IF5A1_SCHPO
ID IF5A1_SCHPO Reviewed; 157 AA.
AC P56289; Q76N36;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 5A-1;
DE Short=eIF-5A-1;
GN Name=tif51a; Synonyms=tif51; ORFNames=SPAC26H5.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-157.
RA Kawamukai M.;
RT "S. pombe eIF5A.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77 AND THR-78, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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-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:P23301}.
CC -!- MISCELLANEOUS: There are two genes for eIF-5A in S.pombe.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16195.1; -; Genomic_DNA.
DR EMBL; AB009604; BAA24001.1; -; mRNA.
DR PIR; T38429; T38429.
DR PIR; T43305; T43305.
DR RefSeq; NP_594457.1; NM_001019886.2.
DR AlphaFoldDB; P56289; -.
DR SMR; P56289; -.
DR BioGRID; 279147; 6.
DR STRING; 4896.SPAC26H5.10c.1; -.
DR iPTMnet; P56289; -.
DR MaxQB; P56289; -.
DR PaxDb; P56289; -.
DR PRIDE; P56289; -.
DR EnsemblFungi; SPAC26H5.10c.1; SPAC26H5.10c.1:pep; SPAC26H5.10c.
DR GeneID; 2542694; -.
DR KEGG; spo:SPAC26H5.10c; -.
DR PomBase; SPAC26H5.10c; -.
DR VEuPathDB; FungiDB:SPAC26H5.10c; -.
DR eggNOG; KOG3271; Eukaryota.
DR HOGENOM; CLU_102600_1_0_1; -.
DR InParanoid; P56289; -.
DR OMA; TIMINIQ; -.
DR PhylomeDB; P56289; -.
DR Reactome; R-SPO-204626; Hypusine synthesis from eIF5A-lysine.
DR PRO; PR:P56289; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043022; F:ribosome binding; ISO:PomBase.
DR GO; GO:0003723; F:RNA binding; ISO:PomBase.
DR GO; GO:0003746; F:translation elongation factor activity; ISO:PomBase.
DR GO; GO:0008079; F:translation termination factor activity; ISO:PomBase.
DR GO; GO:0002182; P:cytoplasmic translational elongation; ISO:PomBase.
DR GO; GO:0002184; P:cytoplasmic translational termination; ISO:PomBase.
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 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; Hypusine; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..157
FT /note="Eukaryotic translation initiation factor 5A-1"
FT /id="PRO_0000142485"
FT MOD_RES 52
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P23301"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 157 AA; 17152 MW; 7D8877E20DC5D2C0 CRC64;
MAEEEHVDFE GGEAGASLTF PMQCSALRKN GHVVIKGRPC KIVDMSTSKT GKHGHAKVHI
VALDIFNGRK YEDMSPSTHN MDVPVVKRDE YQLVNIDDGY LNLMTTDGTT KDDVRLPEGE
LGNEIEEGFD EGRDLIITVV SAMGEETALA CRDAPSS
