ID L5MAX1_MYODS Unreviewed; 911 AA.
AC L5MAX1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit C {ECO:0000256|HAMAP-Rule:MF_03002};
DE Short=eIF3c {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 8 {ECO:0000256|HAMAP-Rule:MF_03002};
DE AltName: Full=eIF3 p110 {ECO:0000256|HAMAP-Rule:MF_03002};
GN Name=EIF3C {ECO:0000256|HAMAP-Rule:MF_03002};
GN Synonyms=EIF3S8 {ECO:0000256|HAMAP-Rule:MF_03002};
GN ORFNames=MDA_GLEAN10007335 {ECO:0000313|EMBL:ELK35430.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK35430.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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:0000256|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. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000256|HAMAP-Rule:MF_03002}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit C family. {ECO:0000256|HAMAP-
CC Rule:MF_03002}.
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DR EMBL; KB102349; ELK35430.1; -; Genomic_DNA.
DR RefSeq; XP_006756925.1; XM_006756862.2.
DR AlphaFoldDB; L5MAX1; -.
DR GeneID; 102760018; -.
DR KEGG; myd:102760018; -.
DR eggNOG; KOG1076; Eukaryota.
DR OrthoDB; 5482362at2759; -.
DR Proteomes; UP000010556; 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 Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; EUKARYOTIC TRANSLATION INITATION FACTOR 3, SUBUNIT 8 EIF3S8 -RELATED; 1.
DR PANTHER; PTHR13937:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT C-RELATED; 1.
DR Pfam; PF05470; eIF-3c_N; 1.
DR Pfam; PF01399; PCI; 1.
DR SMART; SM00088; PINT; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50250; PCI; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03002};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_03002};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_03002}; Reference proteome {ECO:0000313|Proteomes:UP000010556}.
FT DOMAIN 671..847
FT /note="PCI"
FT /evidence="ECO:0000259|PROSITE:PS50250"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..911
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..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03002"
SQ SEQUENCE 911 AA; 105238 MW; 870B96FE9D4BAF19 CRC64;
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL
WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITNYK QNPEQSADED AEKNEEDSEG
SSDGDEDGVS AAAFLKKKSE APSGESRKFL KKMEDEDEDS EDSEEDEEWD TGSTSSDSDS
EEEEGKQTVL ASRFLKKAPA TEEDKKAAEK KREDKAKKKH DRKSKRLDEE EEDNEGGEWE
RVRGGVPLVK EKPKMFAKGT EITHAVVIKK LNEILQARGK KGTDRASQIE LLQLLVQIAS
ENNLGEGVAI KIKFNIIASL YDYNPNLATY MKPEMWQKCL DCINELMDIL FANPNIFVGE
NILEESENLH NVDQPLRVRG CILTLVERMD EEFTKIMQNT DPHSQEYVEH LKDEAQVCAI
IERVQHYLEE KGTTEEICRV YLRRILHTYY KFDYKAHQRQ LTLPEGSSKS DQDQAENEGE
DSALLMERLC KYIYAKDRTD RIRTCAILCH IYHHALHSRW YQARDLMLMS HLQDNIQHAD
PPVQILYNRT MVQLGICAFR QGLTKDAHNA LLDIQSSGRA KELLGQGLLL RSLQERNQEQ
EKVERRRQVP FHLHINLELL ECVYVVSTML LEIPYMAAHE SDARRRMISK QFHHQLRVGE
RQPLLGPPES MREHVVAASK AMKMGDWKTC HSFIINEKMN GKVWDLFPEA DKVRTMLVRK
IQEESLRTYL FTYSSVYDSI SMETLSDMFE LDLPTVHSII SKMIINEELM ASLDQPTQTV
VMHRTEPTAQ QNLALQLAEK LGSLVENNER VFDHKQGTYG GYFRDQKDGY RKNEGYMRRG
GYRQQQSQTA Y
//
