EIF3C_YEAST
ID EIF3C_YEAST Reviewed; 812 AA.
AC P32497; D6W0D6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 93 kDa subunit;
DE Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Nuclear transport protein NIP1;
DE AltName: Full=Translation initiation factor eIF3, p93 subunit;
GN Name=NIP1 {ECO:0000255|HAMAP-Rule:MF_03002}; OrderedLocusNames=YMR309C;
GN ORFNames=YM9924.01C, YM9952.11C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=1332047; DOI=10.1073/pnas.89.21.10355;
RA Gu Z., Moerschell R.P., Sherman F., Goldfarb D.S.;
RT "NIP1, a gene required for nuclear transport in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10355-10359(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=7798228; DOI=10.1016/s0021-9258(18)31633-8;
RA Naranda T., MacMillan S.E., Hershey J.W.B.;
RT "Purified yeast translational initiation factor eIF-3 is an RNA-binding
RT protein complex that contains the PRT1 protein.";
RL J. Biol. Chem. 269:32286-32292(1994).
RN [5]
RP INTERACTION WITH PRT1, AND ASSOCIATION WITH 40S RIBOSOMES.
RX PubMed=9722586; DOI=10.1074/jbc.273.36.23485;
RA Greenberg J.R., Phan L., Gu Z., deSilva A., Apolito C., Sherman F.,
RA Hinnebusch A.G., Goldfarb D.S.;
RT "Nip1p associates with 40 S ribosomes and the Prt1p subunit of eukaryotic
RT initiation factor 3 and is required for efficient translation initiation.";
RL J. Biol. Chem. 273:23485-23494(1998).
RN [6]
RP IDENTIFICATION IN THE EIF-3 CORE COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND INTERACTION WITH TIF5 AND SUI1.
RX PubMed=9671501; DOI=10.1128/mcb.18.8.4935;
RA Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R.,
RA Qin J., Hinnebusch A.G.;
RT "Identification of a translation initiation factor 3 (eIF3) core complex,
RT conserved in yeast and mammals, that interacts with eIF5.";
RL Mol. Cell. Biol. 18:4935-4946(1998).
RN [7]
RP INTERACTION WITH TIF5.
RX PubMed=10075937; DOI=10.1093/emboj/18.6.1673;
RA Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.;
RT "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-
RT activating and GDP-GTP exchange factors in translation initiation, mediate
RT binding to their common substrate eIF2.";
RL EMBO J. 18:1673-1688(1999).
RN [8]
RP FUNCTION, ASSOCIATION WITH THE 40S RIBOSOME, AND INTERACTION WITH RPS0A.
RX PubMed=12651896; DOI=10.1101/gad.1065403;
RA Valasek L., Mathew A.A., Shin B.-S., Nielsen K.H., Szamecz B.,
RA Hinnebusch A.G.;
RT "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical
RT connections with the 40S ribosome in vivo.";
RL Genes Dev. 17:786-799(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP INTERACTION WITH PRT1, AND ASSOCIATION WITH THE 40S RIBOSOME.
RX PubMed=16581774; DOI=10.1128/mcb.26.8.2984-2998.2006;
RA Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.;
RT "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of
RT eukaryotic initiation factor 3 in yeast.";
RL Mol. Cell. Biol. 26:2984-2998(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP IDENTIFICATION IN THE EIF-3 COMPLEX WITH PRT1; TIF32; TIF34 AND TIF35.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-99 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC 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_03002, ECO:0000269|PubMed:12651896}.
CC -!- SUBUNIT: The eukaryotic translation initiation factor 3 (eIF-3) core
CC complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. A subcomplex
CC of TIF32, NIP1 and PRT1 mediates the interaction with eIF-1, TIF5/eIF-5
CC and HCR1. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. TIF32, NIP1 and TIF5/eIF-5 comprise a minimal 40S-ribosome-
CC binding unit. NIP1 interacts with TIF5/eIF-5 and SUI1.
CC {ECO:0000269|PubMed:10075937, ECO:0000269|PubMed:12651896,
CC ECO:0000269|PubMed:16581774, ECO:0000269|PubMed:18599441,
CC ECO:0000269|PubMed:7798228, ECO:0000269|PubMed:9671501,
CC ECO:0000269|PubMed:9722586}.
CC -!- INTERACTION:
CC P32497; P06103: PRT1; NbExp=12; IntAct=EBI-8965, EBI-8973;
CC P32497; P20433: RPB4; NbExp=5; IntAct=EBI-8965, EBI-15777;
CC P32497; P38249: RPG1; NbExp=13; IntAct=EBI-8965, EBI-8981;
CC P32497; P38431: TIF5; NbExp=5; IntAct=EBI-8965, EBI-9038;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002,
CC ECO:0000269|PubMed:1332047}. Note=Mainly cytoplasmic.
CC -!- MISCELLANEOUS: Present with 78900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; L02899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z54141; CAA90827.1; -; Genomic_DNA.
DR EMBL; Z49212; CAA89142.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10210.1; -; Genomic_DNA.
DR PIR; A46417; A46417.
DR RefSeq; NP_014040.1; NM_001182820.1.
DR PDB; 3JAP; EM; 4.90 A; p=193-812.
DR PDB; 4U1C; X-ray; 3.50 A; C=247-812.
DR PDB; 5H7U; NMR; -; A=36-163.
DR PDB; 6FYX; EM; 3.05 A; q=251-812.
DR PDB; 6FYY; EM; 3.05 A; q=251-812.
DR PDB; 6GSM; EM; 5.15 A; q=96-794.
DR PDB; 6GSN; EM; 5.75 A; q=96-794.
DR PDB; 6ZCE; EM; 5.30 A; q=1-812.
DR PDB; 6ZU9; EM; 6.20 A; q=1-812.
DR PDBsum; 3JAP; -.
DR PDBsum; 4U1C; -.
DR PDBsum; 5H7U; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P32497; -.
DR SMR; P32497; -.
DR BioGRID; 35489; 281.
DR ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR DIP; DIP-1470N; -.
DR IntAct; P32497; 63.
DR MINT; P32497; -.
DR STRING; 4932.YMR309C; -.
DR iPTMnet; P32497; -.
DR MaxQB; P32497; -.
DR PaxDb; P32497; -.
DR PRIDE; P32497; -.
DR EnsemblFungi; YMR309C_mRNA; YMR309C; YMR309C.
DR GeneID; 855357; -.
DR KEGG; sce:YMR309C; -.
DR SGD; S000004926; NIP1.
DR VEuPathDB; FungiDB:YMR309C; -.
DR eggNOG; KOG1076; Eukaryota.
DR GeneTree; ENSGT00390000017900; -.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; P32497; -.
DR OMA; VVMHRSE; -.
DR BioCyc; YEAST:G3O-32973-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:P32497; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32497; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:SGD.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR13937; PTHR13937; 1.
DR Pfam; PF05470; eIF-3c_N; 2.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..812
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000123530"
FT DOMAIN 608..783
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 111
FT /note="V -> D (in Ref. 1; L02899)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="Q -> H (in Ref. 1; L02899)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="K -> N (in Ref. 1; L02899)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="K -> N (in Ref. 1; L02899)"
FT /evidence="ECO:0000305"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5H7U"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:5H7U"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:5H7U"
FT TURN 126..132
FT /evidence="ECO:0007829|PDB:5H7U"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5H7U"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:5H7U"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5H7U"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:4U1C"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 289..306
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:4U1C"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 315..335
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 350..355
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 363..366
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 368..386
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 392..418
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 445..457
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 478..489
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 496..513
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 530..534
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 538..556
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 560..571
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 576..579
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 585..592
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 595..602
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 608..610
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 614..637
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 652..660
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 671..684
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 687..695
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 698..702
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 706..729
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:4U1C"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 738..745
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 749..763
FT /evidence="ECO:0007829|PDB:4U1C"
FT STRAND 768..770
FT /evidence="ECO:0007829|PDB:4U1C"
FT TURN 771..774
FT /evidence="ECO:0007829|PDB:4U1C"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:4U1C"
FT HELIX 784..793
FT /evidence="ECO:0007829|PDB:4U1C"
SQ SEQUENCE 812 AA; 93204 MW; EE05097C44C45A4C CRC64;
MSRFFSSNYE YDVASSSSEE DLLSSSEEDL LSSSSSESEL DQESDDSFFN ESESESEADV
DSDDSDAKPY GPDWFKKSEF RKQGGGSNKF LKSSNYDSSD EESDEEDGKK VVKSAKEKLL
DEMQDVYNKI SQAENSDDWL TISNEFDLIS RLLVRAQQQN WGTPNIFIKV VAQVEDAVNN
TQQADLKNKA VARAYNTTKQ RVKKVSRENE DSMAKFRNDP ESFDKEPTAD LDISANGFTI
SSSQGNDQAV QEDFFTRLQT IIDSRGKKTV NQQSLISTLE ELLTVAEKPY EFIMAYLTLI
PSRFDASANL SYQPIDQWKS SFNDISKLLS ILDQTIDTYQ VNEFADPIDF IEDEPKEDSD
GVKRILGSIF SFVERLDDEF MKSLLNIDPH SSDYLIRLRD EQSIYNLILR TQLYFEATLK
DEHDLERALT RPFVKRLDHI YYKSENLIKI METAAWNIIP AQFKSKFTSK DQLDSADYVD
NLIDGLSTIL SKQNNIAVQK RAILYNIYYT ALNKDFQTAK DMLLTSQVQT NINQFDSSLQ
ILFNRVVVQL GLSAFKLCLI EECHQILNDL LSSSHLREIL GQQSLHRISL NSSNNASADE
RARQCLPYHQ HINLDLIDVV FLTCSLLIEI PRMTAFYSGI KVKRIPYSPK SIRRSLEHYD
KLSFQGPPET LRDYVLFAAK SMQKGNWRDS VKYLREIKSW ALLPNMETVL NSLTERVQVE
SLKTYFFSFK RFYSSFSVAK LAELFDLPEN KVVEVLQSVI AELEIPAKLN DEKTIFVVEK
GDEITKLEEA MVKLNKEYKI AKERLNPPSN RR
