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Elongation factor 1-delta (EF-1-delta)

 EF1D_RAT                Reviewed;         281 AA.
Q68FR9;
01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-SEP-2009, sequence version 2.
23-MAY-2018, entry version 98.
RecName: Full=Elongation factor 1-delta;
Short=EF-1-delta;
Name=Eef1d;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-133; THR-147
AND SER-162, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Isoform 1: EF-1-beta and EF-1-delta stimulate the
exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-
alpha for another round of transfer of aminoacyl-tRNAs to the
ribosome. {ECO:0000250}.
-!- FUNCTION: Isoform 2: Regulates induction of heat-shock-responsive
genes through association with heat shock transcription factors
and direct DNA-binding at heat shock promoter elements (HSE).
{ECO:0000250}.
-!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta
isoform 1, and gamma. Isoform 2 interacts with HSF1 and NFE2L2 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q68FR9-1; Sequence=Displayed;
Name=2; Synonyms=eEF1BdeltaL;
IsoId=Q68FR9-2; Sequence=VSP_037887;
-!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
{ECO:0000305}.
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EMBL; CH473950; EDM16037.1; -; Genomic_DNA.
EMBL; BC079391; AAH79391.1; -; mRNA.
RefSeq; NP_001013122.1; NM_001013104.1. [Q68FR9-2]
RefSeq; XP_008763779.1; XM_008765557.1. [Q68FR9-1]
RefSeq; XP_008763780.1; XM_008765558.1. [Q68FR9-1]
RefSeq; XP_008763781.1; XM_008765559.1. [Q68FR9-1]
UniGene; Rn.71883; -.
SMR; Q68FR9; -.
BioGrid; 256417; 1.
IntAct; Q68FR9; 2.
STRING; 10116.ENSRNOP00000034828; -.
iPTMnet; Q68FR9; -.
PaxDb; Q68FR9; -.
PRIDE; Q68FR9; -.
Ensembl; ENSRNOT00000029456; ENSRNOP00000034828; ENSRNOG00000021638. [Q68FR9-2]
GeneID; 300033; -.
KEGG; rno:300033; -.
UCSC; RGD:621174; rat. [Q68FR9-1]
CTD; 1936; -.
RGD; 621174; Eef1d.
eggNOG; KOG1668; Eukaryota.
eggNOG; COG2092; LUCA.
GeneTree; ENSGT00390000011747; -.
HOGENOM; HOG000139586; -.
InParanoid; Q68FR9; -.
KO; K15410; -.
OMA; WLEKPRY; -.
OrthoDB; EOG091G0P0Z; -.
PhylomeDB; Q68FR9; -.
Reactome; R-RNO-156842; Eukaryotic Translation Elongation.
PRO; PR:Q68FR9; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000021638; -.
Genevisible; Q68FR9; RN.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00292; EF1B; 1.
Gene3D; 3.30.70.60; -; 1.
InterPro; IPR036219; eEF-1beta-like_sf.
InterPro; IPR018940; EF-1_beta_acid_region_euk.
InterPro; IPR014038; EF1B_bsu/dsu_GNE.
InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
Pfam; PF10587; EF-1_beta_acid; 1.
Pfam; PF00736; EF1_GNE; 1.
SMART; SM01182; EF-1_beta_acid; 1.
SMART; SM00888; EF1_GNE; 1.
SUPFAM; SSF54984; SSF54984; 1.
PROSITE; PS00825; EF1BD_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; DNA-binding;
Elongation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
Reference proteome; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P29692}.
CHAIN 2 281 Elongation factor 1-delta.
/FTId=PRO_0000382456.
REGION 80 115 Leucine-zipper. {ECO:0000250}.
REGION 173 281 Catalytic (GEF). {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 107 107 N6-acetyllysine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 117 117 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 117 117 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P57776}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 129 129 Phosphothreonine.
{ECO:0000250|UniProtKB:P29692}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 162 162 Phosphoserine; by CK2.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
VAR_SEQ 1 1 M -> MRSGKASCALETVWEDKHKYEEAERRFHEHEATQAA
AASVQQLLAEVPAVNGPSSQEDAEDTDEAETPNTSSRSDPR
KSHECKKPLQKKRKRSPKSWLGQADLALVGLSADHVWLDKP
LFDQAESSYRQRLADVAAQAAQSPALAPRGPCTHGSHVACH
HVTWGIWVNKSCFDQAERAFVEWSQALLLAAEGSHREGTPD
TGQQAVTPDLALACQPCPPANGQPPLGSLQALVREVWLEKP
RYDAAERGFYEALFDGHPPGKVRLQERASQAEGTRRGRRDR
RSRNTVGNKRAGSKRADGEAPSALPYWYFLHKDAEAPWLSK
PTYDSAECRHHAAEALRIAWRLEAASLAHRPTPRSGPSMSS
LRPKKM (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037887.
SEQUENCE 281 AA; 31330 MW; E77BE1BD8BACBA7D CRC64;
MATNFLMHEK IWFDKFKYDD AERRFYEQMN GPVTAGSRQE NGASVILRDI ARARENIQKS
LAGSSGPGAS SGPGGDHSDL IVRIASLEVE NQNLRGVVQD LQQAISKLEV RLSTLEKSSP
THRATAPQTQ HVSPMRQVEP PAKKGATPAE DDEDNDIDLF GSDEEEEDKE AARLREERLR
QYAEKKAKKP TLVAKSSILL DVKPWDDETD MAQLETCVRS IQLDGLVWGA SKLVPVGYGI
RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I


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