IF5A1_MOUSE
ID IF5A1_MOUSE Reviewed; 154 AA.
AC P63242; P10159; Q16182; Q5NCX0; Q78NR3; Q9D0G2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Jenkins Z.A., Johansson H.E.;
RT "Mouse eIF5A, genes and mRNAs.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP PROTEIN SEQUENCE OF 56-67 AND 87-109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP FUNCTION, AND HYPUSINE.
RX PubMed=15377278; DOI=10.1042/bj20041477;
RA Nishimura K., Murozumi K., Shirahata A., Park M.H., Kashiwagi K.,
RA Igarashi K.;
RT "Independent roles of eIF5A and polyamines in cell proliferation.";
RL Biochem. J. 385:779-785(2005).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=17707773; DOI=10.1016/j.bbrc.2007.07.185;
RA Parreiras-E-Silva L.T., Gomes M.D., Oliveira E.B., Costa-Neto C.M.;
RT "The N-terminal region of eukaryotic translation initiation factor 5A
RT signals to nuclear localization of the protein.";
RL Biochem. Biophys. Res. Commun. 362:393-398(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation (By
CC similarity). Has an important function at the level of mRNA turnover,
CC probably acting downstream of decapping (By similarity). Critical for
CC the efficient synthesis of peptide bonds between consecutive proline
CC residues (By similarity). Can resolve ribosomal stalling caused by
CC consecutive prolines during translation (By similarity). Involved in
CC actin dynamics and cell cycle progression, mRNA decay and probably in a
CC pathway involved in stress response and maintenance of cell wall
CC integrity (By similarity). With syntenin SDCBP, functions as a
CC regulator of p53/TP53 and p53/TP53-dependent apoptosis (By similarity).
CC Regulates also TNF-alpha-mediated apoptosis (By similarity). Mediates
CC effects of polyamines on neuronal process extension and survival
CC (PubMed:15377278). May play an important role in brain development and
CC function, and in skeletal muscle stem cell differentiation (By
CC similarity). {ECO:0000250|UniProtKB:P63241,
CC ECO:0000250|UniProtKB:Q3T1J1, ECO:0000269|PubMed:15377278}.
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:0000269|PubMed:17707773}. Nucleus
CC {ECO:0000269|PubMed:17707773}. 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:15377278}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI35154.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY129323; AAN17521.1; -; mRNA.
DR EMBL; AY129324; AAN17527.1; -; mRNA.
DR EMBL; AY129325; AAN17528.1; -; mRNA.
DR EMBL; AY129326; AAN17532.1; -; mRNA.
DR EMBL; AY129327; AAN17534.1; -; mRNA.
DR EMBL; AY129328; AAN17535.1; -; mRNA.
DR EMBL; AY129329; AAN17539.1; -; mRNA.
DR EMBL; AK011306; BAB27532.1; -; mRNA.
DR EMBL; AK011470; BAB27641.1; -; mRNA.
DR EMBL; AK149705; BAE29039.1; -; mRNA.
DR EMBL; AL596185; CAI35153.1; -; Genomic_DNA.
DR EMBL; AL596185; CAI35154.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC003889; AAH03889.1; -; mRNA.
DR EMBL; BC008093; AAH08093.1; -; mRNA.
DR EMBL; BC024899; AAH24899.1; -; mRNA.
DR CCDS; CCDS24923.1; -.
DR RefSeq; NP_001160061.1; NM_001166589.1.
DR RefSeq; NP_001160062.1; NM_001166590.1.
DR RefSeq; NP_001160063.1; NM_001166591.1.
DR RefSeq; NP_001160064.1; NM_001166592.1.
DR RefSeq; NP_001160065.1; NM_001166593.1.
DR RefSeq; NP_001160066.1; NM_001166594.1.
DR RefSeq; NP_001160067.1; NM_001166595.1.
DR RefSeq; NP_001160068.1; NM_001166596.1.
DR RefSeq; NP_853613.1; NM_181582.4.
DR RefSeq; XP_011247360.1; XM_011249058.2.
DR AlphaFoldDB; P63242; -.
DR BMRB; P63242; -.
DR SMR; P63242; -.
DR BioGRID; 234898; 68.
DR IntAct; P63242; 4.
DR MINT; P63242; -.
DR STRING; 10090.ENSMUSP00000047008; -.
DR iPTMnet; P63242; -.
DR PhosphoSitePlus; P63242; -.
DR SwissPalm; P63242; -.
DR REPRODUCTION-2DPAGE; P63242; -.
DR UCD-2DPAGE; P63242; -.
DR EPD; P63242; -.
DR jPOST; P63242; -.
DR MaxQB; P63242; -.
DR PaxDb; P63242; -.
DR PeptideAtlas; P63242; -.
DR PRIDE; P63242; -.
DR ProteomicsDB; 267265; -.
DR TopDownProteomics; P63242; -.
DR DNASU; 276770; -.
DR Ensembl; ENSMUST00000043419; ENSMUSP00000047008; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000070996; ENSMUSP00000067077; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000071026; ENSMUSP00000068651; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108607; ENSMUSP00000104247; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108608; ENSMUSP00000104248; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108609; ENSMUSP00000104249; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108610; ENSMUSP00000104250; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108611; ENSMUSP00000104251; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108612; ENSMUSP00000104252; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000108613; ENSMUSP00000104253; ENSMUSG00000078812.
DR Ensembl; ENSMUST00000164359; ENSMUSP00000132717; ENSMUSG00000078812.
DR GeneID; 276770; -.
DR KEGG; mmu:276770; -.
DR UCSC; uc007jsq.2; mouse.
DR CTD; 1984; -.
DR MGI; MGI:106248; Eif5a.
DR VEuPathDB; HostDB:ENSMUSG00000078812; -.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR InParanoid; P63242; -.
DR OMA; VFRNEYQ; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; P63242; -.
DR TreeFam; TF101534; -.
DR Reactome; R-MMU-204626; Hypusine synthesis from eIF5A-lysine.
DR BioGRID-ORCS; 276770; 26 hits in 73 CRISPR screens.
DR ChiTaRS; Eif5a; mouse.
DR PRO; PR:P63242; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63242; protein.
DR Bgee; ENSMUSG00000078812; Expressed in presomitic mesoderm and 240 other tissues.
DR ExpressionAtlas; P63242; baseline and differential.
DR Genevisible; P63242; MM.
DR GO; GO:0005642; C:annulate lamellae; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
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 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_0000142452"
FT REGION 2..19
FT /note="Nuclear localization regulation"
FT /evidence="ECO:0000269|PubMed:17707773"
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:0007744|PubMed:23806337"
FT CONFLICT 8
FT /note="E -> Y (in Ref. 2; BAB27641)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="A -> S (in Ref. 2; BAB27641)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="S -> F (in Ref. 2; BAB27641)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> K (in Ref. 2; BAB27641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 16832 MW; 07EF043C7DEA3091 CRC64;
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG
KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK
