EIF3C_XENLA
ID EIF3C_XENLA Reviewed; 926 AA.
AC Q4QR58;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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, 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; BC097542; AAH97542.1; -; mRNA.
DR RefSeq; NP_001129648.1; NM_001136176.1.
DR AlphaFoldDB; Q4QR58; -.
DR SMR; Q4QR58; -.
DR BioGRID; 932866; 2.
DR IntAct; Q4QR58; 1.
DR DNASU; 100191027; -.
DR GeneID; 100191027; -.
DR KEGG; xla:100191027; -.
DR CTD; 100191027; -.
DR Xenbase; XB-GENE-5720535; eif3c.L.
DR OrthoDB; 273138at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 100191027; Expressed in internal ear and 19 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; 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; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
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..926
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000365378"
FT DOMAIN 675..851
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 107004 MW; E6216C22DF2AFDDD CRC64;
MSRFFATGSD SESESSLSGD EILPKPVGGT FGKQPIILSD DEEDTKRVVR SAKDKRFEEL
TNLIKTIRNA MKIRDMTKCL EEFELLVKAF IKAKNIVDKE GVPRFYIRLL SDLDDYLNEL
WEDKEGKKKM NKNNAKALST LRQKLRKYNR DFEASITAYK QNPEESADED QEKDEDSEAS
SSSDDDSDEG MSASKFLKKA ESAPPESRSK FLKKEEAEDE AESSEDEDWG SDSDESDSDE
SDDENKHASM ASRFLKKTVT EGDRQAVEKK KEDKAKKKQH RKVKRKDEEG EEGEEDDNEG
GGEWEKVKGG VPLVKEKPKM FAKGTEITPP IVVKKLNEIL LARGKKGTDR AAQIELLQLL
AGIAEENNLG QGIAVKIKFN IMASLYDYNT NLATYMKSDM WKKCLDCIHD LLDILFANSN
MFIGEHIVED SENLSNLEQP LRVRGCILTL IERMEEEFTK IMQNTDPHSQ EYVDNLKDEA
RVCEVIERAQ KYLQEKGSTE EICRVYLRRI MHTYYKFDYK AHQRQLSTEQ ESKSEQDQAE
NEAEDSAILM DRLCKYIYAK DRTDRIRTCA ILCHIYHHAL HNRWFQARDL MLMSHLQDNI
QHADPPVQIL YNRTMVQLGI CAFRQGMIRD AHNALLDIQS SGRAKELLGQ GLLMRTMQER
NQEQEKIEKR RQIPFHMHIN LELLECVYLV SAMLLEIPYM AAHEFDARRR MISKQFHHQL
RVGERQPLLG PPESMREHVV AASKAMKMGD WKTCKNFIIN EKMNGKVWDL FPEAERVRGM
LVRKIQEESL RTYLFTYSSV YDSIRMGILG DMFQLEIPTV HSIISKMIIN EELMASLDQP
TQTVVMHGTE PSSLQNTALQ LAEKLGNLVE NNERIFDHKQ GSYGGYFNRG DRGDRGDRDQ
KDQYQRKEGG YMRRGYRRDQ QGQSNY
