ID   EIF3C_BOMMO             Reviewed;         876 AA.
AC   Q0ZB76;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=eIF3-S8 {ECO:0000255|HAMAP-Rule:MF_03002};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang L.-L., Chen K.-P., Yao Q., Hu Z.-G., Chen H.-Q.;
RT   "Translation initiation factors in Bombyx mori.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ645460; ABG54288.1; -; mRNA.
DR   RefSeq; NP_001037658.1; NM_001044193.1.
DR   STRING; 7091.BGIBMGA012851-TA; -.
DR   PRIDE; Q0ZB76; -.
DR   GeneID; 733086; -.
DR   KEGG; bmor:733086; -.
DR   CTD; 8663; -.
DR   eggNOG; KOG1076; Eukaryota.
DR   HOGENOM; CLU_004304_0_0_1; -.
DR   InParanoid; Q0ZB76; -.
DR   OrthoDB; 273138at2759; -.
DR   Proteomes; UP000005204; 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   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   2: Evidence at transcript level;
KW   Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..876
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   C"
FT                   /id="PRO_0000365383"
FT   DOMAIN          632..808
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..876
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  101570 MW;  B11C533B6CDFD9DF CRC64;
     MSRFFATGTD SESESSSEDE PVVRAPAPVY TFSDDEEETK RVVRSMKEKR YEELEGIIHS
     IRNHRKIKDF SSALASFEEL QKAYTRAAPV VQKEENGVAP RFFIRALVEL DDWVVGAWNE
     REARKALSKG NSKALTSLRQ KLRKYTKDFE AEISXFREDP DLPDDNERKD SSSSDESEDE
     EKPIKEKPKP EPLLRPPPED DESSDSMDWA SSSSDSSFSS DDEERGTSNI REQFIKKVTK
     KEDDEEKIKL KLKKREERRE RSGKINKRDV ADDGGEWETV RKGAATSDKP KMFAKDSDID
     AALVVKKLGE ISAARGRKRT DRRAQLELLH ELRTVALQHN LGDALQLKLR SAIVAALFDY
     NPKVSDAMKP EYWSKLVENI DHMVTLLLAH EDMVLSETIL EENEQLVTPP YQVRGCLLTY
     LERLDDEFTK LLKECDPHSN EYVERLKDEV RVSALIDRVC QVVERDGTPQ EICRAYLRKI
     DHLYYKFDPR AVRKDLPPTE ETTIKKMERY CKYIYAHDET DRLRTRAILS HIYHHALHDN
     WFQARDLLLM SHLQETVQHS DPSTQILYNR TMANLGLCAF RRGNVKEAHG CLAELMMTGK
     PKELLAQGLL PQRQHERSKE QEKIEKQRQM PFHMHINLEL LECVYLVSAM LIEIPYMAAH
     EFDARRRMIS KTFYQNLRAS ERQALVGPPE SMREHAVAAA RAMRRGDWRA CLNYIVNEKM
     NAKVWDLMVG ADNVRAMLGR LIREESLRTY LFTYAHVYAS LSLRSLADMF ELPRQRVHSL
     VSKMIINEEL LASLDDPSEC AILHRSEPTR MQALALQLAD KVGNLVDSNE RIFEKQGSFF
     QRGGAQRGEG RQRERPREGW NRRTRNRRRD DERADD