ID   IF4G_SCHPO              Reviewed;        1403 AA.
AC   Q10475; P78832;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma;
DE            Short=eIF-4-gamma;
DE            Short=eIF-4G;
GN   Name=tif471; ORFNames=SPAC17C9.03;
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, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12581158; DOI=10.1046/j.1365-2443.2003.00623.x;
RA   Hashemzadeh-Bonehi L., Curtis P.S., Morley S.J., Thorpe J.R., Pain V.M.;
RT   "Overproduction of a conserved domain of fission yeast and mammalian
RT   translation initiation factor eIF4G causes aberrant cell morphology and
RT   results in disruption of the localization of F-actin and the organization
RT   of microtubules.";
RL   Genes Cells 8:163-178(2003).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 865-1403.
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-452; SER-455;
RP   SER-456; SER-459; SER-866; SER-882; THR-884; SER-886; SER-911; SER-919;
RP   SER-921; TYR-923 AND SER-1333, AND 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 protein complex eIF4F, which is involved in
CC       the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC       secondary structure and recruitment of mRNA to the ribosome.
CC       {ECO:0000269|PubMed:12581158}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:12581158}. Note=Localized to the perinuclear
CC       region, the growing tips and septum.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAA97349.1; -; Genomic_DNA.
DR   EMBL; D89180; BAA13842.1; -; mRNA.
DR   PIR; T11583; T11583.
DR   PIR; T42624; T42624.
DR   RefSeq; NP_594602.1; NM_001020030.2.
DR   AlphaFoldDB; Q10475; -.
DR   SMR; Q10475; -.
DR   BioGRID; 278758; 14.
DR   ELM; Q10475; -.
DR   IntAct; Q10475; 2.
DR   STRING; 284812.Q10475; -.
DR   iPTMnet; Q10475; -.
DR   MaxQB; Q10475; -.
DR   PaxDb; 4896-SPAC17C9-03-1; -.
DR   EnsemblFungi; SPAC17C9.03.1; SPAC17C9.03.1:pep; SPAC17C9.03.
DR   GeneID; 2542290; -.
DR   KEGG; spo:SPAC17C9.03; -.
DR   PomBase; SPAC17C9.03; tif471.
DR   VEuPathDB; FungiDB:SPAC17C9.03; -.
DR   eggNOG; KOG0401; Eukaryota.
DR   HOGENOM; CLU_254179_0_0_1; -.
DR   InParanoid; Q10475; -.
DR   OMA; QFYSVIT; -.
DR   Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SPO-166208; mTORC1-mediated signalling.
DR   Reactome; R-SPO-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR   Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:Q10475; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; TAS:PomBase.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; TAS:PomBase.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:PomBase.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR   InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR   InterPro; IPR045208; IF4G.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4G1, ISOFORM B-RELATED; 1.
DR   Pfam; PF12152; eIF_4G1; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..1403
FT                   /note="Eukaryotic translation initiation factor 4 gamma"
FT                   /id="PRO_0000213333"
FT   DOMAIN          1009..1245
FT                   /note="MIF4G"
FT   REGION          1..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..774
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1266..1403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        717..738
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..753
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..774
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..889
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        969..983
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1003
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1266..1293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1299..1314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1381..1395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         459
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         866
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         882
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         884
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         886
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         911
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         919
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         921
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         923
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         1333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        1017
FT                   /note="N -> T (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1249
FT                   /note="K -> L (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1253
FT                   /note="E -> G (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1257
FT                   /note="K -> G (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1301
FT                   /note="N -> T (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1304
FT                   /note="F -> P (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1353
FT                   /note="S -> Y (in Ref. 3; BAA13842)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1403 AA;  154035 MW;  0317EE65BE2A1E63 CRC64;
     MSSKPPSNTP KFSYARALAS SQSNKSNSTK ASENNTATAE KQAVKPSGVE PTNTSRANAQ
     KKTESTGKIT SEADTEKYNS SKSPVNKEGS VEKKSSEKSS TNNKPWRGDN TSKPSANSSA
     ERTSSQHQKP ETSSQIGKDN AAPVENVNEK STSQETAPPV STVPIQFGSI TRNAAIPSKP
     KVSGNMQNKS GVSSYSSKSQ SVNSSVTSNP PHTEEPVAAK PEASSTATKG PRPTTSASNT
     NTSPANGAPT NKPSTDINTT DPATQTTQVS ASNSPALSGS STPSNTSSRS NRQNHGNFSE
     KRHYDRYGNS HPSYNKYSHY QHGFNYNNSG NNRNESGHPR FRNSRRNYNN QGAYPTYMSN
     GRSANQSPRN NPQNVNNGST PIQIPVSLQT PYGQVYGQPQ YIVDPNMVQY GPILQPGYVP
     QYYPVYHQTP YTQNFPNMSR SGSQVSDQVV ESPNSSTLSP RNGFAPIVKQ QKKSSALKIV
     NPVTHTEVVV PQKNASSPNP SETNSRAETP TAAPPQISEE EASQRKDAIK LAIQQRIQEK
     AEAEAKRKAE EKARLEAEEN AKREAEEQAK REAEEKAKRE AEEKAKREAE EKAKREAEEN
     AKREAEEKAK REAEEKAKRE AEEKAKREAE EKAKREAEEK AKREAEEKAK REAEEKAKRE
     AEENAKREAE EKAKREAEEN AKREAEEKVK RETEENAKRK AEEEGKREAD KNPEIKSSAP
     LASSEANVDT SKQTNATEPE VVDKTKVEKL KASEGKSTSS LSSPSHSTSS KRDLLSGLES
     LSLKTNPKSE QCLESLLNSQ FITDFSALVY PSTIKPPSTE EALKAGKYEY DVPFLLQFQS
     VYTDKPMKGW DERMKETVAS AFSDKSSRGM YSSSRQSSRS GSNTHSHAGP GFGGPSERKG
     ISRLGIDRGF SSSGAGFGSG SNYKSAPSRG VSHHGHGGMS GSHRGSQRGS RRGGGERDKP
     DPSSLTIPVD QVAPLQLSAN RWQPKKLTEK PAETKGEDEE ALLPPEVVQR KVKGSLNKMT
     LEKFDKISDQ ILEIAMQSRK ENDGRTLKQV IQLTFEKATD EPNFSNMYAR FARKMMDSID
     DSIRDEGVLD KNNQPVRGGL LFRKYLLSRC QEDFERGWKA NLPSGKAGEA EIMSDEYYVA
     AAIKRRGLGL VRFIGELFKL SMLSEKIMHE CIKRLLGNVT DPEEEEIESL CRLLMTVGVN
     IDATEKGHAA MDVYVLRMET ITKIPNLPSR IKFMLMDVMD SRKNGWAVKN EVEKGPKTIA
     EIHEEAERKK ALAESQRPSS GRMHGRDMNR GDSRMGGRGS NPPFSSSDWS NNKDGYARLG
     QGIRGLKSGT QGSHGPTSLS SMLKGGSVSR TPSRQNSALR REQSVRAPPS NVAVTSANSF
     ELLEEHDHDN DGGQKDSNSK TSS
//