ID   EI2BD_RAT               Reviewed;         524 AA.
AC   Q63186;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Translation initiation factor eIF-2B subunit delta;
DE   AltName: Full=eIF-2B GDP-GTP exchange factor subunit delta;
GN   Name=Eif2b4; Synonyms=Eif2bd;
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=Brain;
RX   PubMed=8929216; DOI=10.1042/bj3180637;
RA   Price N.T., Mellor H., Craddock B.L., Flowers K.M., Kimball S.R.,
RA   Wilmer T., Jefferson L.S., Proud C.G.;
RT   "eIF2B, the guanine nucleotide-exchange factor for eukaryotic initiation
RT   factor 2. Sequence conservation between the alpha, beta and delta subunits
RT   of eIF2B from mammals and yeast.";
RL   Biochem. J. 318:637-643(1996).
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.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC       {ECO:0000305}.
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DR   EMBL; Z48225; CAA88256.1; -; mRNA.
DR   PIR; S71961; S71961.
DR   RefSeq; NP_446402.1; NM_053950.1.
DR   AlphaFoldDB; Q63186; -.
DR   SMR; Q63186; -.
DR   IntAct; Q63186; 8.
DR   STRING; 10116.ENSRNOP00000007763; -.
DR   iPTMnet; Q63186; -.
DR   PhosphoSitePlus; Q63186; -.
DR   jPOST; Q63186; -.
DR   PRIDE; Q63186; -.
DR   Ensembl; ENSRNOT00000007763; ENSRNOP00000007763; ENSRNOG00000005301.
DR   GeneID; 117019; -.
DR   KEGG; rno:117019; -.
DR   CTD; 8890; -.
DR   RGD; 620208; Eif2b4.
DR   eggNOG; KOG1467; Eukaryota.
DR   GeneTree; ENSGT00550000075009; -.
DR   InParanoid; Q63186; -.
DR   OrthoDB; 797227at2759; -.
DR   Reactome; R-RNO-72731; Recycling of eIF2:GDP.
DR   PRO; PR:Q63186; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:RGD.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:RGD.
DR   GO; GO:0003743; F:translation initiation factor activity; NAS:UniProtKB.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:RGD.
DR   GO; GO:0021766; P:hippocampus development; IEP:RGD.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; IDA:RGD.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle 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:0006413; P:translational initiation; ISS:UniProtKB.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   CHAIN           2..524
FT                   /note="Translation initiation factor eIF-2B subunit delta"
FT                   /id="PRO_0000156070"
FT   REGION          1..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
FT   MOD_RES         86
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UI10"
SQ   SEQUENCE   524 AA;  57809 MW;  4B63F2AB10313924 CRC64;
     MAAVAVAVRE ESRSEMKTEL SPRPGAAGRE LTQEEKLQLR KEKKQQKKKR KEEKGADQEI
     GSAVSAAQRQ DPVRELQGTG SQLGGTTGEK LPAGRSKAEL RAERRAKQEA ERALKQARKG
     EQGGPSPQAC PSTAGEATSG VKRVPEHTQA DDPTLLRRLL RKPDRQQVPT RKDYGSKVSL
     FSHLPQYSRQ SSLTQYMSIP SSVIHPAMVR LGLQYSQGLV SGSNARCIAL LHALQQVIQD
     YTTPPNEELS RDLVNKLKPY ISFLTQCRPM SASMCNAIKF FNKEVTGMSS SKREEEAKSE
     LKEAIDRYVQ EKIVLASQAI SRFASKKISD GDVILVYGCS SLVSRILQEA WVEGRRFRVV
     VVDSRPRLEG RHMLHCLVRA GVPTSYLLIP AASYVLPEVS KVLLGAHALL ANGSVMSRVG
     TAQLALVARA HNVPVLVCCE TYKFCERVQT DAFVSNELDD PDDLQCKRGD QVTLANWQNN
     SSLRLLNLVY DVTPPELVDL VITELGMIPC SSVPVVLRVK SSDQ