EIF3G_SCHPO
ID EIF3G_SCHPO Reviewed; 282 AA.
AC P78795;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF3g {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Translation initiation factor eIF3 p33 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF3 p33 homolog {ECO:0000255|HAMAP-Rule:MF_03006};
GN Name=tif35; Synonyms=eif3g; ORFNames=SPBC18H10.03;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-282.
RA Kawamukai M.;
RT "S.pombe translation initiation factor 3.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-282.
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 [4]
RP INTERACTION WITH INT6, IDENTIFICATION IN THE EIF-3 COMPLEX, AND
RP IDENTIFICATION BY MASS 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 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-164, 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. This
CC subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006}.
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_03006,
CC ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
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DR EMBL; CU329671; CAA18400.1; -; Genomic_DNA.
DR EMBL; AB011823; BAA25105.1; -; mRNA.
DR EMBL; D89144; BAA13806.1; -; mRNA.
DR PIR; T39767; T39767.
DR RefSeq; NP_595727.1; NM_001021625.2.
DR AlphaFoldDB; P78795; -.
DR SMR; P78795; -.
DR BioGRID; 277337; 8.
DR IntAct; P78795; 1.
DR MINT; P78795; -.
DR STRING; 4896.SPBC18H10.03.1; -.
DR iPTMnet; P78795; -.
DR MaxQB; P78795; -.
DR PaxDb; P78795; -.
DR PRIDE; P78795; -.
DR EnsemblFungi; SPBC18H10.03.1; SPBC18H10.03.1:pep; SPBC18H10.03.
DR GeneID; 2540819; -.
DR KEGG; spo:SPBC18H10.03; -.
DR PomBase; SPBC18H10.03; tif35.
DR VEuPathDB; FungiDB:SPBC18H10.03; -.
DR eggNOG; KOG0122; Eukaryota.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; P78795; -.
DR OMA; TTKCPFK; -.
DR PhylomeDB; P78795; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
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:P78795; -.
DR Proteomes; UP000002485; Chromosome II.
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:0001732; P:formation of cytoplasmic translation initiation complex; IC:PomBase.
DR CDD; cd12933; eIF3G; 1.
DR CDD; cd12408; RRM_eIF3G_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03006; eIF3g; 1.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR034240; eIF3G_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..282
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G"
FT /id="PRO_0000123513"
FT DOMAIN 202..280
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006,
FT ECO:0000269|PubMed:18257517"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006,
FT ECO:0000269|PubMed:18257517"
FT CONFLICT 79
FT /note="G -> R (in Ref. 2; BAA25105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 31494 MW; B05F7C0B6CABEE7D CRC64;
MSSSKSLDWA DDEDYGTGLP SIQTFDNPDG TKTMIEFRID DNGKKVKVTR VIRKTVITER
VQHAVAERKK WKKFGKEAGK NSGVDARTTS VGENVQLRLQ LGWTTTKEEE QDEAALAAAK
VKAKGSSVVR CRACKGNHFT AQCPYKSIIG PVDEPPLDAS PVSSRASGAL GEKGRYIAPH
LRAGSGRESG DSMFKRERDD SATLRVTNLS DDTREEELRD LFRRFGGIQR VYLAKDKETG
RAKGFAFVSY YDRDCAIKAR DRLDGYGWNN LILRCEFSKP RD
