IF5A1_ARATH
ID IF5A1_ARATH Reviewed; 158 AA.
AC Q9XI91; Q9LMG2;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Eukaryotic translation initiation factor 5A-1;
DE Short=AtELF5A-1;
DE Short=eIF-5A-1;
GN Name=ELF5A-1; OrderedLocusNames=At1g13950; ORFNames=F16A14.17, F7A19.4;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND HYPUSINE AT LYS-51.
RX PubMed=11278418; DOI=10.1074/jbc.m008544200;
RA Wang T.-W., Lu L., Wang D., Thompson J.E.;
RT "Isolation and characterization of senescence-induced cDNAs encoding
RT deoxyhypusine synthase and eucaryotic translation initiation factor 5A from
RT tomato.";
RL J. Biol. Chem. 276:17541-17549(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=16600425; DOI=10.1016/j.jplph.2006.02.001;
RA Duguay J., Jamal S., Liu Z., Wang T.W., Thompson J.E.;
RT "Leaf-specific suppression of deoxyhypusine synthase in Arabidopsis
RT thaliana enhances growth without negative pleiotropic effects.";
RL J. Plant Physiol. 164:408-420(2007).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18304977; DOI=10.1093/jxb/ern017;
RA Liu Z., Duguay J., Ma F., Wang T.W., Tshin R., Hopkins M.T., McNamara L.,
RA Thompson J.E.;
RT "Modulation of eIF5A1 expression alters xylem abundance in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 59:939-950(2008).
RN [7]
RP DEVELOPMENTAL STAGE.
RX PubMed=20492553; DOI=10.1111/j.1365-3040.2010.02173.x;
RA Ma F., Liu Z., Wang T.W., Hopkins M.T., Peterson C.A., Thompson J.E.;
RT "Arabidopsis eIF5A3 influences growth and the response to osmotic and
RT nutrient stress.";
RL Plant Cell Environ. 33:1682-1696(2010).
RN [8]
RP INDUCTION BY IRON DEFICIENCY.
RX PubMed=21173025; DOI=10.1104/pp.110.169508;
RA Lan P., Li W., Wen T.N., Shiau J.Y., Wu Y.C., Lin W., Schmidt W.;
RT "iTRAQ protein profile analysis of Arabidopsis roots reveals new aspects
RT critical for iron homeostasis.";
RL Plant Physiol. 155:821-834(2011).
RN [9]
RP INDUCTION BY IRON DEFICIENCY.
RX PubMed=21383540; DOI=10.4161/psb.6.4.14747;
RA Lan P., Schmidt W.;
RT "The enigma of eIF5A in the iron deficiency response of Arabidopsis.";
RL Plant Signal. Behav. 6:528-530(2011).
RN [10]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24163315; DOI=10.1105/tpc.113.116236;
RA Ren B., Chen Q., Hong S., Zhao W., Feng J., Feng H., Zuo J.;
RT "The Arabidopsis eukaryotic translation initiation factor eIF5A-2 regulates
RT root protoxylem development by modulating cytokinin signaling.";
RL Plant Cell 25:3841-3857(2013).
CC -!- FUNCTION: The precise role of eIF-5A in protein biosynthesis is not
CC known but it may function as a bimodular protein capable of binding to
CC both RNA and proteins. Involved in xylogenesis.
CC {ECO:0000269|PubMed:18304977}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf vasculature and inflorescence
CC stems. Present in xylem tissue but not in phloem, and in developing
CC vessel members, but not in mature vessels members. Detected in anthers.
CC {ECO:0000269|PubMed:16600425, ECO:0000269|PubMed:18304977,
CC ECO:0000269|PubMed:24163315}.
CC -!- DEVELOPMENTAL STAGE: Increases at the onset of leaf senescence.
CC {ECO:0000269|PubMed:20492553}.
CC -!- INDUCTION: Up-regulated at post-transcriptional level by iron
CC deficiency. {ECO:0000269|PubMed:21173025, ECO:0000269|PubMed:21383540}.
CC -!- PTM: Lys-51 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:11278418}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but presence of extra root
CC protoxylem cell files. {ECO:0000269|PubMed:24163315}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79401.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF296082; AAG53646.1; -; mRNA.
DR EMBL; AC007576; AAD39281.1; -; Genomic_DNA.
DR EMBL; AC068197; AAF79401.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29088.1; -; Genomic_DNA.
DR EMBL; AY063780; AAL36087.1; -; mRNA.
DR EMBL; AY117272; AAM51347.1; -; mRNA.
DR PIR; F86272; F86272.
DR RefSeq; NP_172848.1; NM_101261.3.
DR AlphaFoldDB; Q9XI91; -.
DR SMR; Q9XI91; -.
DR BioGRID; 23195; 1.
DR STRING; 3702.AT1G13950.1; -.
DR PaxDb; Q9XI91; -.
DR PRIDE; Q9XI91; -.
DR ProteomicsDB; 250673; -.
DR EnsemblPlants; AT1G13950.1; AT1G13950.1; AT1G13950.
DR GeneID; 837955; -.
DR Gramene; AT1G13950.1; AT1G13950.1; AT1G13950.
DR KEGG; ath:AT1G13950; -.
DR Araport; AT1G13950; -.
DR TAIR; locus:2014784; AT1G13950.
DR eggNOG; KOG3271; Eukaryota.
DR HOGENOM; CLU_102600_1_0_1; -.
DR InParanoid; Q9XI91; -.
DR OMA; VTYPQQC; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q9XI91; -.
DR PRO; PR:Q9XI91; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI91; baseline and differential.
DR Genevisible; Q9XI91; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; 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:0010089; P:xylem development; IMP:TAIR.
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 Hypusine; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..158
FT /note="Eukaryotic translation initiation factor 5A-1"
FT /id="PRO_0000142463"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93VP3"
FT MOD_RES 51
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:11278418"
SQ SEQUENCE 158 AA; 17360 MW; DD837BD71E2DEC7D CRC64;
MSDEEHHFES SDAGASKTYP QQAGTIRKNG YIVIKNRPCK VVEVSTSKTG KHGHAKCHFV
AIDIFTSKKL EDIVPSSHNC DVPHVNRTDY QLIDISEDGY VSLLTDNGST KDDLKLPNDD
TLLQQIKSGF DDGKDLVVSV MSAMGEEQIN ALKDIGPK
