EIF3C_ASHGO
ID EIF3C_ASHGO Reviewed; 812 AA.
AC Q751S5;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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}; OrderedLocusNames=AGL344C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54147.1; -; Genomic_DNA.
DR RefSeq; NP_986323.1; NM_211385.1.
DR AlphaFoldDB; Q751S5; -.
DR SMR; Q751S5; -.
DR STRING; 33169.AAS54147; -.
DR EnsemblFungi; AAS54147; AAS54147; AGOS_AGL344C.
DR GeneID; 4622616; -.
DR KEGG; ago:AGOS_AGL344C; -.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_2_1; -.
DR InParanoid; Q751S5; -.
DR OMA; VVMHRSE; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR GO; GO:0071540; C:eukaryotic translation initiation factor 3 complex, eIF3e; IEA:EnsemblFungi.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:EnsemblFungi.
DR GO; GO:0043614; C:multi-eIF complex; IEA:EnsemblFungi.
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; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; Protein biosynthesis; Reference proteome.
FT CHAIN 1..812
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000364272"
FT DOMAIN 607..783
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..56
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 92489 MW; 946FB09482335025 CRC64;
MSRFFSRGYH YDTASSSEDE ELLTSSEEEL MSSSEEEVVS DDSFFNDSES ESAESDDDSD
GKPYGPDWFK KPQFRKGGAP GGSGASRFLK GNADSSDESD DEGKKVVKSA RDKLLDELNN
TYNKIDAAEM TQDWTTILSE FESATKLLVK AQQQNMGTPN VFVRVVAQVE DLVAETSQAE
IKNKIVAKAY NTVKQRVRKI ARENEELLAK FRQHPEAFEK DSTVEFGQAR DFDASDLTLM
GRKVADRSAI VSSPSDFFSA LRIVIDSRGK KGTDIQAQIK TMEELVSISK SPYESIIAYL
NLIPIRFDAC ANLAYQPLEQ WKASHNNVTS LLELLEANIE SYHVTELAPR NEFIEEEPQP
NENGVRMILG SVFTFVERLD DEFNKSLLNT DPHSSDYLDR LRDEQSVYNL ILRSQLYLEK
VLPEDTASKH LCRSFVRRLD HIYYKTSKLV DIVERAAWAS VPANSSSKYI TYSDDPDYNF
KLVNTLCTVV SSEQEMLKRR ATLYQIYYYA LNNQFSKAKE MLVQSNVRNS INSQDPTIQI
LFNRVVVQLG LAAFKLCLVE DCHQILNEVS TASHLRDIMG QQSLQRVSNN ISSNGTVTPT
EMLCLPFHQH INLDLIDAVF MTCSLLIEIP HMAAFYSGIK VKRIPYSQKS IRRALEHYEK
SSFQGPPETL RDHVIHAAKA MQRGNWAQCI NYLRSISTWT LLGDKMEKVL EQLAERIQIE
SLKTYIFTYK RFYTKLSVQK LSELFSLPTE QVISVIQTLE NTINIKGSLN EAKEMLIFDK
GDEITKLEEV AIKLTKETKY QSERLNNVSQ RQ
