IF5A3_ARATH
ID IF5A3_ARATH Reviewed; 158 AA.
AC Q9C505; Q94JU4;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Eukaryotic translation initiation factor 5A-3;
DE Short=AtELF5A-3;
DE Short=eIF-5A-3;
GN Name=ELF5A-3; OrderedLocusNames=At1g69410; ORFNames=F10D13.8, F23O10.2;
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 [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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
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 [6]
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 [7]
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 [8]
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 supporting growth and plays a
CC regulatory role in the response to sub-lethal osmotic and nutrient
CC stress. {ECO:0000269|PubMed:20492553}.
CC -!- TISSUE SPECIFICITY: Expressed in the vascular tissues of roots, stems
CC and leaves. Localized in phloem companion cells rather than sieve-tube
CC members. Not expressed in xylem or procambium. Detected in root tips
CC and in the chalazal tissue of fertilized ovules.
CC {ECO:0000269|PubMed:20492553, ECO:0000269|PubMed:24163315}.
CC -!- INDUCTION: Up-regulated at post-transcriptional level by iron
CC deficiency. {ECO:0000269|PubMed:21173025, ECO:0000269|PubMed:21383540}.
CC -!- PTM: Lys-52 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:Q9XI91}.
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}.
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DR EMBL; AC018364; AAG52496.1; -; Genomic_DNA.
DR EMBL; AC073178; AAG60110.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34921.1; -; Genomic_DNA.
DR EMBL; AF372933; AAK50073.1; -; mRNA.
DR EMBL; AY060530; AAL31161.1; -; mRNA.
DR EMBL; AY087040; AAM64601.1; -; mRNA.
DR RefSeq; NP_177100.1; NM_105608.4.
DR AlphaFoldDB; Q9C505; -.
DR SMR; Q9C505; -.
DR BioGRID; 28494; 1.
DR STRING; 3702.AT1G69410.1; -.
DR iPTMnet; Q9C505; -.
DR PaxDb; Q9C505; -.
DR PRIDE; Q9C505; -.
DR ProteomicsDB; 250681; -.
DR EnsemblPlants; AT1G69410.1; AT1G69410.1; AT1G69410.
DR GeneID; 843273; -.
DR Gramene; AT1G69410.1; AT1G69410.1; AT1G69410.
DR KEGG; ath:AT1G69410; -.
DR Araport; AT1G69410; -.
DR TAIR; locus:2007176; AT1G69410.
DR eggNOG; KOG3271; Eukaryota.
DR HOGENOM; CLU_102600_1_0_1; -.
DR InParanoid; Q9C505; -.
DR OMA; KREDYQV; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q9C505; -.
DR PRO; PR:Q9C505; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C505; baseline and differential.
DR Genevisible; Q9C505; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; 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 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 2: Evidence at transcript level;
KW Hypusine; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..158
FT /note="Eukaryotic translation initiation factor 5A-3"
FT /id="PRO_0000142465"
FT REGION 1..23
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:0000250|UniProtKB:Q9XI91"
FT CONFLICT 144
FT /note="M -> I (in Ref. 3; AAK50073/AAL31161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 17207 MW; DBA58FCF3F4DEE1B CRC64;
MSDDEHHFES SDAGASKTYP QQAGNIRKGG HIVIKGRPCK VVEVSTSKTG KHGHAKCHFV
AIDIFTSKKL EDIVPSSHNC DVPHVNRVDY QLIDISEDGF VSLLTDNGST KDDLKLPTDE
ALLTQLKNGF EEGKDIVVSV MSAMGEEQMC ALKEVGPK
