IF5A2_ARATH
ID IF5A2_ARATH Reviewed; 159 AA.
AC Q93VP3; F4HPA2; Q547G3; Q9LQY9;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 5A-2;
DE Short=AtELF5A-2;
DE Short=eIF-5A-2;
DE AltName: Full=Protein FUMONISIN B1-RESISTANT 12;
GN Name=ELF5A-2; Synonyms=FBR12; OrderedLocusNames=At1g26630;
GN ORFNames=T24P13.1;
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].
RA Li C., Zhan H., Qi Q., Li G., Ling Q.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17513484; DOI=10.1104/pp.107.098079;
RA Feng H., Chen Q., Feng J., Zhang J., Yang X., Zuo J.;
RT "Functional characterization of the Arabidopsis eukaryotic translation
RT initiation factor 5A-2 that plays a crucial role in plant growth and
RT development by regulating cell division, cell growth, and cell death.";
RL Plant Physiol. 144:1531-1545(2007).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=18633122; DOI=10.1104/pp.108.118869;
RA Hopkins M.T., Lampi Y., Wang T.W., Liu Z., Thompson J.E.;
RT "Eukaryotic translation initiation factor 5A is involved in pathogen-
RT induced cell death and development of disease symptoms in Arabidopsis.";
RL Plant Physiol. 148:479-489(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP MUTAGENESIS OF SER-2, AND PHOSPHORYLATION AT SER-2.
RC STRAIN=cv. Columbia;
RX PubMed=20018887; DOI=10.1074/jbc.m109.018770;
RA Lebska M., Ciesielski A., Szymona L., Godecka L., Lewandowska-Gnatowska E.,
RA Szczegielniak J., Muszynska G.;
RT "Phosphorylation of maize eukaryotic translation initiation factor 5A
RT (eIF5A) by casein kinase 2: identification of phosphorylated residue and
RT influence on intracellular localization of eIF5A.";
RL J. Biol. Chem. 285:6217-6226(2010).
RN [10]
RP FUNCTION, MUTAGENESIS OF LYS-51, SUBCELLULAR LOCATION, INTERACTION WITH
RP AHK4 AND AHP1, 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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX PubMed=19676114; DOI=10.1002/prot.22530;
RA Teng Y.B., Ma X.X., He Y.X., Jiang Y.L., Du J., Xiang C., Chen Y.,
RA Zhou C.Z.;
RT "Crystal structure of Arabidopsis translation initiation factor eIF-5A2.";
RL Proteins 77:736-740(2009).
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. Regulates cytokinin-mediated root protoxylem
CC specification and represses secifically the expression of AHP6.
CC Regulates the induction of programmed cell death caused by infection
CC with virulent pathogen. {ECO:0000269|PubMed:17513484,
CC ECO:0000269|PubMed:18633122, ECO:0000269|PubMed:24163315}.
CC -!- SUBUNIT: Homodimer. Interacts with AHK4 and AHP1. Cytokinin regulates
CC the formation of the AHP1-AHK4-ELF5A-2 complex.
CC {ECO:0000269|PubMed:19676114, ECO:0000269|PubMed:24163315}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24163315}. Nucleus
CC {ECO:0000269|PubMed:24163315}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93VP3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93VP3-2; Sequence=VSP_054952;
CC -!- TISSUE SPECIFICITY: Ubiquitous. In roots, expressed mostly inside the
CC stele of the mature zone. {ECO:0000269|PubMed:17513484}.
CC -!- INDUCTION: Constitutively expressed. Up-regulated at post-
CC transcriptional level by wounding and pathogen infection.
CC {ECO:0000269|PubMed:18633122}.
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:0000250|UniProtKB:Q9XI91}.
CC -!- DISRUPTION PHENOTYPE: Severe defects in plant growth and development.
CC Delayed dark-induced leaf senescence. Dwarfism, defective sporogenesis
CC and shorter primary roots. Impaired protoxylem development.
CC {ECO:0000269|PubMed:17513484, ECO:0000269|PubMed:24163315}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF492850; AAM11676.1; -; mRNA.
DR EMBL; AC006535; AAF87023.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30711.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30712.1; -; Genomic_DNA.
DR EMBL; AY039588; AAK62643.1; -; mRNA.
DR EMBL; AY055789; AAL06956.1; -; mRNA.
DR EMBL; AY084827; AAM61392.1; -; mRNA.
DR RefSeq; NP_001077597.1; NM_001084128.1. [Q93VP3-2]
DR RefSeq; NP_173985.1; NM_102425.4. [Q93VP3-1]
DR PDB; 3HKS; X-ray; 2.30 A; A/B=1-159.
DR PDBsum; 3HKS; -.
DR AlphaFoldDB; Q93VP3; -.
DR SMR; Q93VP3; -.
DR BioGRID; 24439; 9.
DR IntAct; Q93VP3; 1.
DR STRING; 3702.AT1G26630.1; -.
DR iPTMnet; Q93VP3; -.
DR SwissPalm; Q93VP3; -.
DR PaxDb; Q93VP3; -.
DR PRIDE; Q93VP3; -.
DR ProteomicsDB; 250680; -. [Q93VP3-1]
DR EnsemblPlants; AT1G26630.1; AT1G26630.1; AT1G26630. [Q93VP3-1]
DR EnsemblPlants; AT1G26630.2; AT1G26630.2; AT1G26630. [Q93VP3-2]
DR GeneID; 839203; -.
DR Gramene; AT1G26630.1; AT1G26630.1; AT1G26630. [Q93VP3-1]
DR Gramene; AT1G26630.2; AT1G26630.2; AT1G26630. [Q93VP3-2]
DR KEGG; ath:AT1G26630; -.
DR Araport; AT1G26630; -.
DR TAIR; locus:2200570; AT1G26630.
DR eggNOG; KOG3271; Eukaryota.
DR HOGENOM; CLU_102600_1_0_1; -.
DR InParanoid; Q93VP3; -.
DR OMA; HHFESSE; -.
DR PhylomeDB; Q93VP3; -.
DR EvolutionaryTrace; Q93VP3; -.
DR PRO; PR:Q93VP3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VP3; baseline and differential.
DR Genevisible; Q93VP3; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
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:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:0034050; P:programmed cell death induced by symbiont; IDA:TAIR.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0006413; P:translational initiation; 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 3D-structure; Alternative splicing; Cytoplasm; Hypusine; Initiation factor;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..159
FT /note="Eukaryotic translation initiation factor 5A-2"
FT /id="PRO_0000142464"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20018887,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 51
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:Q9XI91"
FT VAR_SEQ 126..159
FT /note="MRLGFDEGKDIVVSVMSSMGEEQICAVKEVGGGK -> LLCFVNADEAWIR
FT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054952"
FT MUTAGEN 2
FT /note="S->A: Loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:20018887"
FT MUTAGEN 51
FT /note="K->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24163315"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3HKS"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3HKS"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 86..95
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:3HKS"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:3HKS"
FT STRAND 146..157
FT /evidence="ECO:0007829|PDB:3HKS"
SQ SEQUENCE 159 AA; 17140 MW; 970A677B8F884463 CRC64;
MSDDEHHFEA SESGASKTYP QSAGNIRKGG HIVIKNRPCK VVEVSTSKTG KHGHAKCHFV
AIDIFTAKKL EDIVPSSHNC DVPHVNRVDY QLIDITEDGF VSLLTDSGGT KDDLKLPTDD
GLTAQMRLGF DEGKDIVVSV MSSMGEEQIC AVKEVGGGK
