P33887 (IF2G_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 56.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Eukaryotic translation initiation factor 2 subunit 3 Alternative name(s): Eukaryotic translation initiation factor 2 subunit gamma Short name=eIF-2-gamma | ||||
| Gene names |
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| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 152 AA. |
| Sequence status | Fragments. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. |
| Subunit structure | Heterotrimer composed of an alpha, a beta and a gamma chain. |
| Sequence similarities | Belongs to the GTP-binding elongation factor family. EIF2G subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Ligand | GTP-binding Nucleotide-binding |
| Molecular function | Initiation factor |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Molecular_function | GTP binding Non-traceable author statement Ref.2Ref.3Ref.1. Source: UniProtKB translation initiation factor activityNon-traceable author statement Ref.2Ref.3Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›152 | ›152 | Eukaryotic translation initiation factor 2 subunit 3 | PRO_0000137442 | |||||
Regions | |||||||||
| Nucleotide binding | 51 – 54 | 4 | GTP By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylalanine By similarity | ||||||
Experimental info | |||||||||
| Sequence uncertainty | 20 | 1 | |||||||
| Sequence conflict | 3 | 1 | G → T AA sequence Ref.1 | ||||||
| Sequence conflict | 112 | 1 | Q → W AA sequence Ref.2 | ||||||
| Non-adjacent residues | 22 – 23 | 2 | |||||||
| Non-adjacent residues | 29 – 30 | 2 | |||||||
| Non-adjacent residues | 41 – 42 | 2 | |||||||
| Non-adjacent residues | 81 – 82 | 2 | |||||||
| Non-adjacent residues | 101 – 102 | 2 | |||||||
| Non-adjacent residues | 137 – 138 | 2 | |||||||
| Non-terminal residue | 152 | 1 | |||||||
Sequences
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References
| [1] | "The NH2-terminal sequence of the alpha and gamma subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme-regulated eIF-2 alpha kinase." Wettenhall R.E.H., Kudlicki W., Kramer G., Hardesty B. J. Biol. Chem. 261:12444-12447(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-22. Tissue: Reticulocyte. |
| [2] | "Amino acid sequence analysis of the beta- and gamma-subunits of eukaryotic initiation factor eIF-2. Identification of regions interacting with GTP." Bommer U.-A., Kraft R., Kurzchalia T.V., Price N.T., Proud C.G. Biochim. Biophys. Acta 1079:308-315(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15 AND 82-126. Tissue: Reticulocyte. |
| [3] | "The purification and characterization of subunits alpha, beta, and gamma from the rabbit reticulocyte eukaryotic initiation factor 2." Schafer M.P., Fairwell T., Parker D.S., Knight M., Anderson W.F., Safer B. Arch. Biochem. Biophys. 255:337-346(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-8. Tissue: Reticulocyte. |
| [4] | "GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit of eIF-2 in Saccharomyces cerevisiae." Hannig E.M., Cigan A.M., Freeman B.A., Kinzy T.G. Mol. Cell. Biol. 13:506-520(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-99 AND 102-152. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR015256. TIF2_gsu_C. IPR009001. Transl_elong_EF1A/Init_IF2_C. [Graphical view] |
| Pfam | PF09173. eIF2_C. 1 hit. [Graphical view] |
| SUPFAM | SSF50465. Elong_init_C. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | IF2G_RABIT | ||||||||
| Accession | Primary (citable) accession number: P33887 Secondary accession number(s): Q9TRV8, Q9TRV9, Q9TRW0 | ||||||||
| Entry history |
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| 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 |

Clusters with
