EIF3J_YEAST
ID EIF3J_YEAST Reviewed; 265 AA.
AC Q05775; D6VYJ5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=Eukaryotic translation initiation factor 3 30 kDa subunit;
DE Short=eIF-3 30 kDa;
DE AltName: Full=High-copy suppressor of Rpg1 protein 1 {ECO:0000303|PubMed:10488093};
GN Name=HCR1 {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000303|PubMed:10488093};
GN OrderedLocusNames=YLR192C; ORFNames=L8167.11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=10488093; DOI=10.1074/jbc.274.39.27567;
RA Valasek L., Hasek J., Trachsel H., Imre E.M., Ruis H.;
RT "The Saccharomyces cerevisiae HCR1 gene encoding a homologue of the p35
RT subunit of human translation initiation factor 3 (eIF3) is a high copy
RT suppressor of a temperature-sensitive mutation in the Rpg1p subunit of
RT yeast eIF3.";
RL J. Biol. Chem. 274:27567-27572(1999).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP INTERACTION WITH PRT1, ASSOCIATION WITH THE 40S RIBOSOME, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ARG-215.
RX PubMed=16581774; DOI=10.1128/mcb.26.8.2984-2998.2006;
RA Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.;
RT "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of
RT eukaryotic initiation factor 3 in yeast.";
RL Mol. Cell. Biol. 26:2984-2998(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75 AND SER-92, 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).
RN [11]
RP METHYLATION AT ARG-220, AND PHOSPHORYLATION AT SER-65 AND THR-75.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
RN [12] {ECO:0007744|PDB:6ZCE, ECO:0007744|PDB:7A1G}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS).
RX PubMed=33289941; DOI=10.15252/embj.2020105179;
RA Kratzat H., Mackens-Kiani T., Ameismeier M., Potocnjak M., Cheng J.,
RA Dacheux E., Namane A., Berninghausen O., Herzog F., Fromont-Racine M.,
RA Becker T., Beckmann R.;
RT "A structural inventory of native ribosomal ABCE1-43S pre-initiation
RT complexes.";
RL EMBO J. 40:e105179-e105179(2021).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000269|PubMed:10488093}.
CC -!- SUBUNIT: Probable component of the eukaryotic translation initiation
CC factor 3 (eIF-3) complex. Is not part of the eIF-3 core complex, with
CC which it is associated in substochiometric amounts.
CC -!- INTERACTION:
CC Q05775; Q03195: RLI1; NbExp=4; IntAct=EBI-8944, EBI-35146;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009,
CC ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Marked reduction in binding of the eIF-3 core
CC complex to 40S ribosomes. {ECO:0000269|PubMed:16581774}.
CC -!- MISCELLANEOUS: Present with 17900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC Rule:MF_03009}.
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DR EMBL; U14913; AAB67433.1; -; Genomic_DNA.
DR EMBL; AY557943; AAS56269.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09511.1; -; Genomic_DNA.
DR PIR; S48545; S48545.
DR RefSeq; NP_013293.1; NM_001182079.1.
DR PDB; 6ZCE; EM; 5.30 A; s/t=1-265.
DR PDB; 7A1G; EM; 3.00 A; y/z=1-265.
DR PDBsum; 6ZCE; -.
DR PDBsum; 7A1G; -.
DR AlphaFoldDB; Q05775; -.
DR SMR; Q05775; -.
DR BioGRID; 31462; 372.
DR DIP; DIP-4532N; -.
DR IntAct; Q05775; 24.
DR MINT; Q05775; -.
DR STRING; 4932.YLR192C; -.
DR iPTMnet; Q05775; -.
DR MaxQB; Q05775; -.
DR PaxDb; Q05775; -.
DR PRIDE; Q05775; -.
DR EnsemblFungi; YLR192C_mRNA; YLR192C; YLR192C.
DR GeneID; 850889; -.
DR KEGG; sce:YLR192C; -.
DR SGD; S000004182; HCR1.
DR VEuPathDB; FungiDB:YLR192C; -.
DR eggNOG; KOG4813; Eukaryota.
DR HOGENOM; CLU_085412_0_0_1; -.
DR InParanoid; Q05775; -.
DR OMA; NVLMKDK; -.
DR BioCyc; YEAST:G3O-32314-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q05775; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05775; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IPI:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IPI:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IPI:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR Gene3D; 1.10.246.60; -; 1.
DR HAMAP; MF_03009; eIF3j; 1.
DR InterPro; IPR023194; eIF3-like_dom_sf.
DR InterPro; IPR013906; eIF3j.
DR PANTHER; PTHR21681; PTHR21681; 1.
DR Pfam; PF08597; eIF3_subunit; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..265
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000123509"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MUTAGEN 215
FT /note="R->I: Increased association of the eIF-3 complex and
FT 40S ribosomes."
FT /evidence="ECO:0000269|PubMed:16581774"
FT HELIX 147..161
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 190..218
FT /evidence="ECO:0007829|PDB:7A1G"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:7A1G"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7A1G"
SQ SEQUENCE 265 AA; 29564 MW; BDDBC5943DD7F9BB CRC64;
MSWDDEAING SMGNDDAVLM DSWDAEIGDD EPVMQSWDAE EEEKKPAPKP KKEQPKKVKK
GKESSADRAL LDIDTLDEKT RKELIKKAEM ESDLNNAADL FAGLGVAEEH PRARALQKEQ
EEQALKRPAF TKDTPIETHP LFNAETKREY QDLRKALTAA ITPMNKKSPL NYSSSLAIDL
IRDVAKPMSI ESIRQTVATL NVLIKDKERE ERQARLARVR GGTATGGAGK KKVKGKTNLG
GAFKKDQDFD LDGPDDFEFG DDDFM
