EIF3C_CAEEL
ID EIF3C_CAEEL Reviewed; 898 AA.
AC O02328;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 132.
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=T23D8.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; Z81128; CAB03403.1; -; Genomic_DNA.
DR PIR; T25167; T25167.
DR RefSeq; NP_492638.1; NM_060237.3.
DR AlphaFoldDB; O02328; -.
DR SMR; O02328; -.
DR BioGRID; 38280; 28.
DR IntAct; O02328; 4.
DR STRING; 6239.T23D8.4; -.
DR iPTMnet; O02328; -.
DR EPD; O02328; -.
DR PaxDb; O02328; -.
DR PeptideAtlas; O02328; -.
DR EnsemblMetazoa; T23D8.4.1; T23D8.4.1; WBGene00001226.
DR GeneID; 172858; -.
DR KEGG; cel:CELE_T23D8.4; -.
DR CTD; 172858; -.
DR WormBase; T23D8.4; CE18958; WBGene00001226; eif-3.C.
DR eggNOG; KOG1076; Eukaryota.
DR GeneTree; ENSGT00390000017900; -.
DR HOGENOM; CLU_004304_0_0_1; -.
DR InParanoid; O02328; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR PhylomeDB; O02328; -.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CEL-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; O02328; -.
DR PRO; PR:O02328; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001226; Expressed in adult organism and 4 other tissues.
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..898
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000123526"
FT DOMAIN 630..806
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 103843 MW; D8D36FBF89CD2FDA CRC64;
MSRFFHAKED SDSDTSSSED EVEDQKVNKS AKFRDDLDFM AGPEEDEKRV VRAQKDKKFD
ELKGIIKQNR DAKSNKDLNR LLTGFDSLAK AYDKSKTVFQ RQNVANPRFY IRSLVEIEDY
VNKLWDDKDA KSALSKNNAK ALPPLRQKLK KYIKDQQLQD LVTDYRVNPD EDGYETPEDE
DDDDFGEVSE SKAEKSPGKP SEKAAVSDSD SDSDDDDSSN WSSEPESNSS DDEDSVTKME
QLRRYFLKKE FRVESKDDKK EKKKRVIRVK EAVEEDDDAD WTPVNREKSV VHFDPKEEVT
HDVMIKKLNE VMSARGKRTT DRNQHVANLR KLLEVSEEKE LGLGINVKIS FCIISALFEL
NAKISDHMEY ETFMTTLQTV NSLLDLLIGT DRVKLSVTYA EEDENLKDDT QEYRIQGSIL
IAVQRLDGEL AKILQNADCH SNDYIEKLKA EKDMCSLIEK AEKYVELRND SGIFDKHEVC
KVYMMRIEHA YYKYQDQNEE DAGKLMDYLC NKIYTLDDEK RLRQRAMLCH VYYLAVHDKW
HRARDLLLMS HMQAIVDHSD VDTQILYNRT ICQLGLCAFR HGFIREAHQG LSEIQNTQRA
KELLAQAVGT RQHEKTAEQE KIDRSRQVPY HMHINVELME CVYLICSMLL EIPHMASCEF
EMRRRMLSRS FHYQLKQSEK ASLTGPPENT REHVVAASKA MLNGDWKKCQ DYIVNDKMNQ
KVWNLFHNAE TVKGMVVRRI QEESLRTYLL TYSTVYATVS LKKLADLFEL SKKDVHSIIS
KMIIQEELSA TLDEPTDCLI MHRVEPSRLQ MLALNLSDKL QTLAENNEQI LEPRTGRGGY
QGPGSWFPGR NERQGDKQKG SGGYQGERRG GQGQDGKRGN WGSQGGQQRR HPQKPRAF
