EF1B_DICDI
ID EF1B_DICDI Reviewed; 216 AA.
AC Q9GRF8; O60954; Q54Q62;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Elongation factor 1-beta;
DE AltName: Full=DdEF-1 beta;
GN Name=efa1B; Synonyms=eEF1beta; ORFNames=DDB_G0284035;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9546041; DOI=10.1016/s0167-4838(97)00220-3;
RA Chae S.-C., Maeda Y.;
RT "Cloning and sequence analysis of the cDNA encoding the elongation factor-1
RT beta of Dictyostelium discoideum.";
RL Biochim. Biophys. Acta 1383:1-3(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ACTIN.
RC STRAIN=AX3;
RX PubMed=11479029; DOI=10.1016/s0304-4165(01)00157-x;
RA Furukawa R., Jinks T.M., Tishgarten T., Mazzawi M., Morris D.R.,
RA Fechheimer M.;
RT "Elongation factor 1beta is an actin-binding protein.";
RL Biochim. Biophys. Acta 1527:130-140(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP PROTEIN SEQUENCE OF 2-18; 75-88 AND 168-176, CLEAVAGE OF INITIATOR
RP METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Patel H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC to EF-1-alpha to GTP. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and gamma
CC (By similarity). Interacts with actin. {ECO:0000250,
CC ECO:0000269|PubMed:11479029}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11479029}.
CC Note=Found in cortical and hyaline cytoplasm.
CC -!- DEVELOPMENTAL STAGE: Expressed during the vegetative growth phase,
CC followed by marked decrease in response to cell differentiation induced
CC by starvation. {ECO:0000269|PubMed:9546041}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25924.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB007025; BAA25924.1; ALT_FRAME; mRNA.
DR EMBL; U15926; AAG23402.1; -; mRNA.
DR EMBL; AAFI02000063; EAL65358.1; -; Genomic_DNA.
DR RefSeq; XP_638735.1; XM_633643.1.
DR AlphaFoldDB; Q9GRF8; -.
DR SMR; Q9GRF8; -.
DR STRING; 44689.DDB0191174; -.
DR PaxDb; Q9GRF8; -.
DR PRIDE; Q9GRF8; -.
DR EnsemblProtists; EAL65358; EAL65358; DDB_G0284035.
DR GeneID; 8624405; -.
DR KEGG; ddi:DDB_G0284035; -.
DR dictyBase; DDB_G0284035; efa1B.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_050172_0_2_1; -.
DR InParanoid; Q9GRF8; -.
DR OMA; FEVKPWD; -.
DR PhylomeDB; Q9GRF8; -.
DR Reactome; R-DDI-156842; Eukaryotic Translation Elongation.
DR PRO; PR:Q9GRF8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; ISS:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:dictyBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; ISS:dictyBase.
DR GO; GO:0030041; P:actin filament polymerization; IDA:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0006414; P:translational elongation; ISS:dictyBase.
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; IPR036282; Glutathione-S-Trfase_C_sf.
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; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..216
FT /note="Elongation factor 1-beta"
FT /id="PRO_0000326429"
FT CONFLICT 2..4
FT /note="PSF -> LL (in Ref. 1; BAA25924)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="E -> D (in Ref. 1; BAA25924)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24121 MW; 3E16C6CD6A703A5B CRC64;
MPSFADLTTE NGLVELNKFV SDKTYIVGFV PSSADVQAFN LVKTAPCATK YPHAARWFNT
IASYSAAEQG QFEKVTETVT IAAPAAPKAD DDVDLFGSDD EDDEEYERQL EERRKKAMEH
KKPKETVIAK SSILLDVKPW DDETDMVELE KCVRSIEMDG LVWGASKLVA VGYGIKKLVI
NLVVEDLKVS TDELEEKIKD FEDYVQSVDV AAFNKI
