EIF3L_BOVIN
ID EIF3L_BOVIN Reviewed; 564 AA.
AC Q3ZCK1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit L {ECO:0000255|HAMAP-Rule:MF_03011};
DE Short=eIF3l {ECO:0000255|HAMAP-Rule:MF_03011};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 6-interacting protein {ECO:0000255|HAMAP-Rule:MF_03011};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit E-interacting protein {ECO:0000255|HAMAP-Rule:MF_03011};
GN Name=EIF3L {ECO:0000255|HAMAP-Rule:MF_03011};
GN Synonyms=EIF3EIP {ECO:0000255|HAMAP-Rule:MF_03011},
GN EIF3S6IP {ECO:0000255|HAMAP-Rule:MF_03011};
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_03011}.
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. Interacts with RRN3.
CC {ECO:0000255|HAMAP-Rule:MF_03011}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03011}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit L family. {ECO:0000255|HAMAP-
CC Rule:MF_03011}.
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DR EMBL; BC102112; AAI02113.1; -; mRNA.
DR RefSeq; NP_001030373.1; NM_001035296.2.
DR AlphaFoldDB; Q3ZCK1; -.
DR SMR; Q3ZCK1; -.
DR STRING; 9913.ENSBTAP00000014281; -.
DR PaxDb; Q3ZCK1; -.
DR PeptideAtlas; Q3ZCK1; -.
DR PRIDE; Q3ZCK1; -.
DR Ensembl; ENSBTAT00000014281; ENSBTAP00000014281; ENSBTAG00000010790.
DR GeneID; 514449; -.
DR KEGG; bta:514449; -.
DR CTD; 51386; -.
DR VEuPathDB; HostDB:ENSBTAG00000010790; -.
DR VGNC; VGNC:28402; EIF3L.
DR eggNOG; KOG3677; Eukaryota.
DR GeneTree; ENSGT00390000000411; -.
DR HOGENOM; CLU_029210_0_1_1; -.
DR InParanoid; Q3ZCK1; -.
DR OMA; AGWFIRN; -.
DR OrthoDB; 393910at2759; -.
DR TreeFam; TF101523; -.
DR Reactome; R-BTA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000010790; Expressed in myometrium and 106 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:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IEA:Ensembl.
DR HAMAP; MF_03011; eIF3l; 1.
DR InterPro; IPR019382; eIF3l.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13242; PTHR13242; 1.
DR Pfam; PF10255; Paf67; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50250; PCI; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03011"
FT CHAIN 2..564
FT /note="Eukaryotic translation initiation factor 3 subunit
FT L"
FT /id="PRO_0000297493"
FT DOMAIN 331..537
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y262, ECO:0000255|HAMAP-
FT Rule:MF_03011"
FT MOD_RES 465
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y262"
FT MOD_RES 549
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y262"
SQ SEQUENCE 564 AA; 66727 MW; C43BD17143D42E3C CRC64;
MSYPADDYES EAAYDPYAYP GDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH
KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT KLTERFFKNT PWPEAETIAP
QVGNDAVFLI LYKELYYRHI YAKVSGGPSL EQRFESYYNY CNLFNYILNA DGPAPLELPN
QWLWDIIDEF IYQFQSFSQY RCKTAKKSEE EIDFLRSNPK IWNVHSVLNV LHSLVDKSNI
NRQLEVYTSG GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF QRTTYKYEMI
NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR MQKGDPQVYE ELFSYSCPKF
LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD
LTEQEFRIQL LVFKHKMKNL VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG
DFFIRQIHKF EELNRTLKKM GQRP
