EIF3C_BOVIN
ID EIF3C_BOVIN Reviewed; 912 AA.
AC Q3SYW6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
DE AltName: Full=eIF3 p110 {ECO:0000255|HAMAP-Rule:MF_03002};
GN Name=EIF3C {ECO:0000255|HAMAP-Rule:MF_03002};
GN Synonyms=EIF3S8 {ECO:0000255|HAMAP-Rule:MF_03002};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis. The eIF-3 complex associates with the 40S
CC ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC required for disassembly and recycling of post-termination ribosomal
CC complexes and subsequently prevents premature joining of the 40S and
CC 60S ribosomal subunits prior to initiation. The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression.
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. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Identified in a HCV IRES-
CC mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3
CC and HCV RNA-replicon. Interacts with ALKBH4, IFIT1 and IFIT2 (By
CC similarity). Interacts with BZW2/5MP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03002}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {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; BC103352; AAI03353.1; -; mRNA.
DR RefSeq; NP_001029790.1; NM_001034618.2.
DR RefSeq; XP_005224985.1; XM_005224928.1.
DR AlphaFoldDB; Q3SYW6; -.
DR SMR; Q3SYW6; -.
DR STRING; 9913.ENSBTAP00000023384; -.
DR PaxDb; Q3SYW6; -.
DR PeptideAtlas; Q3SYW6; -.
DR PRIDE; Q3SYW6; -.
DR Ensembl; ENSBTAT00000023384; ENSBTAP00000023384; ENSBTAG00000006543.
DR GeneID; 534882; -.
DR KEGG; bta:534882; -.
DR CTD; 728689; -.
DR VEuPathDB; HostDB:ENSBTAG00000006543; -.
DR eggNOG; KOG1076; Eukaryota.
DR GeneTree; ENSGT00390000017900; -.
DR HOGENOM; CLU_004304_0_0_1; -.
DR InParanoid; Q3SYW6; -.
DR OMA; VVMHRSE; -.
DR OrthoDB; 273138at2759; -.
DR TreeFam; TF101520; -.
DR Reactome; R-BTA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000006543; Expressed in intramuscular adipose tissue and 110 other tissues.
DR ExpressionAtlas; Q3SYW6; baseline and differential.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
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; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_03002; eIF3c; 1.
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 PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..912
FT /note="Eukaryotic translation initiation factor 3 subunit
FT C"
FT /id="PRO_0000259423"
FT DOMAIN 672..848
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 99
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
FT MOD_RES 642
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1B4"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99613, ECO:0000255|HAMAP-
FT Rule:MF_03002"
SQ SEQUENCE 912 AA; 105366 MW; C082A25F4D78C67B CRC64;
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITNYK QNPEQSADED AEKNEEDSEG
SSDEDEDDDG VTAAAFLKKK SEAPSGDSRK FLKKEDEDED SEESEDSEAW DTSSTSSDSD
SEEEEGKQTV LASRFLKKAP TTEEDKKAAE KKREDKAKKK HDRKSRRPDE EEEDNEGGEW
ERVRGGVPLV KEKPKMFAKG TEITHAVVIK KLNEILQARG KKGTDRAAQI ELLQLLVQIA
SENNLGEGVI VKIKFNIIAS LYDYNPNLAT YMKPEMWQKC LDCINELMDI LFANPNIFVG
ENILEESENL HNADQPLRVR GCILTLVERM DEEFTKIMQN TDPHSQEYVE HLKDEAQVCA
IIERVQRYLE EKGTTEEVCR IYLRRILHTY YKFDYKAHQR QLTPPEGSSK SEQDQAENEG
EDSAVLMERL CKYIYAKDRT DRIRTCAILC HIYHHALHSR WYQARDLMLM SHLQDNIQHA
DPPVQILYNR TMVQLGICAF RQGLTKDAHN ALLDIQSSGR AKELLGQGLL LRSLQERNQE
QEKVERRRQV PFHLHINLEL LECVYLVSAM LLEIPYMAAH ESDARRRMIS KQFHHQLRVG
ERQPLLGPPE SMREHVVAAS KAMKMGDWKT CHSFIINEKM NGKVWDLFPE ADKVRTMLVR
KIQEESLRTY LFTYSSVYDS ISMETLSDMF ELDLPTVHSI ISKMIINEEL MASLDQPTQT
VVMHRTEPTA QQNLALQLAE KLGSLVENNE RVFDHKQGTY GGYFRDQKDG YRKNEGYMRR
GGYRQQQSQT AY
