Eukaryotic translation initiation factor 3 subunit F

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A5A6I3 (EIF3F_PANTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 41. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Pan troglodytes (Chimpanzee) [Reference proteome]

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

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 transcript 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 By similarity. 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 interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads 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.
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 sequence or structural similarity. Source: UniProtKB
Cellular_component	eukaryotic translation initiation factor 3 complex Inferred from sequence or structural similarity. 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

Removed By similarity

Chain

2 – 361

360

Eukaryotic translation initiation factor 3 subunit F HAMAP-Rule MF_03005

PRO_0000297557

Regions

Domain

91 – 200

110

MPN

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine; by CDK11; in vitro By similarity

Modified residue

242

N6-acetyllysine By similarity

Modified residue

262

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A5A6I3 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 35F35C9CE0C99C4E
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FASTA

361

37,918

        10         20         30         40         50         60 
MATPAVPVSA PPATPAPVPA AAPVSAPASV PAPTPAPAAA PVPAAAPASS SDPAAAAATT 

        70         80         90        100        110        120 
AAPGQTPASA QAPAQTPAPA LPGPALPGPF PGGRVVRLHP VILASIVDSY ERRNEGAARV 

       130        140        150        160        170        180 
IGTLLGTVDK HSVEVTNCFS VPHNESEDEV AVDMEFAKNM YELHKKVSPN ELILGWYATG 

       190        200        210        220        230        240 
HDITEHSVLI HEYYSREAPN PIHLTVDTSL QNGRMSIKAY 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

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References

[1]

"Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome."
Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I., Kusuda J., Gojobori T., Hashimoto K., Hirai M.
Gene 399:1-10(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cerebellum.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB222111 mRNA. Translation: BAF62356.1.
RefSeq	NP_001104282.1. NM_001110812.1.
UniGene	Ptr.2608.
3D structure databases
ProteinModelPortal	A5A6I3.
ModBase	Search...
Protein-protein interaction databases
STRING	9598.ENSPTRP00000005810.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	451007.
KEGG	ptr:451007.
Organism-specific databases
CTD	8665.
Phylogenomic databases
eggNOG	COG1310.
HOGENOM	HOG000241154.
HOVERGEN	HBG107843.
InParanoid	A5A6I3.
KO	K03249.
OrthoDB	EOG44XJHN.
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
NextBio	20833681.

Entry information

Entry name

EIF3F_PANTR

Accession

Primary (citable) accession number: A5A6I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	June 12, 2007
Last modified:	April 3, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Translation initiation factors

List of translation initiation factor entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents