ID   EF1D_RABIT              Reviewed;         280 AA.
AC   P53787;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Elongation factor 1-delta;
DE            Short=EF-1-delta;
GN   Name=EEF1D; Synonyms=EF1D;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RX   PubMed=9407120; DOI=10.1074/jbc.272.52.33290;
RA   Sheu G.-T., Traugh J.A.;
RT   "Recombinant subunits of mammalian elongation factor 1 expressed in
RT   Escherichia coli. Subunit interactions, elongation activity, and
RT   phosphorylation by protein kinase CKII.";
RL   J. Biol. Chem. 272:33290-33297(1997).
CC   -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC       to EF-1-alpha to GTP.
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR   EMBL; U42769; AAA84382.1; -; mRNA.
DR   EMBL; U47663; AAA89167.1; -; mRNA.
DR   RefSeq; NP_001075838.1; NM_001082369.1.
DR   AlphaFoldDB; P53787; -.
DR   SMR; P53787; -.
DR   iPTMnet; P53787; -.
DR   PRIDE; P53787; -.
DR   GeneID; 100009222; -.
DR   KEGG; ocu:100009222; -.
DR   CTD; 100009222; -.
DR   InParanoid; P53787; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
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; Elongation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..280
FT                   /note="Elongation factor 1-delta"
FT                   /id="PRO_0000155048"
FT   REGION          113..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         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         162
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P29692"
FT   CONFLICT        44
FT                   /note="T -> S (in Ref. 1; AAA89167)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   280 AA;  31075 MW;  FE58B4AC2A6C9058 CRC64;
     MTTNFLVHEK IWFDKFKYDD AERSFYERMN GPVPGPSRQE NGATVILRDI ARARENIQKS
     LAGSSGPGAS SGPGGDHSEL AVRIASLEVE NQNLRGVVQD LQRAVSKLEA RLSALEKSSP
     THRASAPQTQ HVSPMRQVEP PAKKAAAPAE DDEDDDIDLF GSDEEEDKEA ARLREERLRQ
     YAEKKARKPA LVAKSSILLD VKPWDDETDM ARLEACVRSV QLDGLVWGAS KLVPVGYGIR
     KLQIQCVVED DKVGTDLLEE EITKFEEHVQ SVDIAAFNKI