EF1D_RAT
ID EF1D_RAT Reviewed; 281 AA.
AC Q68FR9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Elongation factor 1-delta;
DE Short=EF-1-delta;
GN Name=Eef1d;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-133; THR-147 AND
RP SER-162, AND 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).
CC -!- FUNCTION: [Isoform 1]: EF-1-beta and EF-1-delta stimulate the exchange
CC of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another
CC round of transfer of aminoacyl-tRNAs to the ribosome. {ECO:0000250}.
CC -!- FUNCTION: [Isoform 2]: Regulates induction of heat-shock-responsive
CC genes through association with heat shock transcription factors and
CC direct DNA-binding at heat shock promoter elements (HSE).
CC {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta isoform 1,
CC and gamma. Isoform 2 interacts with HSF1 and NFE2L2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68FR9-1; Sequence=Displayed;
CC Name=2; Synonyms=eEF1BdeltaL;
CC IsoId=Q68FR9-2; Sequence=VSP_037887;
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; CH473950; EDM16037.1; -; Genomic_DNA.
DR EMBL; BC079391; AAH79391.1; -; mRNA.
DR RefSeq; NP_001013122.1; NM_001013104.1. [Q68FR9-2]
DR RefSeq; XP_008763779.1; XM_008765557.1. [Q68FR9-1]
DR RefSeq; XP_008763780.1; XM_008765558.1. [Q68FR9-1]
DR RefSeq; XP_008763781.1; XM_008765559.1. [Q68FR9-1]
DR AlphaFoldDB; Q68FR9; -.
DR SMR; Q68FR9; -.
DR BioGRID; 256417; 3.
DR IntAct; Q68FR9; 2.
DR STRING; 10116.ENSRNOP00000034828; -.
DR iPTMnet; Q68FR9; -.
DR PhosphoSitePlus; Q68FR9; -.
DR jPOST; Q68FR9; -.
DR PaxDb; Q68FR9; -.
DR PRIDE; Q68FR9; -.
DR GeneID; 300033; -.
DR KEGG; rno:300033; -.
DR UCSC; RGD:621174; rat. [Q68FR9-1]
DR CTD; 1936; -.
DR RGD; 621174; Eef1d.
DR VEuPathDB; HostDB:ENSRNOG00000021638; -.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_020166_0_0_1; -.
DR InParanoid; Q68FR9; -.
DR OMA; RVWLDKP; -.
DR OrthoDB; 1464823at2759; -.
DR PhylomeDB; Q68FR9; -.
DR Reactome; R-RNO-156842; Eukaryotic Translation Elongation.
DR PRO; PR:Q68FR9; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Proteomes; UP000234681; Chromosome 7.
DR Bgee; ENSRNOG00000021638; Expressed in testis and 20 other tissues.
DR Genevisible; Q68FR9; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:RGD.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF10587; EF-1_beta_acid; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM01182; EF-1_beta_acid; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Elongation factor; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT CHAIN 2..281
FT /note="Elongation factor 1-delta"
FT /id="PRO_0000382456"
FT REGION 80..115
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT REGION 115..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..281
FT /note="Catalytic (GEF)"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 107
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P57776"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P29692"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 162
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1
FT /note="M -> MRSGKASCALETVWEDKHKYEEAERRFHEHEATQAAAASVQQLLAEV
FT PAVNGPSSQEDAEDTDEAETPNTSSRSDPRKSHECKKPLQKKRKRSPKSWLGQADLALV
FT GLSADHVWLDKPLFDQAESSYRQRLADVAAQAAQSPALAPRGPCTHGSHVACHHVTWGI
FT WVNKSCFDQAERAFVEWSQALLLAAEGSHREGTPDTGQQAVTPDLALACQPCPPANGQP
FT PLGSLQALVREVWLEKPRYDAAERGFYEALFDGHPPGKVRLQERASQAEGTRRGRRDRR
FT SRNTVGNKRAGSKRADGEAPSALPYWYFLHKDAEAPWLSKPTYDSAECRHHAAEALRIA
FT WRLEAASLAHRPTPRSGPSMSSLRPKKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037887"
SQ 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
