Q9DCH4 (EIF3F_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 3 subunit F
Short name=eIF3f

Alternative name(s):
Deubiquitinating enzyme eIF3f
EC=3.4.19.12
Eukaryotic translation initiation factor 3 subunit 5
eIF-3-epsilon
eIF3 p47

Gene names

Name:	Eif3f
Synonyms:	Eif3s5

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	361 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. HAMAP-Rule MF_03005 Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling By similarity. HAMAP-Rule MF_03005
Catalytic activity	Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). HAMAP-Rule MF_03005
Subunit structure	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex may interact with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation may lead to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with DTX1, the interaction is required for deubiquitinating activity towards NOTCH1 By similarity. Ref.4 Ref.5
Subcellular location	Cytoplasm By similarity.
Domain	The MPN domain mediates deubiquitinating activity By similarity. HAMAP-Rule MF_03005
Post-translational modification	Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11 By similarity. HAMAP-Rule MF_03005
Sequence similarities	Belongs to the eIF-3 subunit F family. Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
Biological process	Protein biosynthesis Ubl conjugation pathway
Cellular component	Cytoplasm
Molecular function	Hydrolase Initiation factor Protease Thiol protease
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW translational initiation Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	eukaryotic translation initiation factor 3 complex Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	cysteine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW translation initiation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 361	360	Eukaryotic translation initiation factor 3 subunit F HAMAP-Rule MF_03005		PRO_0000213965
Regions
	Domain	91 – 200	110	MPN
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	52	1	Phosphoserine; by CDK11; in vitro By similarity
	Modified residue	242	1	N6-acetyllysine By similarity
	Modified residue	262	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	198	1	A → S in BAB22352. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9DCH4 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: D0BE3309F9141E40	FASTA	361	37,984
	10 20 30 40 50 60 MASPAVPANV PPATAAAAPA PVVTAAPASA PTPSTPAPTP AATPAASPAP VSSDPAVAAP 70 80 90 100 110 120 AAPGQTPASA PAPAQTPAPS QPGPALPGPF PGGRVVRLHP VILASIVDSY ERRNEGAARV 130 140 150 160 170 180 IGTLLGTVDK HSVEVTNCFS VPHNESEDEV AVDMEFAKNM YELHKKVSPN ELILGWYATG 190 200 210 220 230 240 HDITEHSVLI HEYYSREAPN PIHLTVDTGL QHGRMSIKAY VSTLMGVPGR TMGVMFTPLT 250 260 270 280 290 300 VKYAYYDTER IGVDLIMKTC FSPNRVIGLS SDLQQVGGAS ARIQDALSTV LQYAEDVLSG 310 320 330 340 350 360 KVSADNTVGR FLMSLVNQVP KIVPDDFETM LNSNINDLLM VTYLANLTQS QIALNEKLVN L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[2]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	"mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin." Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E., Lawrence J.C. Jr. EMBO J. 25:1659-1668(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EIF3B AND MTOR.
[5]	"Reconstitution reveals the functional core of mammalian eIF3." Masutani M., Sonenberg N., Yokoyama S., Imataka H. EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK002778 mRNA. Translation: BAB22352.1. CH466531 Genomic DNA. Translation: EDL16920.1. BC083190 mRNA. Translation: AAH83190.1.
IPI	IPI00120914.
RefSeq	NP_079620.2. NM_025344.2.
UniGene	Mm.182962.
3D structure databases
ProteinModelPortal	Q9DCH4.
SMR	Q9DCH4. Positions 96-297.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-42766N.
IntAct	Q9DCH4. 2 interactions.
MINT	MINT-1899046.
STRING	10090.ENSMUSP00000033342.
Protein family/group databases
MEROPS	M67.974.
PTM databases
PhosphoSite	Q9DCH4.
Proteomic databases
PaxDb	Q9DCH4.
PRIDE	Q9DCH4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000033342; ENSMUSP00000033342; ENSMUSG00000031029.
GeneID	66085.
KEGG	mmu:66085.
Organism-specific databases
CTD	8665.
MGI	MGI:1913335. Eif3f.
Phylogenomic databases
eggNOG	COG1310.
GeneTree	ENSGT00530000063075.
HOGENOM	HOG000241154.
HOVERGEN	HBG107843.
InParanoid	Q5XJV3.
KO	K03249.
OMA	HPVVLFQ.
OrthoDB	EOG44XJHN.
Gene expression databases
ArrayExpress	Q9DCH4.
Bgee	Q9DCH4.
Genevestigator	Q9DCH4.
GermOnline	ENSMUSG00000031029. Mus musculus.
Family and domain databases
HAMAP	MF_03005. eIF3f.
InterPro	IPR000555. JAB1_Mov34_MPN_PAD1. IPR024969. Rpn11/EIF3F_C. [Graphical view]
Pfam	PF01398. JAB. 1 hit. PF13012. MitMem_reg. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EIF3F. mouse.
NextBio	320584.
SOURCE	Search...

Entry information

Entry name

EIF3F_MOUSE

Accession

Primary (citable) accession number: Q9DCH4
Secondary accession number(s): Q5XJV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program