IF5A2_YEAST
ID IF5A2_YEAST Reviewed; 157 AA.
AC P19211; D6VWL8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Eukaryotic translation initiation factor 5A-2;
DE Short=eIF-5A-2;
DE AltName: Full=Anaerobically induced protein 1;
DE AltName: Full=Hypusine-containing protein HP1;
DE AltName: Full=eIF-4D;
GN Name=ANB1; Synonyms=HYP1, TIF51B; OrderedLocusNames=YJR047C;
GN ORFNames=J1651;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2187871; DOI=10.1016/s0021-9258(19)38959-8;
RA Mehta K.D., Leung D., Lefebvre L., Smith M.;
RT "The ANB1 locus of Saccharomyces cerevisiae encodes the protein synthesis
RT initiation factor eIF-4D.";
RL J. Biol. Chem. 265:8802-8807(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND HYPUSINE AT LYS-51.
RX PubMed=1903841; DOI=10.1128/mcb.11.6.3105-3114.1991;
RA Schnier J., Schwelberger H.G., Smit-Mcbride Z., Kang H.A., Hershey J.W.B.;
RT "Translation initiation factor 5A and its hypusine modification are
RT essential for cell viability in the yeast Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 11:3105-3114(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBY874;
RA Sandholzer U.R.;
RL Submitted (DEC-1990) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7668047; DOI=10.1002/yea.320110809;
RA Huang M.-E., Chuat J.-C., Galibert F.;
RT "Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA
RT genes and 14 new open reading frames including a gene most probably
RT belonging to the family of ubiquitin-protein ligases.";
RL Yeast 11:775-781(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8, AND INDUCTION.
RX PubMed=2656688; DOI=10.1016/s0021-9258(18)81844-0;
RA Mehta K.D., Smith M.;
RT "Identification of an upstream repressor site controlling the expression of
RT an anaerobic gene (ANB1) in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 264:8670-8675(1989).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RX PubMed=2233724; DOI=10.1128/mcb.10.11.5921-5926.1990;
RA Lowry C.V., Esperanza Cerdan M., Zitomer R.S.;
RT "A hypoxic consensus operator and a constitutive activation region regulate
RT the ANB1 gene of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:5921-5926(1990).
RN [10]
RP FUNCTION.
RX PubMed=641056; DOI=10.1016/s0021-9258(17)40805-2;
RA Benne R., Hershey J.W.B.;
RT "The mechanism of action of protein synthesis initiation factors from
RT rabbit reticulocytes.";
RL J. Biol. Chem. 253:3078-3087(1978).
RN [11]
RP INDUCTION.
RX PubMed=3540607; DOI=10.1128/mcb.6.12.4145-4148.1986;
RA Lowry C.V., Lieber R.H.;
RT "Negative regulation of the Saccharomyces cerevisiae ANB1 gene by heme, as
RT mediated by the ROX1 gene product.";
RL Mol. Cell. Biol. 6:4145-4148(1986).
RN [12]
RP HYPUSINE FORMATION.
RX PubMed=3119589; DOI=10.1016/s0021-9258(18)49297-6;
RA Gordon E.D., Mora R., Meredith S.C., Lindquist S.L.;
RT "Hypusine formation in eukaryotic initiation factor 4D is not reversed when
RT rates or specificity of protein synthesis is altered.";
RL J. Biol. Chem. 262:16590-16595(1987).
RN [13]
RP INDUCTION.
RX PubMed=2852136; DOI=10.1093/genetics/120.3.671;
RA Trueblood C.E., Poyton R.O.;
RT "Identification of REO1, a gene involved in negative regulation of COX5b
RT and ANB1 in aerobically grown Saccharomyces cerevisiae.";
RL Genetics 120:671-680(1988).
RN [14]
RP INDUCTION.
RX PubMed=3062365; DOI=10.1128/mcb.8.11.4651-4658.1988;
RA Lowry C.V., Zitomer R.S.;
RT "ROX1 encodes a heme-induced repression factor regulating ANB1 and CYC7 of
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 8:4651-4658(1988).
RN [15]
RP INDUCTION.
RX PubMed=8314769; DOI=10.1016/s0021-9258(19)85203-1;
RA Schwelberger H.G., Kang H.A., Hershey J.W.B.;
RT "Translation initiation factor eIF-5A expressed from either of two yeast
RT genes or from human cDNA. Functional identity under aerobic and anaerobic
RT conditions.";
RL J. Biol. Chem. 268:14018-14025(1993).
RN [16]
RP FUNCTION.
RX PubMed=8307948; DOI=10.1016/s0021-9258(17)41723-6;
RA Kang H.A., Hershey J.W.B.;
RT "Effect of initiation factor eIF-5A depletion on protein synthesis and
RT proliferation of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:3934-3940(1994).
RN [17]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [18]
RP FUNCTION.
RX PubMed=19338753; DOI=10.1016/j.bbrc.2009.01.148;
RA Gregio A.P.B., Cano V.P.S., Avaca J.S., Valentini S.R., Zanelli C.F.;
RT "eIF5A has a function in the elongation step of translation in yeast.";
RL Biochem. Biophys. Res. Commun. 380:785-790(2009).
RN [19]
RP FUNCTION.
RX PubMed=19424157; DOI=10.1038/nature08034;
RA Saini P., Eyler D.E., Green R., Dever T.E.;
RT "Hypusine-containing protein eIF5A promotes translation elongation.";
RL Nature 459:118-121(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND THR-7, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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. Essential for polarized growth, a
CC process necessary for G1/S transition. May mediate large range of
CC effects of the polyamine spermidine in the cell (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P63241,
CC ECO:0000269|PubMed:19338753, ECO:0000269|PubMed:19424157,
CC ECO:0000269|PubMed:641056, ECO:0000269|PubMed:8307948}.
CC -!- SUBUNIT: Homodimer. Interacts with DYS1 and LIA1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Concentrates in the perinuclear
CC region.
CC -!- INDUCTION: Expressed in anaerobic conditions. Down-regulated by heme
CC and the ROX1 and REO1 transcription factors in aerobic conditions.
CC {ECO:0000269|PubMed:2656688, ECO:0000269|PubMed:2852136,
CC ECO:0000269|PubMed:3062365, ECO:0000269|PubMed:3540607,
CC ECO:0000269|PubMed:8314769}.
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:0000269|PubMed:1903841, ECO:0000269|PubMed:3119589}.
CC -!- MISCELLANEOUS: There are two genes for eIF-5A in yeast.
CC -!- MISCELLANEOUS: Present with 14200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a translation initiation factor
CC but further analysis (PubMed:19424157 and PubMed:19338753) clearly
CC suggests that it is involved in translation elongation and not
CC translation initiation. {ECO:0000305|PubMed:641056}.
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DR EMBL; J05455; AAA34425.1; -; Genomic_DNA.
DR EMBL; M63542; AAA35156.1; -; Genomic_DNA.
DR EMBL; M60477; AAA34424.1; -; Genomic_DNA.
DR EMBL; L36344; AAA88750.1; -; Genomic_DNA.
DR EMBL; Z49547; CAA89575.1; -; Genomic_DNA.
DR EMBL; AY557894; AAS56220.1; -; Genomic_DNA.
DR EMBL; X56235; CAA39692.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08834.1; -; Genomic_DNA.
DR PIR; B40259; FIBYA2.
DR RefSeq; NP_012581.3; NM_001181705.3.
DR AlphaFoldDB; P19211; -.
DR SMR; P19211; -.
DR BioGRID; 33800; 56.
DR IntAct; P19211; 3.
DR MINT; P19211; -.
DR STRING; 4932.YJR047C; -.
DR iPTMnet; P19211; -.
DR MaxQB; P19211; -.
DR PaxDb; P19211; -.
DR PRIDE; P19211; -.
DR EnsemblFungi; YJR047C_mRNA; YJR047C; YJR047C.
DR GeneID; 853506; -.
DR KEGG; sce:YJR047C; -.
DR SGD; S000003808; ANB1.
DR VEuPathDB; FungiDB:YJR047C; -.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; P19211; -.
DR OMA; VTYPQQC; -.
DR BioCyc; YEAST:G3O-31682-MON; -.
DR Reactome; R-SCE-204626; Hypusine synthesis from eIF5A-lysine.
DR PRO; PR:P19211; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P19211; protein.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; ISA:SGD.
DR GO; GO:0003723; F:RNA binding; ISA:SGD.
DR GO; GO:0003746; F:translation elongation factor activity; ISA:SGD.
DR GO; GO:0045901; P:positive regulation of translational elongation; IGI:SGD.
DR GO; GO:0045905; P:positive regulation of translational termination; ISA:SGD.
DR GO; GO:0006452; P:translational frameshifting; IGI:SGD.
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 Acetylation; Cytoplasm; Elongation factor; Hypusine; Isopeptide bond;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23301"
FT CHAIN 2..157
FT /note="Eukaryotic translation initiation factor 5A-2"
FT /id="PRO_0000142487"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P23301"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 51
FT /note="Hypusine"
FT /evidence="ECO:0000269|PubMed:1903841"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23301"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P23301"
SQ SEQUENCE 157 AA; 17131 MW; A578164B760ED9E7 CRC64;
MSDEEHTFEN ADAGASATYP MQCSALRKNG FVVIKGRPCK IVDMSTSKTG KHGHAKVHLV
TLDIFTGKKL EDLSPSTHNL EVPFVKRSEY QLLDIDDGYL SLMTMDGETK DDVKAPEGEL
GDSMQAAFDE GKDLMVTIIS AMGEEAAISF KEAPRSD
