EIF3I_SCHPO
ID EIF3I_SCHPO Reviewed; 328 AA.
AC P79083; P78838;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit I {ECO:0000255|HAMAP-Rule:MF_03008};
DE Short=eIF3i {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=Eukaryotic translation initiation factor 3 39 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03008};
DE Short=eIF-3 39 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03008};
DE Short=eIF3 p39;
DE AltName: Full=Suppressor of uncontrolled mitosis 1;
GN Name=sum1; Synonyms=eif3i, tif34; ORFNames=SPAC4D7.05;
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], AND FUNCTION.
RX PubMed=9560390; DOI=10.1093/genetics/148.4.1731;
RA Humphrey T., Enoch T.;
RT "Sum1, a highly conserved WD-repeat protein, suppresses S-M checkpoint
RT mutants and inhibits the osmotic stress cell cycle response in fission
RT yeast.";
RL Genetics 148:1731-1742(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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 IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [5]
RP INTERACTION WITH INT6; MOE1 AND SPAC25G10.08.
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 [6]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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_03008, ECO:0000269|PubMed:9560390}.
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. {ECO:0000255|HAMAP-Rule:MF_03008,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit I family. {ECO:0000255|HAMAP-
CC Rule:MF_03008}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y09529; CAA70722.1; -; mRNA.
DR EMBL; D89187; BAA13849.1; ALT_INIT; mRNA.
DR EMBL; CU329670; CAB11277.1; -; Genomic_DNA.
DR PIR; T38796; T38796.
DR PIR; T42745; T42745.
DR PIR; T46558; T46558.
DR RefSeq; NP_594958.1; NM_001020389.2.
DR AlphaFoldDB; P79083; -.
DR SMR; P79083; -.
DR BioGRID; 279954; 28.
DR STRING; 4896.SPAC4D7.05.1; -.
DR iPTMnet; P79083; -.
DR MaxQB; P79083; -.
DR PaxDb; P79083; -.
DR PRIDE; P79083; -.
DR EnsemblFungi; SPAC4D7.05.1; SPAC4D7.05.1:pep; SPAC4D7.05.
DR GeneID; 2543537; -.
DR KEGG; spo:SPAC4D7.05; -.
DR PomBase; SPAC4D7.05; sum1.
DR VEuPathDB; FungiDB:SPAC4D7.05; -.
DR eggNOG; KOG0643; Eukaryota.
DR HOGENOM; CLU_043845_0_1_1; -.
DR InParanoid; P79083; -.
DR OMA; VWFSHNG; -.
DR PhylomeDB; P79083; -.
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:P79083; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0010494; C:cytoplasmic stress granule; EXP:PomBase.
DR GO; GO:0005829; C:cytosol; HDA: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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IMP:PomBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03008; eIF3i; 1.
DR InterPro; IPR027525; eIF3i.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Nucleus; Protein biosynthesis;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..328
FT /note="Eukaryotic translation initiation factor 3 subunit
FT I"
FT /id="PRO_0000051040"
FT REPEAT 8..49
FT /note="WD 1"
FT REPEAT 50..89
FT /note="WD 2"
FT REPEAT 145..184
FT /note="WD 3"
FT REPEAT 189..228
FT /note="WD 4"
FT REPEAT 286..327
FT /note="WD 5"
SQ SEQUENCE 328 AA; 36811 MW; B8AD55B50F84583C CRC64;
MRPIILQGHE RPLTQIKYNH DGDLLFSCAK DKVINVWFSH NGERLGTYEG HTGAIWTCDI
NKSSTLMVSG AADNTMRLWD VKTGKQLYKW EFPTAVKRVE FNEDDTRILA VTEERMGYAG
TVTVFRVPIS ESDAAAETPL YVITTRESKA TVAGWSYLSK FLFTGHEDGS VSRYDAITGE
FVESKQVHNS GSTITDLQFY PDRTYFITSC KDTTAKAIDV DSFEVIKTYL TDTPLNTSSF
TPVQDFVILG GGQEARDVTT TAARQGKFEA RFYHAILEEE LGRVKGHFGP INTIAVHPKG
TGYASGGEDG YVRVHFFDKN YFDFKYTL
