EF1A2_RABIT
ID EF1A2_RABIT Reviewed; 463 AA.
AC Q71V39;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Elongation factor 1-alpha 2;
DE Short=EF-1-alpha-2;
DE AltName: Full=Eukaryotic elongation factor 1 A-2;
DE Short=eEF1A-2;
DE AltName: Full=Statin-S1;
GN Name=EEF1A2;
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], PARTIAL PROTEIN SEQUENCE, METHYLATION AT LYS-55
RP AND LYS-165, ETHANOLAMINYLATION AT GLU-301 AND GLU-374, CHARACTERIZATION,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=9518480; DOI=10.1093/nar/26.8.1884;
RA Kahns S., Lund A., Kristensen P., Knudsen C.R., Clark B.F.C., Cavallius J.,
RA Merrick W.C.;
RT "The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and
RT characterization of the protein.";
RL Nucleic Acids Res. 26:1884-1890(1998).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q71V39; P19174: PLCG1; Xeno; NbExp=3; IntAct=EBI-7645815, EBI-79387;
CC Q71V39; Q06124: PTPN11; Xeno; NbExp=2; IntAct=EBI-7645815, EBI-297779;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9518480}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, brain and
CC aorta. Not expressed in liver, kidney, spleen and lung.
CC -!- PTM: Methylated (PubMed:9518480). Trimethylated at Lys-165 by
CC EEF1AKMT3. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4;
CC trimethylated form is predominant. Methylation by EEF1AKMT4 contributes
CC to the fine-tuning of translation rates for a subset of tRNAs (By
CC similarity). Trimethylated at the N-terminus and dimethylated at Lys-55
CC by METTL13 (By similarity). {ECO:0000250|UniProtKB:Q05639,
CC ECO:0000269|PubMed:9518480}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000305}.
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DR EMBL; AF035178; AAC39252.1; -; mRNA.
DR RefSeq; NP_001075500.1; NM_001082031.1.
DR PDB; 4C0S; X-ray; 2.70 A; A/B=1-463.
DR PDB; 6RA9; X-ray; 2.70 A; A=1-454, B=1-461.
DR PDBsum; 4C0S; -.
DR PDBsum; 6RA9; -.
DR AlphaFoldDB; Q71V39; -.
DR SMR; Q71V39; -.
DR IntAct; Q71V39; 5.
DR MINT; Q71V39; -.
DR GeneID; 100008677; -.
DR KEGG; ocu:100008677; -.
DR CTD; 1917; -.
DR InParanoid; Q71V39; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00118_A; EF_Tu_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Elongation factor;
KW GTP-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..463
FT /note="Elongation factor 1-alpha 2"
FT /id="PRO_0000090893"
FT DOMAIN 5..242
FT /note="tr-type G"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000250"
FT REGION 444..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT MOD_RES 36
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 36
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 36
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 55
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:9518480"
FT MOD_RES 55
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 79
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 165
FT /note="N6,N6,N6-trimethyllysine; alternate; by EEF1AKMT3"
FT /evidence="ECO:0000269|PubMed:9518480"
FT MOD_RES 165
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 165
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62632"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:9518480"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000269|PubMed:9518480"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05639"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 164..181
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6RA9"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6RA9"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6RA9"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 285..298
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 366..379
FT /evidence="ECO:0007829|PDB:6RA9"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:6RA9"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:6RA9"
FT STRAND 431..443
FT /evidence="ECO:0007829|PDB:6RA9"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:6RA9"
SQ SEQUENCE 463 AA; 50470 MW; 31E4E341CEE797EC CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK
IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
EALPGDNVGF NVKNVSVKDI RRGNVCGDSK SDPPQEAAQF TSQVIILNHP GQISAGYSPV
IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
