IF5A1_RAT
ID IF5A1_RAT Reviewed; 154 AA.
AC Q3T1J1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 56-67 AND 87-109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [3]
RP FUNCTION.
RX PubMed=18606156; DOI=10.1016/j.brainres.2008.06.057;
RA Luchessi A.D., Cambiaghi T.D., Alves A.S., Parreiras-E-Silva L.T.,
RA Britto L.R.G., Costa-Neto C.M., Curi R.;
RT "Insights on eukaryotic translation initiation factor 5A (eIF5A) in the
RT brain and aging.";
RL Brain Res. 1228:6-13(2008).
RN [4]
RP FUNCTION.
RX PubMed=19006180; DOI=10.1002/jcp.21619;
RA Luchessi A.D., Cambiaghi T.D., Hirabara S.M., Lambertucci R.H.,
RA Silveira L.R., Baptista I.L., Moriscot A.S., Costa-Neto C.M., Curi R.;
RT "Involvement of eukaryotic translation initiation factor 5A (eIF5A) in
RT skeletal muscle stem cell differentiation.";
RL J. Cell. Physiol. 218:480-489(2009).
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 (PubMed:18606156, PubMed:19006180).
CC {ECO:0000250|UniProtKB:P63241, ECO:0000269|PubMed:18606156,
CC ECO:0000269|PubMed:19006180}.
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:0000250|UniProtKB:P63241}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; BC101891; AAI01892.1; -; mRNA.
DR RefSeq; NP_001028853.1; NM_001033681.1.
DR RefSeq; XP_006246699.1; XM_006246637.3.
DR RefSeq; XP_006246700.1; XM_006246638.1.
DR AlphaFoldDB; Q3T1J1; -.
DR BMRB; Q3T1J1; -.
DR SMR; Q3T1J1; -.
DR BioGRID; 252165; 3.
DR IntAct; Q3T1J1; 3.
DR STRING; 10116.ENSRNOP00000022343; -.
DR iPTMnet; Q3T1J1; -.
DR PhosphoSitePlus; Q3T1J1; -.
DR SwissPalm; Q3T1J1; -.
DR jPOST; Q3T1J1; -.
DR PaxDb; Q3T1J1; -.
DR PRIDE; Q3T1J1; -.
DR Ensembl; ENSRNOT00000114161; ENSRNOP00000089068; ENSRNOG00000016478.
DR GeneID; 287444; -.
DR KEGG; rno:287444; -.
DR UCSC; RGD:1308029; rat.
DR CTD; 1984; -.
DR RGD; 1308029; Eif5a.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; Q3T1J1; -.
DR OMA; VFRNEYQ; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q3T1J1; -.
DR TreeFam; TF101534; -.
DR Reactome; R-RNO-204626; Hypusine synthesis from eIF5A-lysine.
DR PRO; PR:Q3T1J1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000016478; Expressed in thymus and 19 other tissues.
DR Genevisible; Q3T1J1; RN.
DR GO; GO:0005642; C:annulate lamellae; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005643; C:nuclear pore; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:RGD.
DR GO; GO:0098586; P:cellular response to virus; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IMP:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
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:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
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:0000250|UniProtKB:P63241"
FT CHAIN 2..154
FT /note="Eukaryotic translation initiation factor 5A-1"
FT /id="PRO_0000229763"
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:0000250|UniProtKB:P63241"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63242"
SQ SEQUENCE 154 AA; 16832 MW; 07EF043C7DEA3091 CRC64;
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG
KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK
