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Protein

Eukaryotic translation initiation factor 2 subunit 3

Gene

EIF2S3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi48 – 55GTPBy similarity8
Nucleotide bindingi134 – 138GTPBy similarity5
Nucleotide bindingi190 – 193GTPBy similarity4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-382556. ABC-family proteins mediated transport.
R-BTA-72649. Translation initiation complex formation.
R-BTA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-BTA-72702. Ribosomal scanning and start codon recognition.
R-BTA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-BTA-72731. Recycling of eIF2:GDP.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EIF2S3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome X

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00003160032 – 472Eukaryotic translation initiation factor 2 subunit 3Add BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei16PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ2KHU8.
PeptideAtlasiQ2KHU8.
PRIDEiQ2KHU8.

Expressioni

Gene expression databases

BgeeiENSBTAG00000014337.

Interactioni

Subunit structurei

Heterotrimer composed of an alpha subunit, also called subunit 1 (encoded by EIF2S1), a beta subunit, also called subunit 2 (encoded by EIF2S2) and a gamma subunit, also called subunit 3 (encoded EIF2S3).Curated

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019064.

Structurei

3D structure databases

ProteinModelPortaliQ2KHU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 248tr-type GPROSITE-ProRule annotationAdd BLAST210

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 55G1PROSITE-ProRule annotation8
Regioni76 – 80G2PROSITE-ProRule annotation5
Regioni134 – 137G3PROSITE-ProRule annotation4
Regioni190 – 193G4PROSITE-ProRule annotation4
Regioni225 – 227G5PROSITE-ProRule annotation3

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0466. Eukaryota.
COG5257. LUCA.
GeneTreeiENSGT00550000074801.
HOGENOMiHOG000229292.
HOVERGENiHBG006123.
InParanoidiQ2KHU8.
KOiK03242.
OMAiATFRMIS.
OrthoDBiEOG091G0624.
TreeFamiTF101513.

Family and domain databases

CDDicd15490. eIF2_gamma_III. 1 hit.
Gene3Di3.40.50.300. 2 hits.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR015256. TIF2_gsu_C.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PfamiPF09173. eIF2_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2KHU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGEAGVTL GQPHLSRQDL ATLDVSKLTP LSHEVISRQA TINIGTIGHV
60 70 80 90 100
AHGKSTVVKA ISGVHTVRFK NELERNITIK LGYANAKIYK LDDPSCPRPE
110 120 130 140 150
CYRSCGSSTP DEFPTDIPGT KGNFKLVRHV SFVDCPGHDI LMATMLNGAA
160 170 180 190 200
VMDAALLLIA GNESCPQPQT SEHLAAIEIM KLKHILILQN KIDLVKESQA
210 220 230 240 250
KEQYEQILAF VQGTVAEGAP IIPISAQLKY NIEVVCEYIV KKIPVPPRDF
260 270 280 290 300
TSEPRLIVIR SFDVNKPGCE VDDLKGGVAG GSILKGVLKV GQEIEVRPGI
310 320 330 340 350
VSKDSEGKLM CKPIFSKIVS LFAEHNDLQY AAPGGLIGVG TKIDPTLCRA
360 370 380 390 400
DRMVGQVLGA VGALPEIFTE LEISYFLLRR LLGVRTEGDK KAAKVQKLSK
410 420 430 440 450
NEVLMVNIGS LSTGGRVSAV KADLGKIVLT NPVCTEVGEK IALSRRVEKH
460 470
WRLIGWGQIR RGVTIKPTVD DD
Length:472
Mass (Da):51,065
Last modified:March 7, 2006 - v1
Checksum:i87DFA2A7CFED4DFA
GO

Sequence cautioni

The sequence ABQ12931 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti203Q → H in ABQ12931 (PubMed:16305752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112875 mRNA. Translation: AAI12876.1.
BT030491 mRNA. Translation: ABQ12931.1. Different initiation.
RefSeqiNP_001039582.1. NM_001046117.2.
UniGeneiBt.21351.

Genome annotation databases

EnsembliENSBTAT00000019064; ENSBTAP00000019064; ENSBTAG00000014337.
GeneIDi512350.
KEGGibta:512350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC112875 mRNA. Translation: AAI12876.1.
BT030491 mRNA. Translation: ABQ12931.1. Different initiation.
RefSeqiNP_001039582.1. NM_001046117.2.
UniGeneiBt.21351.

3D structure databases

ProteinModelPortaliQ2KHU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000019064.

Proteomic databases

PaxDbiQ2KHU8.
PeptideAtlasiQ2KHU8.
PRIDEiQ2KHU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000019064; ENSBTAP00000019064; ENSBTAG00000014337.
GeneIDi512350.
KEGGibta:512350.

Organism-specific databases

CTDi1968.

Phylogenomic databases

eggNOGiKOG0466. Eukaryota.
COG5257. LUCA.
GeneTreeiENSGT00550000074801.
HOGENOMiHOG000229292.
HOVERGENiHBG006123.
InParanoidiQ2KHU8.
KOiK03242.
OMAiATFRMIS.
OrthoDBiEOG091G0624.
TreeFamiTF101513.

Enzyme and pathway databases

ReactomeiR-BTA-382556. ABC-family proteins mediated transport.
R-BTA-72649. Translation initiation complex formation.
R-BTA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-BTA-72702. Ribosomal scanning and start codon recognition.
R-BTA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-BTA-72731. Recycling of eIF2:GDP.

Gene expression databases

BgeeiENSBTAG00000014337.

Family and domain databases

CDDicd15490. eIF2_gamma_III. 1 hit.
Gene3Di3.40.50.300. 2 hits.
InterProiIPR004161. EFTu-like_2.
IPR027417. P-loop_NTPase.
IPR000795. TF_GTP-bd_dom.
IPR015256. TIF2_gsu_C.
IPR009000. Transl_B-barrel.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
[Graphical view]
PfamiPF09173. eIF2_C. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF50465. SSF50465. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIF2G_BOVIN
AccessioniPrimary (citable) accession number: Q2KHU8
Secondary accession number(s): A5D972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: November 30, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.