reviewed; 144 AA.
AC Q09121; Q5ZLI6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 106.
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=EIF5A1; ORFNames=RCJMB04_6a12;
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 [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP PROTEIN SEQUENCE OF 21-39 AND 44-121, HYPUSINE AT LYS-50, AND BLOCKED
RP 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}.
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:1556119}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC -!- CAUTION: The C-terminal section of the sequence may be incorrect.
CC {ECO:0000305}.
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DR EMBL; AJ719748; CAG31407.1; -; mRNA.
DR AlphaFoldDB; Q09121; -.
DR SMR; Q09121; -.
DR PRIDE; Q09121; -.
DR VEuPathDB; HostDB:LOC107050352; -.
DR InParanoid; Q09121; -.
DR PhylomeDB; Q09121; -.
DR Proteomes; UP000000539; Unplaced.
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..144
FT /note="Eukaryotic translation initiation factor 5A-1"
FT /id="PRO_0000142455"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
FT MOD_RES 50
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:1556119"
FT CONFLICT 87
FT /note="C -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 15889 MW; 3695B498CF00C2AC CRC64;
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRCDFQ LIGIQDGFLS LLQDSGEVRE DLRLPEGELG
REIEQKYDCG EEIITIHGAR FTTS
