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EIF3B_SCHPO
ID   EIF3B_SCHPO             Reviewed;         725 AA.
AC   Q10425;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Eukaryotic translation initiation factor 3 90 kDa subunit homolog {ECO:0000255|HAMAP-Rule:MF_03001};
DE            Short=eIF3 p90 {ECO:0000255|HAMAP-Rule:MF_03001};
DE   AltName: Full=Translation initiation factor eIF3 p90 subunit homolog;
DE   AltName: Full=spPrt1;
GN   ORFNames=SPAC25G10.08;
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   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   [3]
RP   INTERACTION WITH SUM1, AND ASSOCIATION WITH THE 40S 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   [4]
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-135 AND THR-136, 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: RNA-binding component of the eukaryotic translation
CC       initiation factor 3 (eIF-3) complex, which is involved in protein
CC       synthesis of a specialized repertoire of mRNAs and, together with other
CC       initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC       the 40S 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_03001}.
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_03001,
CC       ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001,
CC       ECO:0000269|PubMed:15904532}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC       Rule:MF_03001}.
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DR   EMBL; CU329670; CAA94637.1; -; Genomic_DNA.
DR   PIR; T38379; T38379.
DR   RefSeq; NP_594528.1; NM_001019957.2.
DR   AlphaFoldDB; Q10425; -.
DR   SMR; Q10425; -.
DR   BioGRID; 278567; 24.
DR   IntAct; Q10425; 1.
DR   STRING; 4896.SPAC25G10.08.1; -.
DR   iPTMnet; Q10425; -.
DR   MaxQB; Q10425; -.
DR   PaxDb; Q10425; -.
DR   PRIDE; Q10425; -.
DR   EnsemblFungi; SPAC25G10.08.1; SPAC25G10.08.1:pep; SPAC25G10.08.
DR   GeneID; 2542090; -.
DR   KEGG; spo:SPAC25G10.08; -.
DR   PomBase; SPAC25G10.08; -.
DR   VEuPathDB; FungiDB:SPAC25G10.08; -.
DR   eggNOG; KOG2314; Eukaryota.
DR   HOGENOM; CLU_011152_4_0_1; -.
DR   InParanoid; Q10425; -.
DR   OMA; NVADCKI; -.
DR   PhylomeDB; Q10425; -.
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:Q10425; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA: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:0003723; F:RNA binding; ISM:PomBase.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   CDD; cd12278; RRM_eIF3B; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   HAMAP; MF_03001; eIF3b; 1.
DR   InterPro; IPR011400; EIF3B.
DR   InterPro; IPR034363; eIF3B_RRM.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   InterPro; IPR013979; TIF_beta_prop-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR14068; PTHR14068; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00361; RRM_1; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat.
FT   CHAIN           1..725
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   B"
FT                   /id="PRO_0000123534"
FT   DOMAIN          39..129
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   REPEAT          190..229
FT                   /note="WD 1"
FT   REPEAT          304..344
FT                   /note="WD 2"
FT   REPEAT          347..386
FT                   /note="WD 3"
FT   COILED          630..671
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT                   ECO:0000269|PubMed:18257517"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03001,
FT                   ECO:0000269|PubMed:18257517"
FT   MOD_RES         136
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   725 AA;  84035 MW;  D4725583F7F9EE34 CRC64;
     MSEILIEEIK DQIVVKDEEI DVSELEVKLN VTKPVGYDTV VVIEGAPVVE EAKQQDFFRF
     LSSKVLAKIG KVKENGFYMP FEEKNGKKMS LGLVFADFEN VDGADLCVQE LDGKQILKNH
     TFVVRKLNQL EKAFSTPDEF SFEEREFKER EHLRSWLTDY YGRDQFISYY GNRVSVNWNR
     KSDVPEQIVD RENWTETYVQ WSPMGTYLVS LHLRGIQLWG GESWGMCARF LHPYVKFVDF
     SPNEKYLVSW SYEPVRLPPI GHPARETMPF TDDDEGKHCF VWDIASGRIL RSFKIPPQPE
     GSKDGKKVIW PIFKWSADDK YLARVTVGQS ISVYETPSLA LVDKKTIKID GVQNFEWCPV
     SDALGRDSKE QLLAYWTPEI TNQPARVALI SIPSKSTIRT KNLFNVSDCK LYWQSNGDYL
     CVKVDRHTKT KKSTFSNLEI FRIREKNIPV EVVDLKDVVL NFAWEPKSDR FAIISANDQV
     LNSTNVKTNL SFYGFEQKKN TPSTFRHIIT FDKKTCNSLF MAPKGRFMVA ATLGSSTQYD
     LEFYDLDFDT EKKEPDALAN VQQIGSAEHF GMTELEWDPS GRYVTTSSTI WRHKLENGYR
     LCDFRGTLLR EEMIGEFKQF IWRPRPPSPL TKEDMKKIRK KLKDYNRLFD EEDIAEQSSA
     NRELAARRRQ LISEWQKYRD EVIARVAEER AITGQPAITV PAEEEEIIQE TVEEVISEEI
     EPVED
 
 
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