EIF3L_MOUSE
ID EIF3L_MOUSE Reviewed; 564 AA.
AC Q8QZY1; Q3THF8; Q3TJ04; Q91YE4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
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=66 kDa tyrosine-rich heat shock protein;
DE AltName: Full=67 kDa polymerase-associated factor;
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};
DE AltName: Full=HSP-66Y;
DE AltName: Full=PAF67;
GN Name=Eif3l; Synonyms=Eif3eip, Eif3s6ip, Paf67;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seither P., Iben S., Thiry M., Grummt I.;
RT "Cloning and characterisation of PAF67, a novel protein that is associated
RT with RNA polymerase I.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Muramatsu H., Salama R., Zou K., Ikematsu S., Fan Q., Sakuma S.,
RA Muramatsu T.;
RT "A novel tyrosine-rich heat shock protein (HSP-66Y): molecular cloning and
RT characterization.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J;
RC TISSUE=Bone marrow, Kidney, Liver, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH RRN3.
RX PubMed=12393749; DOI=10.1093/embo-reports/kvf212;
RA Yuan X., Zhao J., Zentgraf H., Hoffmann-Rohrer U., Grummt I.;
RT "Multiple interactions between RNA polymerase I, TIF-IA and TAF(I) subunits
RT regulate preinitiation complex assembly at the ribosomal gene promoter.";
RL EMBO Rep. 3:1082-1087(2002).
RN [6]
RP FUNCTION, CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE
RP EIF-3 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-465, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(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:0000255|HAMAP-Rule:MF_03011, ECO:0000269|PubMed:17581632}.
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 may interact with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation may lead 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, ECO:0000269|PubMed:12393749,
CC ECO:0000269|PubMed:17581632}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ310346; CAC84554.1; -; mRNA.
DR EMBL; AB066095; BAB85122.1; -; Genomic_DNA.
DR EMBL; AK032936; BAC28090.1; -; mRNA.
DR EMBL; AK075584; BAC35837.1; -; mRNA.
DR EMBL; AK150895; BAE29941.1; -; mRNA.
DR EMBL; AK151175; BAE30177.1; -; mRNA.
DR EMBL; AK167640; BAE39691.1; -; mRNA.
DR EMBL; AK168009; BAE39996.1; -; mRNA.
DR EMBL; AK168295; BAE40238.1; -; mRNA.
DR EMBL; BC024463; AAH24463.1; -; mRNA.
DR CCDS; CCDS27632.1; -.
DR RefSeq; NP_660121.2; NM_145139.2.
DR AlphaFoldDB; Q8QZY1; -.
DR SMR; Q8QZY1; -.
DR BioGRID; 230176; 31.
DR IntAct; Q8QZY1; 4.
DR MINT; Q8QZY1; -.
DR STRING; 10090.ENSMUSP00000038839; -.
DR iPTMnet; Q8QZY1; -.
DR PhosphoSitePlus; Q8QZY1; -.
DR SwissPalm; Q8QZY1; -.
DR EPD; Q8QZY1; -.
DR jPOST; Q8QZY1; -.
DR MaxQB; Q8QZY1; -.
DR PaxDb; Q8QZY1; -.
DR PeptideAtlas; Q8QZY1; -.
DR PRIDE; Q8QZY1; -.
DR ProteomicsDB; 275655; -.
DR Antibodypedia; 221; 151 antibodies from 25 providers.
DR DNASU; 223691; -.
DR Ensembl; ENSMUST00000040518; ENSMUSP00000038839; ENSMUSG00000033047.
DR GeneID; 223691; -.
DR KEGG; mmu:223691; -.
DR UCSC; uc007wsk.1; mouse.
DR CTD; 51386; -.
DR MGI; MGI:2386251; Eif3l.
DR VEuPathDB; HostDB:ENSMUSG00000033047; -.
DR eggNOG; KOG3677; Eukaryota.
DR GeneTree; ENSGT00390000000411; -.
DR HOGENOM; CLU_029210_0_1_1; -.
DR InParanoid; Q8QZY1; -.
DR OMA; AGWFIRN; -.
DR OrthoDB; 393910at2759; -.
DR PhylomeDB; Q8QZY1; -.
DR TreeFam; TF101523; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 223691; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Eif3l; mouse.
DR PRO; PR:Q8QZY1; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8QZY1; protein.
DR Bgee; ENSMUSG00000033047; Expressed in 1st arch mandibular component and 262 other tissues.
DR ExpressionAtlas; Q8QZY1; baseline and differential.
DR Genevisible; Q8QZY1; MM.
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; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:MGI.
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 1: Evidence at protein 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_0000297498"
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:0007744|PubMed:23806337"
FT MOD_RES 549
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y262"
FT CONFLICT 149
FT /note="S -> P (in Ref. 3; BAE39691)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> F (in Ref. 1; CAC84554)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="P -> Q (in Ref. 3; BAE40238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 66613 MW; 914324CB5046763D CRC64;
MSYPADDYES EAAYDPYAYP GDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH
KTVSDLIDQK VYELQASRVS SDVIDQKVYE IQDIYENSWT KLTERFFKNT PWPEAEAIAP
QVGNDAVFLI LYKELYYRHI YAKVSGGPSL EQRFESYYNY CNLFNYILNA DGPAPLELPN
QWLWDIIDEF IYQFQSFSQY RCKTAKKSEG EMDFLRSNPK VWNVHSVLNV LHSLVDKSNI
NRQLEVYTSG GDPESVAGEY GRHSLYKMLG YFSLVGLLRL HSLLGDYYQA IKVLENIELN
KKSMYSRVPE CQVTTYYYVG FAYLMMRRYQ DAIRVFANIL LYIQRTKSMF QRTTYKYEMI
NKQNEQMHAL LAIALTMYPM RIDESIHLQL REKYGDKMLR MQKGDPQVYE ELFSYACPKF
LSPVVPNYDN VHPNYHKEPF LQQLKVFSDE VQQQAQLSTI RSFLKLYTTM PVAKLAGFLD
LTEQEFRIQL LVFKHKMKNL VWTSGISALD GEFQSASEVD FYIDKDMIHI ADTKVARRYG
DFFIRQIHKF EELNRTLKKM GQRP
