IF4G_SCHPO
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 25-MAY-2022, entry version 145.
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; 13.
DR ELM; Q10475; -.
DR IntAct; Q10475; 2.
DR STRING; 4896.SPAC17C9.03.1; -.
DR iPTMnet; Q10475; -.
DR MaxQB; Q10475; -.
DR PaxDb; Q10475; -.
DR PRIDE; Q10475; -.
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; VEMELWE; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-166208; mTORC1-mediated signalling.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
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; ISO:PomBase.
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; ISO:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; TAS:PomBase.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:PomBase.
DR Gene3D; 1.20.970.30; -; 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; PTHR23253; 1.
DR Pfam; PF12152; eIF_4G1; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF101489; SSF101489; 1.
DR SUPFAM; SSF48371; SSF48371; 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
