ID   EIF3F_MOUSE             Reviewed;         361 AA.
AC   Q9DCH4; Q5XJV3;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 152.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit F {ECO:0000255|HAMAP-Rule:MF_03005};
DE            Short=eIF3f {ECO:0000255|HAMAP-Rule:MF_03005};
DE   AltName: Full=Deubiquitinating enzyme eIF3f;
DE            EC=3.4.19.12;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 5 {ECO:0000255|HAMAP-Rule:MF_03005};
DE   AltName: Full=eIF-3-epsilon {ECO:0000255|HAMAP-Rule:MF_03005};
DE   AltName: Full=eIF3 p47 {ECO:0000255|HAMAP-Rule:MF_03005};
GN   Name=Eif3f; Synonyms=Eif3s5;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   INTERACTION WITH EIF3B AND MTOR.
RX   PubMed=16541103; DOI=10.1038/sj.emboj.7601047;
RA   Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E.,
RA   Lawrence J.C. Jr.;
RT   "mTOR-dependent stimulation of the association of eIF4G and eIF3 by
RT   insulin.";
RL   EMBO J. 25:1659-1668(2006).
RN   [5]
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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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).
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_03005}.
CC   -!- FUNCTION: Deubiquitinates activated NOTCH1, promoting its nuclear
CC       import, thereby acting as a positive regulator of Notch signaling.
CC       {ECO:0000255|HAMAP-Rule:MF_03005, ECO:0000269|PubMed:17581632}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12;
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 RNF139; the
CC       interaction leads to protein translation inhibitions in a
CC       ubiquitination-dependent manner. Interacts with DTX1, the interaction
CC       is required for deubiquitinating activity towards NOTCH1 (By
CC       similarity). {ECO:0000255|HAMAP-Rule:MF_03005}.
CC   -!- INTERACTION:
CC       Q9DCH4; Q9JLN9: Mtor; NbExp=5; IntAct=EBI-1634316, EBI-1571628;
CC       Q9DCH4; Q86Y01: DTX1; Xeno; NbExp=9; IntAct=EBI-1634316, EBI-1755174;
CC       Q9DCH4; Q14152: EIF3A; Xeno; NbExp=4; IntAct=EBI-1634316, EBI-366617;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03005}.
CC   -!- DOMAIN: The MPN domain mediates deubiquitinating activity.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation is enhanced upon serum stimulation. Phosphorylated
CC       during apoptosis by caspase-processed CDK11 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit F family. {ECO:0000255|HAMAP-
CC       Rule:MF_03005}.
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DR   EMBL; AK002778; BAB22352.1; -; mRNA.
DR   EMBL; CH466531; EDL16920.1; -; Genomic_DNA.
DR   EMBL; BC083190; AAH83190.1; -; mRNA.
DR   CCDS; CCDS21731.1; -.
DR   RefSeq; NP_079620.2; NM_025344.2.
DR   AlphaFoldDB; Q9DCH4; -.
DR   SMR; Q9DCH4; -.
DR   BioGRID; 211203; 25.
DR   DIP; DIP-42766N; -.
DR   IntAct; Q9DCH4; 10.
DR   MINT; Q9DCH4; -.
DR   STRING; 10090.ENSMUSP00000033342; -.
DR   MEROPS; M67.974; -.
DR   GlyGen; Q9DCH4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9DCH4; -.
DR   PhosphoSitePlus; Q9DCH4; -.
DR   SwissPalm; Q9DCH4; -.
DR   EPD; Q9DCH4; -.
DR   jPOST; Q9DCH4; -.
DR   MaxQB; Q9DCH4; -.
DR   PaxDb; 10090-ENSMUSP00000033342; -.
DR   ProteomicsDB; 275736; -.
DR   Pumba; Q9DCH4; -.
DR   Antibodypedia; 11428; 273 antibodies from 31 providers.
DR   DNASU; 66085; -.
DR   Ensembl; ENSMUST00000033342.7; ENSMUSP00000033342.7; ENSMUSG00000031029.7.
DR   GeneID; 66085; -.
DR   KEGG; mmu:66085; -.
DR   UCSC; uc009jdc.2; mouse.
DR   AGR; MGI:1913335; -.
DR   CTD; 8665; -.
DR   MGI; MGI:1913335; Eif3f.
DR   VEuPathDB; HostDB:ENSMUSG00000031029; -.
DR   eggNOG; KOG2975; Eukaryota.
DR   GeneTree; ENSGT00950000183073; -.
DR   HOGENOM; CLU_027018_0_1_1; -.
DR   InParanoid; Q9DCH4; -.
DR   OMA; TVSPMLD; -.
DR   OrthoDB; 231037at2759; -.
DR   PhylomeDB; Q9DCH4; -.
DR   TreeFam; TF101517; -.
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; 66085; 29 hits in 80 CRISPR screens.
DR   ChiTaRS; Eif3f; mouse.
DR   PRO; PR:Q9DCH4; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9DCH4; Protein.
DR   Bgee; ENSMUSG00000031029; Expressed in paneth cell and 254 other cell types or 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; IDA:UniProtKB.
DR   GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISO:MGI.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:MGI.
DR   GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:MGI.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR   CDD; cd08064; MPN_eIF3f; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   HAMAP; MF_03005; eIF3f; 1.
DR   InterPro; IPR027531; eIF3f.
DR   InterPro; IPR024969; EIF3F/CSN6-like_C.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   PANTHER; PTHR10540:SF6; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT F; 1.
DR   PANTHER; PTHR10540; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT F-RELATED; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   Genevisible; Q9DCH4; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Hydrolase; Initiation factor; Phosphoprotein;
KW   Protease; Protein biosynthesis; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03005"
FT   CHAIN           2..361
FT                   /note="Eukaryotic translation initiation factor 3 subunit
FT                   F"
FT                   /id="PRO_0000213965"
FT   DOMAIN          96..226
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..89
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O00303, ECO:0000255|HAMAP-
FT                   Rule:MF_03005"
FT   MOD_RES         52
FT                   /note="Phosphoserine; by CDK11; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:O00303, ECO:0000255|HAMAP-
FT                   Rule:MF_03005"
FT   MOD_RES         242
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00303"
FT   MOD_RES         262
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00303, ECO:0000255|HAMAP-
FT                   Rule:MF_03005"
FT   CONFLICT        198
FT                   /note="A -> S (in Ref. 1; BAB22352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   361 AA;  37984 MW;  D0BE3309F9141E40 CRC64;
     MASPAVPANV PPATAAAAPA PVVTAAPASA PTPSTPAPTP AATPAASPAP VSSDPAVAAP
     AAPGQTPASA PAPAQTPAPS QPGPALPGPF PGGRVVRLHP VILASIVDSY ERRNEGAARV
     IGTLLGTVDK HSVEVTNCFS VPHNESEDEV AVDMEFAKNM YELHKKVSPN ELILGWYATG
     HDITEHSVLI HEYYSREAPN PIHLTVDTGL QHGRMSIKAY VSTLMGVPGR TMGVMFTPLT
     VKYAYYDTER IGVDLIMKTC FSPNRVIGLS SDLQQVGGAS ARIQDALSTV LQYAEDVLSG
     KVSADNTVGR FLMSLVNQVP KIVPDDFETM LNSNINDLLM VTYLANLTQS QIALNEKLVN
     L
//