EF1A1_XENLA
ID EF1A1_XENLA Reviewed; 463 AA.
AC P17506;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
DE AltName: Full=42Sp50;
DE AltName: Full=Thesaurin A;
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=8502575; DOI=10.1093/nar/21.9.2259;
RA Cheng F.-M., Darby M.K., Joho K.E.;
RT "Correction of the nucleotide and amino acid sequence of Xenopus laevis
RT 42Sp50.";
RL Nucleic Acids Res. 21:2259-2259(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [4]
RP FUNCTION.
RX PubMed=2037589; DOI=10.1016/s0021-9258(18)99238-0;
RA Viel A., le Maire M., Philippe H., Morales J., Mazabraud A., Denis H.;
RT "Structural and functional properties of thesaurin a (42Sp50), the major
RT protein of the 42 S particles present in Xenopus laevis previtellogenic
RT oocytes.";
RL J. Biol. Chem. 266:10392-10399(1991).
CC -!- FUNCTION: This protein is one of two protein components of a 42S RNP
CC particle that is very abundant in previtellogenic oocytes. A major
CC function served by 42sp50 appears to be the storage of tRNAs for later
CC use in oogenesis and early embryogenesis. Purified 42S particles can
CC directly transfer aminoacyl tRNA to ribosomes.
CC {ECO:0000269|PubMed:2037589}.
CC -!- SUBUNIT: The 42S RNP particle comprises four subunits each of which
CC contains one molecule of 5S RNA, three molecules of tRNA, two molecules
CC of EF1-alpha and one molecule of the 5S RNA binding protein 43.
CC -!- INTERACTION:
CC P17506; O73932: igf2bp3-a; NbExp=4; IntAct=EBI-8486828, EBI-619004;
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
CC exclusively in immature oocytes.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; Z19545; CAA79605.1; -; mRNA.
DR EMBL; X52975; CAA37167.1; -; mRNA.
DR PIR; S10224; S10224.
DR RefSeq; NP_001095231.1; NM_001101761.1.
DR AlphaFoldDB; P17506; -.
DR SMR; P17506; -.
DR IntAct; P17506; 3.
DR MINT; P17506; -.
DR MoonProt; P17506; -.
DR PRIDE; P17506; -.
DR GeneID; 397889; -.
DR KEGG; xla:397889; -.
DR CTD; 397889; -.
DR Xenbase; XB-GENE-5853356; 42sp50.L.
DR OMA; AHVTCRF; -.
DR OrthoDB; 1150082at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 397889; Expressed in ovary and 15 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
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 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 Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..463
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090899"
FT DOMAIN 8..245
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 17..24
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 73..77
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 94..97
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 156..159
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 197..199
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 94..98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 253..255
FT /note="LQD -> PAY (in Ref. 2; CAA37167)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="V -> A (in Ref. 2; CAA37167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 50678 MW; 96F482F4B198C128 CRC64;
MTDKAPQKTH LNIVIIGHVD SGKSTTTGHL IYKCGGFDPR ALEKVEAAAA QLGKSSFKFA
WILDKLKAER ERGITIDISL WKFQTNRFTI TIIDAPGHRD FIKNMITGTS QADVALLVVS
AATGEFEAGV SRNGQTREHA LLAYTMGVKQ LIVCVNKMDL TDPPYSHKRF DEVVRNVMVY
LKKIGYNPAT IPFVPVSGWT GENISSPSQK MGWFKGWKVK RKDGFTKGQS LLEVLDALVP
PVRPANKPLR LPLQDVYKIG GIGTVPVGKI ETGILKPGMT ISFAPSGFSA EVKSIEMHHE
PLQMAFPGFN IGFNVKNIAV KSLKRGNVAG NSKSDPPTEA SSFTAQVIIL NHPGFIKAGY
SPVIDCHTAH ITCQFAELQE KIDRRTGKKL EDNPGLLKSG DAAIITLKPI KPFCVERFFD
YPPLGRFAAR DLKQTVAVGV VKSVEHKAGA AARRQVQKPV LVK
