EIF3C_YEAS7
ID EIF3C_YEAS7 Reviewed; 812 AA.
AC A6ZN26;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
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 homolog {ECO:0000255|HAMAP-Rule:MF_03002};
DE Short=eIF3 p93 {ECO:0000255|HAMAP-Rule:MF_03002};
DE AltName: Full=Translation initiation factor eIF3, p93 subunit homolog {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=NIP1 {ECO:0000255|HAMAP-Rule:MF_03002}; ORFNames=SCY_4492;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000255|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; AAFW02000021; EDN64250.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZN26; -.
DR SMR; A6ZN26; -.
DR IntAct; A6ZN26; 2.
DR MINT; A6ZN26; -.
DR PRIDE; A6ZN26; -.
DR EnsemblFungi; EDN64250; EDN64250; SCY_4492.
DR HOGENOM; CLU_004304_0_2_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 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 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis.
FT CHAIN 1..812
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000366886"
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:0000250|UniProtKB:P32497, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32497, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32497, ECO:0000255|HAMAP-
FT Rule:MF_03002"
SQ SEQUENCE 812 AA; 93220 MW; 4F89A612358A8D42 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 AQYKSKFTSK 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
