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Protein

Eukaryotic translation initiation factor 5A-1

Gene

ELF5A-1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The precise role of eIF-5A in protein biosynthesis is not known but it may function as a bimodular protein capable of binding to both RNA and proteins. Involved in xylogenesis.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

ReactomeiREACT_344318. Hypusine synthesis from eIF5A-lysine.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 5A-1
Short name:
AtELF5A-1
Short name:
eIF-5A-1
Gene namesi
Name:ELF5A-1
Ordered Locus Names:At1g13950
ORF Names:F16A14.17, F7A19.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G13950.

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, but presence of extra root protoxylem cell files.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158Eukaryotic translation initiation factor 5A-1PRO_0000142463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei51 – 511Hypusine1 Publication

Post-translational modificationi

eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).

Keywords - PTMi

Hypusine, Phosphoprotein

Proteomic databases

PaxDbiQ9XI91.
PRIDEiQ9XI91.

Expressioni

Tissue specificityi

Expressed in leaf vasculature and inflorescence stems. Present in xylem tissue but not in phloem, and in developing vessel members, but not in mature vessels members. Detected in anthers.3 Publications

Developmental stagei

Increases at the onset of leaf senescence.1 Publication

Inductioni

Up-regulated at post-transcriptional level by iron deficiency.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi23195. 1 interaction.
STRINGi3702.AT1G13950.1.

Structurei

3D structure databases

ProteinModelPortaliQ9XI91.
SMRiQ9XI91. Positions 16-156.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-5A family.Curated

Phylogenomic databases

eggNOGiCOG0231.
HOGENOMiHOG000106270.
InParanoidiQ9XI91.
KOiK03263.
OMAiGHAKANI.
PhylomeDBiQ9XI91.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR019769. Trans_elong_IF5A_hypusine_site.
IPR001884. Transl_elong_IF5A.
IPR020189. Transl_elong_IF5A_C.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR11673. PTHR11673. 1 hit.
PfamiPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFiPIRSF003025. eIF5A. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00037. eIF_5A. 1 hit.
PROSITEiPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9XI91-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDEEHHFES SDAGASKTYP QQAGTIRKNG YIVIKNRPCK VVEVSTSKTG
60 70 80 90 100
KHGHAKCHFV AIDIFTSKKL EDIVPSSHNC DVPHVNRTDY QLIDISEDGY
110 120 130 140 150
VSLLTDNGST KDDLKLPNDD TLLQQIKSGF DDGKDLVVSV MSAMGEEQIN

ALKDIGPK
Length:158
Mass (Da):17,360
Last modified:November 1, 1999 - v1
Checksum:iDD837BD71E2DEC7D
GO

Sequence cautioni

The sequence AAF79401.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296082 mRNA. Translation: AAG53646.1.
AC007576 Genomic DNA. Translation: AAD39281.1.
AC068197 Genomic DNA. Translation: AAF79401.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29088.1.
AY063780 mRNA. Translation: AAL36087.1.
AY117272 mRNA. Translation: AAM51347.1.
PIRiF86272.
RefSeqiNP_172848.1. NM_101261.2.
UniGeneiAt.24908.

Genome annotation databases

EnsemblPlantsiAT1G13950.1; AT1G13950.1; AT1G13950.
GeneIDi837955.
KEGGiath:AT1G13950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF296082 mRNA. Translation: AAG53646.1.
AC007576 Genomic DNA. Translation: AAD39281.1.
AC068197 Genomic DNA. Translation: AAF79401.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29088.1.
AY063780 mRNA. Translation: AAL36087.1.
AY117272 mRNA. Translation: AAM51347.1.
PIRiF86272.
RefSeqiNP_172848.1. NM_101261.2.
UniGeneiAt.24908.

3D structure databases

ProteinModelPortaliQ9XI91.
SMRiQ9XI91. Positions 16-156.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi23195. 1 interaction.
STRINGi3702.AT1G13950.1.

Proteomic databases

PaxDbiQ9XI91.
PRIDEiQ9XI91.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G13950.1; AT1G13950.1; AT1G13950.
GeneIDi837955.
KEGGiath:AT1G13950.

Organism-specific databases

TAIRiAT1G13950.

Phylogenomic databases

eggNOGiCOG0231.
HOGENOMiHOG000106270.
InParanoidiQ9XI91.
KOiK03263.
OMAiGHAKANI.
PhylomeDBiQ9XI91.

Enzyme and pathway databases

ReactomeiREACT_344318. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

PROiQ9XI91.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR019769. Trans_elong_IF5A_hypusine_site.
IPR001884. Transl_elong_IF5A.
IPR020189. Transl_elong_IF5A_C.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR11673. PTHR11673. 1 hit.
PfamiPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFiPIRSF003025. eIF5A. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00037. eIF_5A. 1 hit.
PROSITEiPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of senescence-induced cDNAs encoding deoxyhypusine synthase and eucaryotic translation initiation factor 5A from tomato."
    Wang T.-W., Lu L., Wang D., Thompson J.E.
    J. Biol. Chem. 276:17541-17549(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], HYPUSINE AT LYS-51.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Leaf-specific suppression of deoxyhypusine synthase in Arabidopsis thaliana enhances growth without negative pleiotropic effects."
    Duguay J., Jamal S., Liu Z., Wang T.W., Thompson J.E.
    J. Plant Physiol. 164:408-420(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Modulation of eIF5A1 expression alters xylem abundance in Arabidopsis thaliana."
    Liu Z., Duguay J., Ma F., Wang T.W., Tshin R., Hopkins M.T., McNamara L., Thompson J.E.
    J. Exp. Bot. 59:939-950(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  7. "Arabidopsis eIF5A3 influences growth and the response to osmotic and nutrient stress."
    Ma F., Liu Z., Wang T.W., Hopkins M.T., Peterson C.A., Thompson J.E.
    Plant Cell Environ. 33:1682-1696(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "iTRAQ protein profile analysis of Arabidopsis roots reveals new aspects critical for iron homeostasis."
    Lan P., Li W., Wen T.N., Shiau J.Y., Wu Y.C., Lin W., Schmidt W.
    Plant Physiol. 155:821-834(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IRON DEFICIENCY.
  9. "The enigma of eIF5A in the iron deficiency response of Arabidopsis."
    Lan P., Schmidt W.
    Plant Signal. Behav. 6:528-530(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IRON DEFICIENCY.
  10. "The Arabidopsis eukaryotic translation initiation factor eIF5A-2 regulates root protoxylem development by modulating cytokinin signaling."
    Ren B., Chen Q., Hong S., Zhao W., Feng J., Feng H., Zuo J.
    Plant Cell 25:3841-3857(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.

Entry informationi

Entry nameiIF5A1_ARATH
AccessioniPrimary (citable) accession number: Q9XI91
Secondary accession number(s): Q9LMG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Translation initiation factors
    List of translation initiation factor entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.