IF5A_TRYB2
ID IF5A_TRYB2 Reviewed; 166 AA.
AC Q387H6;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Eukaryotic translation initiation factor 5A {ECO:0000255|RuleBase:RU362005};
DE Short=eIF-5A {ECO:0000255|RuleBase:RU362005};
GN Name=eIF5A {ECO:0000303|PubMed:26082486};
GN ORFNames=Tb11.03.0410 {ECO:0000312|EMBL:EAN79055.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1;
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, HYPUSINATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=26082486; DOI=10.1074/jbc.m115.656785;
RA Nguyen S., Leija C., Kinch L., Regmi S., Li Q., Grishin N.V.,
RA Phillips M.A.;
RT "Deoxyhypusine modification of eukaryotic translation initiation factor 5A
RT (eIF5A) is essential for Trypanosoma brucei growth and for expression of
RT polyprolyl-containing proteins.";
RL J. Biol. Chem. 290:19987-19998(2015).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC an important function at the level of mRNA turnover, probably acting
CC downstream of decapping (By similarity). Critical for the efficient
CC synthesis of peptide bonds between consecutive proline residues. Can
CC resolve ribosomal stalling caused by consecutive prolines during
CC translation (PubMed:26082486). Required for cell growth during both
CC bloodstream (BF) and insect procyclic (PF) life cycle stages and for
CC survival of the bloodstream form (PubMed:26082486).
CC {ECO:0000250|UniProtKB:P23301, ECO:0000269|PubMed:26082486}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26082486}.
CC Note=Localizes to the cytoplasm in the procyclic insect (PF) life cycle
CC stage. {ECO:0000269|PubMed:26082486}.
CC -!- DEVELOPMENTAL STAGE: Expressed during both bloodstream (BF) and
CC procyclic insect (PF) life cycle stages. {ECO:0000269|PubMed:26082486}.
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 Hypusination is mediated by the consecutive action of deoxyhypusine
CC synthase DHSc and deoxyhypusine hydroxylase DOHH (PubMed:26082486).
CC {ECO:0000255|RuleBase:RU362005, ECO:0000269|PubMed:26082486}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown at the bloodstream life
CC cycle stage causes a growth arrest followed by death. Cells become
CC abnormally round, the number of cells with 1N1K and 2N2K genetic
CC content is decreased whereas the number of cells with more than 2N2K
CC genetic content is increased. RNAi-mediated knockdown at the insect
CC procyclic life cycle stage causes a growth arrest without cell death.
CC Cells become abnormally round and about 40 percent have lost their
CC flagella. The number of cells with 2N1K and 2N2K genetic content is
CC increased whereas the number of cells with 1N1K and 1N2K genetic
CC content is reduced. The number of cells without nuclear DNA (0N1K),
CC known as zoids, is increased. In addition, protein expression levels of
CC formin (Tb927.5.2300) and CAP/Srv2p (Tb10.6k15.1160) are severely
CC reduced. {ECO:0000269|PubMed:26082486}.
CC -!- SIMILARITY: Belongs to the eIF-5A family.
CC {ECO:0000255|RuleBase:RU362005}.
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DR EMBL; CH464491; EAN79055.1; -; Genomic_DNA.
DR RefSeq; XP_828167.1; XM_823074.1.
DR AlphaFoldDB; Q387H6; -.
DR SMR; Q387H6; -.
DR STRING; 5691.EAN79055; -.
DR PaxDb; Q387H6; -.
DR GeneID; 3665847; -.
DR KEGG; tbr:Tb11.03.0410; -.
DR VEuPathDB; TriTrypDB:Tb927.11.740; -.
DR eggNOG; KOG3271; Eukaryota.
DR InParanoid; Q387H6; -.
DR Proteomes; UP000008524; Chromosome 11 Scaffold 1.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005844; C:polysome; ISO:GeneDB.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
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:0060491; P:regulation of cell projection assembly; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
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; IPR013185; Transl_elong_KOW-like.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF08207; EFP_N; 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 Cytoplasm; Elongation factor; Hypusine; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..166
FT /note="Eukaryotic translation initiation factor 5A"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438860"
FT REGION 99..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
SQ SEQUENCE 166 AA; 17820 MW; C1FC78B873157690 CRC64;
MSDDEGQFAE GGAQVGSLTY PMQAGALKKG GYICINGRPC KVIDLSVSKT GKHGHAKVSI
VALDIFTGNK MEDQAPSTHN VEVPFVKTAT YSVLDIQEDR EDPSKPAHLS LMDDEGETRD
NLDMPPNAEL AGQIKEQFDA GKDVLVVVVS AMGIDQILSF KNAAER
