IF5A_NEUCR
ID IF5A_NEUCR Reviewed; 163 AA.
AC P38672; Q7RVF1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Eukaryotic translation initiation factor 5A;
DE Short=eIF-5A;
DE AltName: Full=eIF-4D;
GN Name=tif-51; ORFNames=NCU05274;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8093005; DOI=10.1042/bj3020517;
RA Tao Y., Chen K.Y.;
RT "PCR-based cloning of the full-length Neurospora eukaryotic initiation
RT factor 5A cDNA: polyhistidine-tagging and overexpression for protein
RT affinity binding.";
RL Biochem. J. 302:517-525(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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. Critical for the efficient synthesis of
CC peptide bonds between consecutive proline residues. Can resolve
CC ribosomal stalling caused by consecutive prolines during translation
CC (By similarity). Involved in actin dynamics and cell cycle progression,
CC mRNA decay and probably in a pathway involved in stress response and
CC maintenance of cell wall integrity. Functions as a regulator of
CC apoptosis (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P63241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Lys-57 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:P23301}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; U02638; AAA61707.1; -; mRNA.
DR EMBL; CM002239; EAA32675.2; -; Genomic_DNA.
DR PIR; S55278; S55278.
DR RefSeq; XP_961911.2; XM_956818.3.
DR AlphaFoldDB; P38672; -.
DR SMR; P38672; -.
DR STRING; 5141.EFNCRP00000004938; -.
DR PRIDE; P38672; -.
DR EnsemblFungi; EAA32675; EAA32675; NCU05274.
DR GeneID; 3878064; -.
DR KEGG; ncr:NCU05274; -.
DR VEuPathDB; FungiDB:NCU05274; -.
DR HOGENOM; CLU_102600_1_0_1; -.
DR InParanoid; P38672; -.
DR OMA; VFRNEYQ; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 Cytoplasm; Elongation factor; Hypusine; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..163
FT /note="Eukaryotic translation initiation factor 5A"
FT /id="PRO_0000142484"
FT MOD_RES 57
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P23301"
FT CONFLICT 21
FT /note="A -> R (in Ref. 1; AAA61707)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..119
FT /note="DV -> EL (in Ref. 1; AAA61707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 18035 MW; 956F5DC9C406BC6A CRC64;
MSAAHDDAQH EHTFDSVDAG ASATYPMQCS ALRKGGHVVI KNRPCKIVDM STSKTGKHGH
AKVHLVAIDI FTGKKLEDLC PSTHNMDVPN VKRTDYQFSY IDEDFLVLID SNGEEKRDVK
MPEGELAKRI EKLEEEGKDF FVGVQTAMGE EAAIDVKEAS NKD
