EIF3C_CAEBR
ID EIF3C_CAEBR Reviewed; 894 AA.
AC A8WWU0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=eif-3.C {ECO:0000255|HAMAP-Rule:MF_03002}; ORFNames=CBG03821;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE600906; CAP24647.1; -; Genomic_DNA.
DR RefSeq; XP_002639260.1; XM_002639214.1.
DR AlphaFoldDB; A8WWU0; -.
DR SMR; A8WWU0; -.
DR STRING; 6238.CBG03821; -.
DR PRIDE; A8WWU0; -.
DR EnsemblMetazoa; CBG03821.1; CBG03821.1; WBGene00026601.
DR GeneID; 8581254; -.
DR KEGG; cbr:CBG_03821; -.
DR CTD; 8581254; -.
DR WormBase; CBG03821; CBP01111; WBGene00026601; Cbr-eif-3.C.
DR eggNOG; KOG1076; Eukaryota.
DR HOGENOM; CLU_004304_0_0_1; -.
DR InParanoid; A8WWU0; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000008549; Chromosome I.
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: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 InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13937; PTHR13937; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..894
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365380"
FT DOMAIN 625..801
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 103744 MW; 60B7059B1FF3A3E6 CRC64;
MSRFYRRGAS DSDTDSSEDE VEELKANKSA KFRDDLDFMA GPEEDEKRVV RAQKDKKFDE
LKSLIKQNRD AKSNKDLNKL LTGFDTLAKA YDKSKTIFQR QNVTNPRFYI RFLVEIEDYV
NKLWEDKEAK AALSKNNTKA LSPLRQKLKK YIKDHGLTDL VSDYRANPDE DGYETPEDEN
DEDDFEEVPE ASPGRQAERA ADSESESDSD DDDSFNWSSE PDTNSSDDEE NVTKMEQLRR
YFLKKEFREE SKDDKKDKRK RVIKVKEVVE EDDDDWTPVS REKSVVHFDP NEEVTHDVMI
KKLNEVMSAR GKRTTDRNQH VANLQKLLEV AEEKQLGLGI SVKISFCIIS ALFELNAKIS
DYMEYETFMN TLRTVNTLLD LLITTDRVKL SVTYAEEDEN LKDENEEYRI QGSILIAVQR
LDGELAKILQ NADCHSNDYI EKLKAEKDMC QLIEKAENYV ELRNHLGIFD KHEVCKVYMM
RIEHTYYKYQ DQNVGEVAKT MDYLCNKIYT LDDEKRLRQR AMLCHVYFLA VHDKWHRARD
LLLMSHMQAI VDHSDVDTQI LYNRTICQLG LCAFRHGFIR EAHQGLSEIQ NTQRAKELLA
QAVGTRPHEK TAEQEKIDRS RQVPYHMHIN VELMECVYLI CSMLLEIPHM ASCEFEMRRR
MLSRSFHYQL KQSEKASLTG PPENTREHVV AASKAMLNGD WKKCKDYIVN EKMNQKVWNL
FHNADQVKDM VVRRIQEESL RTYLLTYSTV YSTVSLKKLA SLFDLSKKDV HSIISKMIIQ
EELSATLDEP TDCLIMHRVE PSRLQMLALN LSDKLQTLAE NNEQILEPRT GRGGYQGPGS
WFPGRNERQG DKQKGSGGFQ GERRGGPGGP DGKRGNWGSQ GGQQRRHPQK PRAF
