EF1A0_XENLA
ID EF1A0_XENLA Reviewed; 462 AA.
AC P13549; Q5D0D3; Q91732;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Elongation factor 1-alpha, somatic form;
DE Short=EF-1-alpha-S;
GN Name=eef1as;
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].
RC TISSUE=Embryo;
RX PubMed=2707491; DOI=10.1016/0012-1606(89)90300-x;
RA Krieg P.A., Varnum S.M., Wormington W.M., Melton D.A.;
RT "The mRNA encoding elongation factor 1-alpha (EF-1 alpha) is a major
RT transcript at the midblastula transition in Xenopus.";
RL Dev. Biol. 133:93-100(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2283000; DOI=10.1111/j.1432-0436.1990.tb00543.x;
RA Poeting A., Danker K., Hartmann L., Koester M., Wedlich D., Knoechel W.;
RT "Two different mRNAs coding for identical elongation factor 1 alpha (EF-1
RT alpha) polypeptides in Xenopus laevis embryos.";
RL Differentiation 44:103-110(1990).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8565334; DOI=10.1002/dvg.1020170313;
RA Johnson A.D., Krieg P.A.;
RT "A Xenopus laevis gene encoding EF-1 alpha S, the somatic form of
RT elongation factor 1 alpha: sequence, structure, and identification of
RT regulatory elements required for embryonic transcription.";
RL Dev. Genet. 17:280-290(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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 -!- DEVELOPMENTAL STAGE: 3 EF-1-alpha are expressed under different
CC developmental control in Xenopus laevis. This protein is expressed in
CC embryos beginning at the mid-blastula transition and in adults cells.
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; M25504; AAA49700.1; -; mRNA.
DR EMBL; X55324; CAA39027.1; -; mRNA.
DR EMBL; M25697; AAB00075.1; -; Genomic_DNA.
DR EMBL; BC041196; AAH41196.1; -; mRNA.
DR EMBL; BC043843; AAH43843.1; -; mRNA.
DR PIR; A60491; A60491.
DR RefSeq; NP_001080911.1; NM_001087442.1.
DR RefSeq; XP_018096058.1; XM_018240569.1.
DR RefSeq; XP_018096059.1; XM_018240570.1.
DR RefSeq; XP_018096060.1; XM_018240571.1.
DR RefSeq; XP_018096061.1; XM_018240572.1.
DR RefSeq; XP_018096062.1; XM_018240573.1.
DR RefSeq; XP_018096063.1; XM_018240574.1.
DR RefSeq; XP_018096064.1; XM_018240575.1.
DR RefSeq; XP_018096065.1; XM_018240576.1.
DR RefSeq; XP_018096066.1; XM_018240577.1.
DR AlphaFoldDB; P13549; -.
DR SMR; P13549; -.
DR BioGRID; 98848; 1.
DR PRIDE; P13549; -.
DR DNASU; 386604; -.
DR GeneID; 108704161; -.
DR GeneID; 386604; -.
DR KEGG; xla:108704161; -.
DR CTD; 108704161; -.
DR CTD; 386604; -.
DR Xenbase; XB-GENE-17330683; eef1a1.L.
DR Xenbase; XB-GENE-865341; eef1a1.S.
DR OMA; AIRDMGM; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 108704161; Expressed in intestine and 19 other tissues.
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 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 2: Evidence at transcript level;
KW Cytoplasm; Elongation factor; GTP-binding; Methylation; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P68104"
FT CHAIN 2..462
FT /note="Elongation factor 1-alpha, somatic form"
FT /id="PRO_0000090898"
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 9
FT /note="N -> K (in Ref. 1; AAA49700)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="N -> I (in Ref. 1; AAA49700)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="V -> L (in Ref. 1; AAA49700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50214 MW; 8A196BECA4012FA0 CRC64;
MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
GEFEAGISKN GQTREHALLA YTLGVKQLIV GINKMDSTEP PYSQKRYEEI VKEVSTYIKK
IGYNPDTVAF VPISGWNGDN MLEPSPNMPW FKGWKITRKE GSGSGTTLLE ALDCILPPSR
PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VIKPGMVVTF APVNVTTEVK SVEMHHEALT
EAVPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAGSF TAQVIILNHP GQIGAGYAPV
LDCHTAHIAC KFAELKEKID RRSGKKLEDN PKFLKSGDAA IVDMIPGKPM CVESFSDYPP
LGRFAVRDMR QTVAVGVIKA VEKKAAGSGK VTKSAQKAAK TK
