EIF3C_DANRE
ID EIF3C_DANRE Reviewed; 926 AA.
AC Q6PFQ2;
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 subunit 8 {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=eif3c; Synonyms=eif3s8;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC eif3m. {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; BC057465; AAH57465.1; -; mRNA.
DR RefSeq; NP_998628.1; NM_213463.1.
DR AlphaFoldDB; Q6PFQ2; -.
DR SMR; Q6PFQ2; -.
DR STRING; 7955.ENSDARP00000111179; -.
DR PaxDb; Q6PFQ2; -.
DR GeneID; 334234; -.
DR KEGG; dre:334234; -.
DR CTD; 8663; -.
DR ZFIN; ZDB-GENE-030131-6166; eif3c.
DR eggNOG; KOG1076; Eukaryota.
DR InParanoid; Q6PFQ2; -.
DR PhylomeDB; Q6PFQ2; -.
DR Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DRE-72649; Translation initiation complex formation.
DR Reactome; R-DRE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DRE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DRE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DRE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q6PFQ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; ISS:UniProtKB.
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:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_03002; eIF3c; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027516; EIF3C.
DR InterPro; IPR008905; EIF3C_N_dom.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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 SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..926
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365377"
FT DOMAIN 672..848
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..244
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 106367 MW; 199924DE6CB9E545 CRC64;
MSRFFATGSD SESEESSSAD EITPKAAGTT LRQQALLLSD DEEDTKRVVR SAKDKRFEEL
TNLIKTIRNA IKIRGISKCL EEFEQLCRAF VKSKTIVDKE GVPKFYIRLL ADLEDYLNQL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFETEIASYK ENPEQSADEE EEKDDIGSGS
SESDDDDDDD ITAKSFMKKK PQEEEKKAPE ASKFLKGAAD EESESDDDED SEDWASDSVG
SDSESEDNDG TAASLAVVFL KKDVGEKASD RKKDDRRRRH KKKERIEEEA EEEGEAEEGG
WEKVKGGVPL VKEKPKMFAK GTEINTGVVV KKLSEILQAR GKKGTDRAAQ IELLHALAGI
AAENNLGEGI LVKIKFNIIA SLYDYNPNLA AFMKADMWKK CLDCIDELLD ILFNNNNIFI
GENIAEDSEN LAISDQPFRV RGCILTLVER MDEEFTKIMQ NTDPHSQEYV DNLKDEGRVC
GIIDRLLQYL ETKGSTEEVC RVYLRRIMHT YYKFDYKAHR RSLGLQGETK SEQDQEESEG
DDSAIIMDRL CKFIYAKDRT DRIRTCAILC HIYHHALHSR WYQARDLMLM SHLQDNIQHA
DPPVQILYNR TMVQLGICAF RQGMIKDAHN ALLDIQSSGR AKELLGQGLL MRNMQERNAE
QEKIEKRRQV PFHMHINLEL LECVYLVSAM LLEIPYMAAH EFDARRRMIS KQFHHQLRVG
ERQPLLGPPE SMREHVVAAS KAMKMGDWRT CHSFIINEKM NSKVWDLFPE AKCVREMLVR
KIQEESLRTY LFTYSSVYDS ISMETLSEMF ELELPTVHSI ISKMIINEEL MASLDQPTQT
VVMHRTEPTS LQNMALQLAE KLGGLVENNE RVFDLKQGVY GGYFNRDQKG GYQQKQGYQR
GDQKGGYQQK QNYQRGGYRN QNQSSY
