EF1G2_ARATH
ID EF1G2_ARATH Reviewed; 413 AA.
AC Q9FVT2; Q94C85;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Probable elongation factor 1-gamma 2;
DE Short=EF-1-gamma 2;
DE AltName: Full=eEF-1B gamma 2;
GN OrderedLocusNames=At1g57720; ORFNames=T8L23.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000250}.
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DR EMBL; AC079733; AAG50755.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33455.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33456.1; -; Genomic_DNA.
DR EMBL; BT000973; AAN41373.1; -; mRNA.
DR EMBL; AY113043; AAM47351.1; -; mRNA.
DR EMBL; AY064630; AAL47343.1; -; mRNA.
DR EMBL; AF428347; AAL16277.1; -; mRNA.
DR EMBL; AF424630; AAL11623.1; -; mRNA.
DR EMBL; AF370502; AAK43879.1; -; mRNA.
DR EMBL; AY035082; AAK59587.1; -; mRNA.
DR EMBL; AY085256; AAM62488.1; -; mRNA.
DR PIR; E96611; E96611.
DR RefSeq; NP_001031202.1; NM_001036125.2.
DR RefSeq; NP_176084.1; NM_104568.4.
DR AlphaFoldDB; Q9FVT2; -.
DR SMR; Q9FVT2; -.
DR BioGRID; 27372; 15.
DR IntAct; Q9FVT2; 2.
DR STRING; 3702.AT1G57720.1; -.
DR PaxDb; Q9FVT2; -.
DR PRIDE; Q9FVT2; -.
DR ProteomicsDB; 224742; -.
DR EnsemblPlants; AT1G57720.1; AT1G57720.1; AT1G57720.
DR EnsemblPlants; AT1G57720.2; AT1G57720.2; AT1G57720.
DR GeneID; 842147; -.
DR Gramene; AT1G57720.1; AT1G57720.1; AT1G57720.
DR Gramene; AT1G57720.2; AT1G57720.2; AT1G57720.
DR KEGG; ath:AT1G57720; -.
DR Araport; AT1G57720; -.
DR TAIR; locus:2206535; AT1G57720.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR HOGENOM; CLU_011226_3_0_1; -.
DR InParanoid; Q9FVT2; -.
DR OMA; PFVMEEC; -.
DR OrthoDB; 1341490at2759; -.
DR PhylomeDB; Q9FVT2; -.
DR PRO; PR:Q9FVT2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVT2; baseline and differential.
DR Genevisible; Q9FVT2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR Gene3D; 3.30.70.1010; -; 1.
DR InterPro; IPR044628; EF-1-gamma_plant.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44372; PTHR44372; 1.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF89942; SSF89942; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Elongation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..413
FT /note="Probable elongation factor 1-gamma 2"
FT /id="PRO_0000208827"
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT DOMAIN 87..215
FT /note="GST C-terminal"
FT DOMAIN 253..413
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 207..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 178
FT /note="K -> E (in Ref. 3; AAK59587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 46400 MW; 2C0993D65B8A4530 CRC64;
MALVMHTYKG NKGANKALIA AEYAGVKIEE SADFQMGVTN KSPEFLKMNP IGKVPVLETP
EGPIFESNAI ARYVSRKNGD NSLNGSSLIE YAHIEQWIDF SSLEIDANML KWFAPRMGYA
PFSAPAEEAA ISALKRGLEA LNTHLASNTF LVGHSVTLAD IVTICNLNLG FATVMTKKFT
SAFPHVERYF WTMVNQPEFK KVLGDAKQTE AVPPVPTKKA PQPAKPKEEP KKAAPVAEAP
KPAEEEEAPK PKAKNPLDLL PPSPMVLDDW KRLYSNTKSN FREVAIKGFW DMYDPEGYSL
WFCDYKYNDE NMVSFVTLNK VGGFLQRMDL ARKYSFGKML ICGSEGPFKV KGLWLFRGPE
IPKFIMDEVY DMELYEWTKV DISDEAQKER VSQMIEDAEP FEGEALLDAK CFK
