EI2BD_MOUSE
ID EI2BD_MOUSE Reviewed; 524 AA.
AC Q61749; Q3TYW7; Q61748; Q8VC35;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
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=Eif2b, Eif2bd, Jgr1a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=CBA/J; TISSUE=Spleen;
RX PubMed=7982969; DOI=10.1016/s0021-9258(18)43844-6;
RA Henderson R.A., Krissansen G.W., Yong R.Y., Leung E., Watson J.D.,
RA Dholakia J.N.;
RT "The delta-subunit of murine guanine nucleotide exchange factor eIF-2B.
RT Characterization of cDNAs predicts isoforms differing at the amino-terminal
RT end.";
RL J. Biol. Chem. 269:30517-30523(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Salivary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61749-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61749-2; Sequence=VSP_001434;
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
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DR EMBL; M98036; AAA68047.1; -; mRNA.
DR EMBL; M98035; AAA68046.1; -; mRNA.
DR EMBL; AK158282; BAE34444.1; -; mRNA.
DR EMBL; CH466524; EDL37345.1; -; Genomic_DNA.
DR EMBL; BC021884; AAH21884.1; -; mRNA.
DR CCDS; CCDS19176.1; -. [Q61749-1]
DR CCDS; CCDS51457.1; -. [Q61749-2]
DR PIR; A55146; A55146.
DR RefSeq; NP_001120827.1; NM_001127355.1. [Q61749-2]
DR RefSeq; NP_001120828.1; NM_001127356.1. [Q61749-2]
DR RefSeq; NP_034252.2; NM_010122.2. [Q61749-1]
DR AlphaFoldDB; Q61749; -.
DR SMR; Q61749; -.
DR BioGRID; 199414; 6.
DR IntAct; Q61749; 2.
DR MINT; Q61749; -.
DR STRING; 10090.ENSMUSP00000110250; -.
DR iPTMnet; Q61749; -.
DR PhosphoSitePlus; Q61749; -.
DR EPD; Q61749; -.
DR jPOST; Q61749; -.
DR MaxQB; Q61749; -.
DR PaxDb; Q61749; -.
DR PRIDE; Q61749; -.
DR ProteomicsDB; 277839; -. [Q61749-1]
DR ProteomicsDB; 277840; -. [Q61749-2]
DR Antibodypedia; 47347; 199 antibodies from 32 providers.
DR Ensembl; ENSMUST00000077693; ENSMUSP00000076875; ENSMUSG00000029145. [Q61749-1]
DR Ensembl; ENSMUST00000114603; ENSMUSP00000110250; ENSMUSG00000029145. [Q61749-2]
DR Ensembl; ENSMUST00000166769; ENSMUSP00000130880; ENSMUSG00000029145. [Q61749-2]
DR GeneID; 13667; -.
DR KEGG; mmu:13667; -.
DR UCSC; uc008wxk.2; mouse. [Q61749-2]
DR UCSC; uc008wxl.2; mouse. [Q61749-1]
DR CTD; 8890; -.
DR MGI; MGI:95300; Eif2b4.
DR VEuPathDB; HostDB:ENSMUSG00000029145; -.
DR eggNOG; KOG1467; Eukaryota.
DR GeneTree; ENSGT00550000075009; -.
DR HOGENOM; CLU_016218_3_3_1; -.
DR InParanoid; Q61749; -.
DR OMA; YIDMVIT; -.
DR OrthoDB; 797227at2759; -.
DR TreeFam; TF101508; -.
DR Reactome; R-MMU-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 13667; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Eif2b4; mouse.
DR PRO; PR:Q61749; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q61749; protein.
DR Bgee; ENSMUSG00000029145; Expressed in primitive streak and 262 other tissues.
DR ExpressionAtlas; Q61749; baseline and differential.
DR Genevisible; Q61749; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; ISO:MGI.
DR GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0009408; P:response to heat; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; 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_0000156068"
FT REGION 1..155
FT /note="Disordered"
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 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"
FT VAR_SEQ 1..10
FT /note="MAAVAVAVRE -> MPTQQPAAPTSLPKSSRSLSGSLCALFSDA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:7982969"
FT /id="VSP_001434"
FT CONFLICT 302
FT /note="R -> K (in Ref. 1; AAA68046/AAA68047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 57624 MW; 86CDB70C63285A02 CRC64;
MAAVAVAVRE ESRSEMKTEL SPRPGAAGRE LTQEEKLQLR KEKKQQKKKR KEEKGADQEI
GSAVSAAQRQ DPIRELPGPG SQLGGTAGEK LPAGRSKAEL RAERRAKQEA ERALKQARKG
EQGGVPPQAC PSTAGETTSG VKRVPEHTPA DDPTLLRRLL RKPDRQQVPT RKDYGSKVSL
FSHLPQYSRQ SSLTQYMSIP SSVIHPAMVR LGLQYSQGLI SGSNARCIAL LHALQQVIQD
YTTPPSEELS RDLVNKLKPY ISFLTQCRPM SASMCNAIKF LTKEVTGMSS SKREEEAKSE
LREALDRYVQ EKIVLAAQAI SRFASTKISD GDVILVYGCS SLVSRILQEA RVEGRRFRVV
VVDSRPRLEG RHMLHSLVRA GVPTSYLLIP AASYVLPEVS KVLLGAHALL ANGSVMSRVG
TAQLALVARA HNVPVLVCCE TYKFCERVQT DAFVSNELDD PDDLQCKRGD QVALANWQSH
PSLRLLNLVY DVTPPELVDL VITELGMIPC SSVPVVLRVK SSDQ
