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P33887 (IF2G_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:EIF2S3
Synonyms:EIF2G
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length152 AA.
Sequence statusFragments.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›152›152Eukaryotic translation initiation factor 2 subunit 3
PRO_0000137442

Regions

Nucleotide binding51 – 544GTP By similarity

Amino acid modifications

Modified residue11N-acetylalanine By similarity

Experimental info

Sequence uncertainty201
Sequence conflict31G → T AA sequence Ref.1
Sequence conflict1121Q → W AA sequence Ref.2
Non-adjacent residues22 – 232
Non-adjacent residues29 – 302
Non-adjacent residues41 – 422
Non-adjacent residues81 – 822
Non-adjacent residues101 – 1022
Non-adjacent residues137 – 1382
Non-terminal residue1521

Sequences

Sequence LengthMass (Da)Tools
P33887 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: CA56E544FA684CA7

FASTA15216,014
        10         20         30         40         50         60 
AGGEAGVTLG QPSLVEQDSH SGFKNELERD GGLLLIAGNE SKLKHILILG NKIDLVKESQ 

        70         80         90        100        110        120 
AKEQYGQILA FVQETVAXGA TVGQVLGAVG ALPEIFTELX IVNIGSLSTG GQVSAVKADL 

       130        140        150 
GKIVLTNPVX TEVGEEKSVE KHWRLIGWGQ IR 

« Hide

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

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR015256. TIF2_gsu_C.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PfamPF09173. eIF2_C. 1 hit.
[Graphical view]
SUPFAMSSF50465. SSF50465. 1 hit.
ProtoNetSearch...

Entry information

Entry nameIF2G_RABIT
AccessionPrimary (citable) accession number: P33887
Secondary accession number(s): Q9TRV8, Q9TRV9, Q9TRW0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 27, 2002
Last modified: April 16, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Translation initiation factors

List of translation initiation factor entries