EIF3E_SCHPO
ID EIF3E_SCHPO Reviewed; 501 AA.
AC O94513;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit E {ECO:0000255|HAMAP-Rule:MF_03004};
DE Short=eIF3e {ECO:0000255|HAMAP-Rule:MF_03004};
GN Name=int6; Synonyms=eif3e, yin6; ORFNames=SPBC646.09c;
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 [MRNA], INTERACTION WITH SPAC25G10.08 AND SUM1,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11071922; DOI=10.1091/mbc.11.11.3993;
RA Crane R., Craig R., Murray R., Dunand-Sauthier I., Humphrey T., Norbury C.;
RT "A fission yeast homolog of int-6, the mammalian oncoprotein and eIF3
RT subunit, induces drug resistance when overexpressed.";
RL Mol. Biol. Cell 11:3993-4003(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH MOE1.
RX PubMed=11121040; DOI=10.1073/pnas.97.26.14370;
RA Yen H.-C.S., Chang E.C.;
RT "Yin6, a fission yeast Int6 homolog, complexes with moe1 and plays a role
RT in chromosome segregation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14370-14375(2000).
RN [3]
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 [4]
RP DISRUPTION PHENOTYPE, ASSOCIATION WITH THE 40S RIBOSOME, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11071923; DOI=10.1091/mbc.11.11.4005;
RA Bandyopadhyay A., Matsumoto T., Maitra U.;
RT "Fission yeast Int6 is not essential for global translation initiation, but
RT deletion of int6(+) causes hypersensitivity to caffeine and affects spore
RT formation.";
RL Mol. Biol. Cell 11:4005-4018(2000).
RN [5]
RP INTERACTION WITH TIF35, IDENTIFICATION IN THE EIF-3 COMPLEX, ASSOCIATION
RP WITH THE 40S RIBOSOME, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11134033; DOI=10.1074/jbc.m010188200;
RA Akiyoshi Y., Clayton J., Phan L., Yamamoto M., Hinnebusch A.G.,
RA Watanabe Y., Asano K.;
RT "Fission yeast homolog of murine Int-6 protein, encoded by mouse mammary
RT tumor virus integration site, is associated with the conserved core
RT subunits of eukaryotic translation initiation factor 3.";
RL J. Biol. Chem. 276:10056-10062(2001).
RN [6]
RP INTERACTION WITH SPAC25G10.08; MOE1 AND SUM1, AND ASSOCIATION WITH THE 40S
RP RIBOSOME.
RX PubMed=11705997; DOI=10.1074/jbc.m107790200;
RA Bandyopadhyay A., Lakshmanan V., Matsumoto T., Chang E.C., Maitra U.;
RT "Moe1 and spInt6, the fission yeast homologues of mammalian translation
RT initiation factor 3 subunits p66 (eIF3d) and p48 (eIF3e), respectively, are
RT required for stable association of eIF3 subunits.";
RL J. Biol. Chem. 277:2360-2367(2002).
RN [7]
RP FUNCTION, INTERACTION WITH RPN501/RPN502, AND DISRUPTION PHENOTYPE.
RX PubMed=12553909; DOI=10.1016/s0092-8674(03)00043-6;
RA Yen H.-C.S., Gordon C., Chang E.C.;
RT "Schizosaccharomyces pombe Int6 and Ras homologs regulate cell division and
RT mitotic fidelity via the proteasome.";
RL Cell 112:207-217(2003).
RN [8]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15904532; DOI=10.1186/1741-7007-3-14;
RA Zhou C., Arslan F., Wee S., Krishnan S., Ivanov A.R., Oliva A.,
RA Leatherwood J., Wolf D.A.;
RT "PCI proteins eIF3e and eIF3m define distinct translation initiation factor
RT 3 complexes.";
RL BMC Biol. 3:14-14(2005).
RN [9]
RP MUTAGENESIS OF LEU-332.
RX PubMed=17761670; DOI=10.1074/jbc.m706276200;
RA Sha Z., Yen H.-C.S., Scheel H., Suo J., Hofmann K., Chang E.C.;
RT "Isolation of the Schizosaccharomyces pombe proteasome subunit Rpn7 and a
RT structure-function study of the proteasome-COP9-initiation factor domain.";
RL J. Biol. Chem. 282:32414-32423(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18502752; DOI=10.1074/jbc.m710017200;
RA Udagawa T., Nemoto N., Wilkinson C.R.M., Narashimhan J., Jiang L., Watt S.,
RA Zook A., Jones N., Wek R.C., Baehler J., Asano K.;
RT "Int6/eIF3e promotes general translation and Atf1 abundance to modulate
RT Sty1 MAPK-dependent stress response in fission yeast.";
RL J. Biol. Chem. 283:22063-22075(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-479, 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: 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 (Potential). Required for maintaining the basal level of atf1 and for
CC transcriptional activation of core environmental stress response genes
CC (CESR genes) in response to histidine starvation (PubMed:18502752). May
CC positively regulate proteasome activity (PubMed:12553909). Required for
CC nuclear localization of the proteasome subunit rpn501/rpn502
CC (PubMed:12553909). {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:12553909, ECO:0000269|PubMed:18502752}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. The eIF-3 complex appears to include tif32/eif3a,
CC SPAC25G10.08/eif3b, tif33/eif3c, SPBC4C3.07/eif3f, tif35/eif3g and
CC sum1/eif3i. This set of common subunits may also associate exclusively
CC with either moe1/eif3d and int6/eif3e, or with SPAC821.05/eif3h and
CC SPAC1751.03/eif3m. The eIF-3 complex may also include
CC SPAC3A12.13c/eif3j. Also interacts with the proteasome via
CC rpn501/rpn502. {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:11071922, ECO:0000269|PubMed:11121040,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:11705997,
CC ECO:0000269|PubMed:12553909, ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004,
CC ECO:0000269|PubMed:11071922, ECO:0000269|PubMed:11071923,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
CC -!- DISRUPTION PHENOTYPE: Slow growth, reduced polysome content and reduced
CC translational initiation in minimal medium. Mislocalization of
CC proteasome subunits to the cytoplasm and impaired proteasome assembly,
CC leading to the accumulation of polyubiquitinated proteins including
CC cut2 and cdc13. Impaired mitosis and spore formation. Enhanced
CC sensitivity to 3-aminotriazole (3AT), caffeine and thiabendazole.
CC {ECO:0000269|PubMed:11071922, ECO:0000269|PubMed:11071923,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:12553909,
CC ECO:0000269|PubMed:18502752}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit E family. {ECO:0000255|HAMAP-
CC Rule:MF_03004}.
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DR EMBL; AF117648; AAD29969.1; -; mRNA.
DR EMBL; AF260238; AAG41139.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22813.1; -; Genomic_DNA.
DR PIR; T40585; T40585.
DR PIR; T50488; T50488.
DR RefSeq; NP_595367.1; NM_001021275.2.
DR AlphaFoldDB; O94513; -.
DR SMR; O94513; -.
DR BioGRID; 277604; 158.
DR STRING; 4896.SPBC646.09c.1; -.
DR iPTMnet; O94513; -.
DR MaxQB; O94513; -.
DR PaxDb; O94513; -.
DR PRIDE; O94513; -.
DR EnsemblFungi; SPBC646.09c.1; SPBC646.09c.1:pep; SPBC646.09c.
DR GeneID; 2541089; -.
DR KEGG; spo:SPBC646.09c; -.
DR PomBase; SPBC646.09c; int6.
DR VEuPathDB; FungiDB:SPBC646.09c; -.
DR eggNOG; KOG2758; Eukaryota.
DR HOGENOM; CLU_031132_0_0_1; -.
DR InParanoid; O94513; -.
DR OMA; TWGKLAC; -.
DR PhylomeDB; O94513; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:O94513; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:PomBase.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:PomBase.
DR GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070196; P:eukaryotic translation initiation factor 3 complex assembly; IMP:PomBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR HAMAP; MF_03004; eIF3e; 1.
DR InterPro; IPR016650; eIF3e.
DR InterPro; IPR019010; eIF3e_N.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR10317; PTHR10317; 1.
DR Pfam; PF09440; eIF3_N; 1.
DR PIRSF; PIRSF016255; eIF3e_su6; 1.
DR SMART; SM01186; eIF3_N; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Stress response.
FT CHAIN 1..501
FT /note="Eukaryotic translation initiation factor 3 subunit
FT E"
FT /id="PRO_0000123519"
FT DOMAIN 245..423
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 332
FT /note="L->D: Abrogates interaction with the proteasome."
FT /evidence="ECO:0000269|PubMed:17761670"
FT CONFLICT 311
FT /note="P -> H (in Ref. 1; AAD29969)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="I -> N (in Ref. 1; AAD29969)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 501 AA; 57114 MW; 425AA7B284913831 CRC64;
MGSELKSTSP LAVKYDLSQK IMQHLDRHLI FPLLEFLSLR QTHDPKELLQ AKYDLLKDTN
MTDYVANLWT NLHGGHTDED MANAFAEKRR SVLQELSELE EEVQGILGVL ENPDLIAALR
QDKGQNLQHL QEHYNITPER IAVLYKFAQF QYNCGNYGGA SDLLYHFRAF SKDPELNASA
TWGKFASEIL TVDWDGAMEE LGKLREMVDS KSFKDSAVQL RNRTWLLHWS LFPLFNHANG
CDTLCDLFFY TPYLNTIQTS CPWLLRYLTV AVVTNQNNAN QKPRNPRQSY QRRMRDLVRI
ISQENYEYSD PVTSFISALY TEVDFEKAQH CLRECEEVLK TDFFLVSLCD HFLEGARKLL
AEAYCRIHSV ISVDVLANKL EMDSAQLIQL VENRNNPSVA AASNVAADQS TEDESIESTS
TNVVADDLIT EAETATEAEE PEPEVQFGFK AKLDGESIII EHPTYSAFQQ IIDRTKSLSF
ESQNLEQSLA KSISELKHAT V
