ID   EF1D_MACFA              Reviewed;         281 AA.
AC   Q4R3D4;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Elongation factor 1-delta;
DE            Short=EF-1-delta;
GN   Name=EEF1D; ORFNames=QthA-21064, QtsA-17735;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis, and Thymus;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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=Q4R3D4-1; Sequence=Displayed;
CC       Name=2; Synonyms=eEF1BdeltaL;
CC         IsoId=Q4R3D4-2; Sequence=VSP_037886;
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; AB169168; BAE01260.1; -; mRNA.
DR   EMBL; AB179332; BAE02383.1; -; mRNA.
DR   EMBL; DK582287; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001271911.1; NM_001284982.1. [Q4R3D4-2]
DR   RefSeq; XP_015310247.1; XM_015454761.1. [Q4R3D4-1]
DR   RefSeq; XP_015310248.1; XM_015454762.1. [Q4R3D4-1]
DR   AlphaFoldDB; Q4R3D4; -.
DR   BMRB; Q4R3D4; -.
DR   SMR; Q4R3D4; -.
DR   STRING; 9541.XP_005564304.1; -.
DR   GeneID; 101866441; -.
DR   KEGG; mcf:101866441; -.
DR   CTD; 1936; -.
DR   VEuPathDB; HostDB:ENSMFAG00000034313; -.
DR   eggNOG; KOG1668; Eukaryota.
DR   OMA; HENIWFE; -.
DR   Proteomes; UP000233100; Chromosome 8.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   2: Evidence at transcript 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_0000382455"
FT   REGION          80..115
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000250"
FT   REGION          118..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        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:0000250|UniProtKB:Q68FR9"
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:0000250|UniProtKB:P29692"
FT   MOD_RES         147
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   MOD_RES         162
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   VAR_SEQ         1
FT                   /note="M -> MRSGKASCTLETVWEDKHKYEEAERRFYEHEAMQAAASAQQLPAEGP
FT                   AMNGPGQDDPEDTDEAEAPDGSSRSDPRKSQDGRKPLQKKRKRSPKSGLGPAAPALLGL
FT                   SAEPVWLDKSGLGPAAPALLGLSAERVWLDKSLFDQAESSYRQKLADVAAQAAQPPALA
FT                   PWGPCTHGSQVACHHVTWGTWVNKSSFDQAERAFVEWSQSLLLAPEGGHRQGTPDTGQQ
FT                   AAVPNPAHQPSPPVNGQPPLGSLQALVREVWLEKPRYDAAERGFYEALFDGHPPGKVRL
FT                   QERAGLAEGARRGRRDRRGRHVLGNKRAGPRWADGEAPSALPYCYFLQKDAEAPWLSKP
FT                   AYDSAECRHHVAEALRMAWCLEAASLSHRPGPRSGLSVSSLRPNRKM (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_037886"
FT   CONFLICT        35
FT                   /note="G -> V (in Ref. 1; DK582287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   281 AA;  31190 MW;  8B05D8532998AD2E CRC64;
     MATNFLVHEK IWFDKFKYDD AERRFYEQMN GPVAGASRQE NGASVILRDI ARARENIQKS
     LAGTSGPGAS SGPSGDHSEL VVRIASLEVE NQSLRGVVQE LQQAISKLEA RLNVLEKSSP
     GHRATAPQTQ HVSPMRQVEP PAKKPATPAE DDEDDDIDLF GSDNEEEDKE AAQLREERLR
     QYAEKKAKKP ALVAKSSILL DVKPWDDETD MAQLEACVRS IQLDGLVWGA SKLVPVGYGI
     RKLQIQCVVE DDKVGTDLLE EEITKFEEHV QSVDIAAFNK I