EI2BE_RAT
ID EI2BE_RAT Reviewed; 716 AA.
AC Q64350; Q5RKL3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Translation initiation factor eIF-2B subunit epsilon;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit epsilon;
GN Name=Eif2b5; Synonyms=Eif2be;
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 [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=8688467; DOI=10.1016/0167-4781(96)00055-3;
RA Flowers K.M., Mellor H., Matts R.L., Kimball S.R., Jefferson L.S.;
RT "Cloning and characterization of complementary and genomic DNAs encoding
RT the epsilon-subunit of rat translation initiation factor-2B.";
RL Biochim. Biophys. Acta 1307:318-324(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-539.
RX PubMed=11311121; DOI=10.1042/bj3550609;
RA Woods Y.L., Cohen P., Becker W., Jakes R., Goedert M., Wang X., Proud C.G.;
RT "The kinase DYRK phosphorylates protein-synthesis initiation factor
RT eIF2Bepsilon at Ser539 and the microtubule-associated protein tau at
RT Thr212: potential role for DYRK as a glycogen synthase kinase 3-priming
RT kinase.";
RL Biochem. J. 355:609-615(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-535 AND SER-539, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP PHOSPHORYLATION AT SER-22; SER-125 AND THR-317, AND UBIQUITINATION AT
RP LYS-56; LYS-98; LYS-136; LYS-212 AND LYS-500 BY NEDD4.
RX PubMed=23707720; DOI=10.1016/j.bbrc.2013.05.053;
RA Tuckow A.P., Kazi A.A., Kimball S.R., Jefferson L.S.;
RT "Identification of ubiquitin-modified lysine residues and novel
RT phosphorylation sites on eukaryotic initiation factor 2B epsilon.";
RL Biochem. Biophys. Res. Commun. 436:41-46(2013).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon. Interacts with RGS2 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine and threonine residues by GSK3B;
CC phosphorylation inhibits its function (By similarity). Phosphorylated
CC at Ser-539 by DYRK2; this is required for subsequent phosphorylation by
CC GSK3B. {ECO:0000250, ECO:0000269|PubMed:11311121,
CC ECO:0000269|PubMed:23707720}.
CC -!- PTM: Polyubiquitinated, probably by NEDD4.
CC {ECO:0000269|PubMed:23707720}.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000305}.
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DR EMBL; U19516; AAB17690.1; -; mRNA.
DR EMBL; U19511; AAB17691.1; -; Genomic_DNA.
DR EMBL; BC085698; AAH85698.1; -; mRNA.
DR RefSeq; NP_620221.2; NM_138866.2.
DR AlphaFoldDB; Q64350; -.
DR SMR; Q64350; -.
DR BioGRID; 251366; 4.
DR IntAct; Q64350; 2.
DR STRING; 10116.ENSRNOP00000002321; -.
DR iPTMnet; Q64350; -.
DR PhosphoSitePlus; Q64350; -.
DR jPOST; Q64350; -.
DR PaxDb; Q64350; -.
DR PRIDE; Q64350; -.
DR Ensembl; ENSRNOT00000002321; ENSRNOP00000002321; ENSRNOG00000038160.
DR GeneID; 192234; -.
DR KEGG; rno:192234; -.
DR CTD; 8893; -.
DR RGD; 708380; Eif2b5.
DR eggNOG; KOG1461; Eukaryota.
DR GeneTree; ENSGT00510000047568; -.
DR HOGENOM; CLU_012507_2_0_1; -.
DR InParanoid; Q64350; -.
DR OMA; HYLYDKD; -.
DR OrthoDB; 369837at2759; -.
DR PhylomeDB; Q64350; -.
DR TreeFam; TF101509; -.
DR Reactome; R-RNO-72731; Recycling of eIF2:GDP.
DR PRO; PR:Q64350; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000038160; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; Q64350; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0031369; F:translation initiation factor binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0014002; P:astrocyte development; ISS:UniProtKB.
DR GO; GO:0048708; P:astrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IDA:RGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; 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:0010226; P:response to lithium ion; IEP:RGD.
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:0006413; P:translational initiation; ISS:UniProtKB.
DR CDD; cd04197; eIF-2B_epsilon_N; 1.
DR CDD; cd11558; W2_eIF2B_epsilon; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035543; eIF-2B_epsilon_N.
DR InterPro; IPR001451; Hexapep.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR InterPro; IPR003307; W2_domain.
DR InterPro; IPR044123; W2_eIF2B_epsilon.
DR Pfam; PF00132; Hexapep; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Initiation factor; Isopeptide bond; Methylation;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..716
FT /note="Translation initiation factor eIF-2B subunit
FT epsilon"
FT /id="PRO_0000156075"
FT DOMAIN 538..715
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHW4"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23707720"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23707720"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23707720"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT MOD_RES 464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 539
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:11311121,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13144"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23707720"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23707720"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23707720"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23707720"
FT CROSSLNK 500
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23707720"
FT CONFLICT 118
FT /note="I -> T (in Ref. 1; AAB17690/AAB17691)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="A -> S (in Ref. 1; AAB17690/AAB17691)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> T (in Ref. 1; AAB17690/AAB17691)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 80206 MW; 4C6E4C570C196CC0 CRC64;
MAATAAVPSA VGGRANKRGG GSGGGGTQGA EEEPPPPLQA VLVADSFDRR FFPISKDQPR
VLLPLANVAL IDYTLEFLTA TGVQETFVFC CWKAAQIKEH LQKSKWCHPT SLNVVRIITS
DLYRSLGDVL RDVDAKALVR SDFLLIYGDV VSNINISKAL EEHRLRRKLE KNVSVMTMVF
KESSPSHPTR CHEDNVVLAV DSTTNRILHF QKTQGLRHFS FPLGLFQGSL DGVEIRYDLL
DCHISICSPQ VAQLFTDNFD YQTRDDFVRG LLVNEEILGN QIHLHVTSRE YGARVSNLHM
YSAVCADVIR RWVYPLTPEV NFTDSSTQSY THSRHNIYRG PEVSLGHGSV LEENVLLGAG
TVVGSNCSIT NSVIGPNCHI GDNVVLDQAY LWQGVRVAAG AQIHQSLLCD RAEVKERVIL
KPHCVLTSQV VVGPDIILPE GSVISLHPPD AEEDEDDGQF SDDSGADQEK EKVKLKGYNP
AEVGPEGQGY LWKAEDVDEK EDEELRQSLW GLMINMEEES ETESERSVDP EELDSRAGSP
QLDDIRVFQN EVLGTLQRGR EENISCDNLV LEINSLKYAY NISLKEVMQV LSHVVLEFPL
QQVDGVLDPN RYCALLLPLL KAWSPVFRNY IKRAADHLEA LAAIEDFFLE HETLVPSLAK
VLMAFYQLEI LAEETILSWF SQRDITDKGQ QLRKNQQLQR FIQWLREAEE ESSDDD
