ID EI2BG_RAT Reviewed; 452 AA.
AC P70541; Q6IN08;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Translation initiation factor eIF2B subunit gamma;
DE AltName: Full=eIF2B GDP-GTP exchange factor subunit gamma;
GN Name=Eif2b3; Synonyms=Eif2bg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX PubMed=8809057; DOI=10.1042/bj3180631;
RA Price N.T., Kimball S.R., Jefferson L.S., Proud C.G.;
RT "Cloning of cDNA for the gamma-subunit of mammalian translation initiation
RT factor 2B, the guanine nucleotide-exchange factor for eukaryotic initiation
RT factor 2.";
RL Biochem. J. 318:631-636(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acts as a component of the translation initiation factor 2B
CC (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the
CC eukaryotic initiation factor 2 (eIF2) complex gamma subunit. Its
CC guanine nucleotide exchange factor activity is repressed when bound to
CC eIF2 complex phosphorylated on the alpha subunit, thereby limiting the
CC amount of methionyl-initiator methionine tRNA available to the ribosome
CC and consequently global translation is repressed.
CC {ECO:0000250|UniProtKB:Q9NR50}.
CC -!- ACTIVITY REGULATION: Activated by the chemical integrated stress
CC response (ISR) inhibitor ISRIB which stimulates guanine nucleotide
CC exchange factor activity for both phosphorylated and unphosphorylated
CC eIF2. {ECO:0000250|UniProtKB:Q9NR50}.
CC -!- SUBUNIT: Component of the translation initiation factor 2B (eIF2B)
CC complex which is a heterodecamer of two sets of five different
CC subunits: alpha, beta, gamma, delta and epsilon. Subunits alpha, beta
CC and delta comprise a regulatory subcomplex and subunits epsilon and
CC gamma comprise a catalytic subcomplex. Within the complex, the
CC hexameric regulatory complex resides at the center, with the two
CC heterodimeric catalytic subcomplexes bound on opposite sides.
CC {ECO:0000250|UniProtKB:Q9NR50}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P56288}.
CC -!- TISSUE SPECIFICITY: Brain, heart, liver, muscle and testis.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000305}.
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DR EMBL; U38253; AAC52788.1; -; mRNA.
DR EMBL; BC072507; AAH72507.1; -; mRNA.
DR PIR; S72266; S72266.
DR RefSeq; NP_598293.2; NM_133609.2.
DR RefSeq; XP_006238692.1; XM_006238630.3.
DR AlphaFoldDB; P70541; -.
DR SMR; P70541; -.
DR BioGRID; 251149; 1.
DR STRING; 10116.ENSRNOP00000024841; -.
DR PhosphoSitePlus; P70541; -.
DR jPOST; P70541; -.
DR PaxDb; 10116-ENSRNOP00000024841; -.
DR Ensembl; ENSRNOT00000097401.1; ENSRNOP00000088850.1; ENSRNOG00000018375.8.
DR Ensembl; ENSRNOT00055021407; ENSRNOP00055017322; ENSRNOG00055012550.
DR Ensembl; ENSRNOT00060051387; ENSRNOP00060042746; ENSRNOG00060029501.
DR Ensembl; ENSRNOT00065028288; ENSRNOP00065022356; ENSRNOG00065016905.
DR GeneID; 171145; -.
DR KEGG; rno:171145; -.
DR UCSC; RGD:620821; rat.
DR AGR; RGD:620821; -.
DR CTD; 8891; -.
DR RGD; 620821; Eif2b3.
DR eggNOG; KOG1462; Eukaryota.
DR GeneTree; ENSGT00510000047486; -.
DR HOGENOM; CLU_016743_0_0_1; -.
DR InParanoid; P70541; -.
DR OrthoDB; 161736at2759; -.
DR PhylomeDB; P70541; -.
DR Reactome; R-RNO-72731; Recycling of eIF2:GDP.
DR PRO; PR:P70541; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000018375; Expressed in ovary and 20 other cell types or tissues.
DR Genevisible; P70541; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:RGD.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:RGD.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0002183; P:cytoplasmic translational initiation; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR GO; GO:0009408; P:response to heat; IDA:UniProtKB.
DR GO; GO:0043434; P:response to peptide hormone; IDA:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:RGD.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR CDD; cd04198; eIF-2B_gamma_N; 1.
DR CDD; cd04652; LbH_eIF2B_gamma_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR45989; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR PANTHER; PTHR45989:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT GAMMA; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..452
FT /note="Translation initiation factor eIF2B subunit gamma"
FT /id="PRO_0000156080"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR50"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR50"
FT CONFLICT 399
FT /note="E -> G (in Ref. 1; AAC52788)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="C -> F (in Ref. 1; AAC52788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50435 MW; BA33492D1700BE4F CRC64;
MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTKDVQ
KALCAEFKMK LKPDIVCIPD EADMGTADSL RHIYPKLKTD VLVLGCDLIT DVALHEVVDL
FRAYDASLAM LMRKGQESTE PVPGQKGKKK TVEQRDFIGV DSTGKRLLFM ANEADLDEEL
VIKGSILQKH PRIHFQTGLV DAHLYCLKKY VVDFLMENKS ITSIRSELIP YLVRKQFSSA
SSQQRQEDKE EDLKKKEPKS LDIYSFIKKD NTLTLAPYDA CWNAFRRDKW EDLSRSQVRC
YVHIMKEGLC SRVSTLGLYM EANRQVPKLL SVLCPEESMI HPSAQIANKH LIGADSLIGS
DTQVGEKSSI KRSVIGSSCV IRDRVTVTNC LLMNSVTVEE GSSIHGSVIC NNAVVEAGAE
IRDCLIGSGQ RIEAKAKRMN EVIVGNDQLM EI
//
