ID EF1A3_XENLA Reviewed; 461 AA.
AC P17508;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Elongation factor 1-alpha, oocyte form;
DE AltName: Full=EF-1-alpha-O1;
DE Short=EF-1AO1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1988459; DOI=10.1083/jcb.112.2.237;
RA Coppard N.J., Poulsen K., Madsen H.O., Frydenberg J., Clark B.F.C.;
RT "42Sp48 in previtellogenic Xenopus oocytes is structurally homologous to
RT EF-1 alpha and may be a stage-specific elongation factor.";
RL J. Cell Biol. 112:237-243(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-461.
RC TISSUE=Oocyte;
RX PubMed=2362804; DOI=10.1093/nar/18.12.3489;
RA Dje M.K., Mazabraud A., Viel A., le Maire M., Denis H., Crawford E.T.,
RA Brown D.D.;
RT "Three genes under different developmental control encode elongation factor
RT 1-alpha in Xenopus laevis.";
RL Nucleic Acids Res. 18:3489-3493(1990).
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1894690; DOI=10.1083/jcb.114.6.1109;
RA Deschamps S., Morales J., Mazabraud A., le Maire M., Denis H., Brown D.D.;
RT "Two forms of elongation factor 1 alpha (EF-1 alpha O and 42Sp50), present
RT in oocytes, but absent in somatic cells of Xenopus laevis.";
RL J. Cell Biol. 114:1109-1111(1991).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Oocyte.
CC -!- DEVELOPMENTAL STAGE: 3 EF-1-alpha are expressed under different
CC developmental control in Xenopus laevis.
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; X56699; CAA40029.1; -; mRNA.
DR EMBL; X52977; CAA37169.1; -; mRNA.
DR PIR; S13806; S13806.
DR AlphaFoldDB; P17508; -.
DR SMR; P17508; -.
DR IntAct; P17508; 2.
DR AGR; Xenbase:XB-GENE-17330483; -.
DR Xenbase; XB-GENE-17330483; eef1a1o.S.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; 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 CDD; cd01883; EF1_alpha; 1.
DR CDD; cd03693; EF1_alpha_II; 1.
DR CDD; cd03705; EF1_alpha_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
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 NCBIfam; TIGR00483; EF-1_alpha; 1.
DR PANTHER; PTHR23115:SF271; ELONGATION FACTOR 1-ALPHA; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
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; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Methylation; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CHAIN 2..461
FT /note="Elongation factor 1-alpha, oocyte form"
FT /id="PRO_0000090901"
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 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 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT CONFLICT 139
FT /note="L -> F (in Ref. 2; CAA37169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 50195 MW; F55AE74BCD8C5BEC CRC64;
MGKEKIHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETGKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAGGV
GEFEAGISKN GQTREHALLA FTLGVKQLII GVNKMDSTEP PFSQKRFEEI TKEVSAYIKK
IGYNPATVPF VPISGWHGDN MLEASTNMPW FKGWKIERKE GNASGITLLE ALDCIIPPQR
PTNKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMIVTF APSNVTTEVK SVEMHHEALV
EALPGDNVGF NVKNISVKDI RRGNVAGDSK NDPPMQAGSF TAQVIILNHP GQISAGYAPV
LDCHTAHIAC KFAELKQKID RRSGKKLEDD PKFLKSGDAA IVEMIPGKPM CVETFSDYPP
LGRFAVRDMR QTVAVGVIKG VDKKLASSGK VTKSAAKAGK K
//
