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 27-MAR-2024, entry version 161.
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; 25.
DR IntAct; Q10425; 1.
DR STRING; 284812.Q10425; -.
DR iPTMnet; Q10425; -.
DR MaxQB; Q10425; -.
DR PaxDb; 4896-SPAC25G10-08-1; -.
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; LWGGPQF; -.
DR PhylomeDB; Q10425; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
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; 3.30.70.330; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 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
//
