IF2A_ARATH
ID IF2A_ARATH Reviewed; 344 AA.
AC Q9FE78; Q9C5N6;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit alpha {ECO:0000305};
DE Short=eIF2-alpha {ECO:0000305};
GN Name=EIF2A {ECO:0000305};
GN OrderedLocusNames=At5g05470 {ECO:0000312|Araport:AT5G05470};
GN ORFNames=K18I23.28 {ECO:0000312|EMBL:BAB11536.1};
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 [MRNA].
RA Browning K.S., Chen R.;
RT "Arabidopsis thaliana protein synthesis initiation factor eIF2 alpha
RT mRNA.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION AT SER-317 AND SER-322.
RX PubMed=19509420; DOI=10.1074/jbc.m109.007658;
RA Dennis M.D., Person M.D., Browning K.S.;
RT "Phosphorylation of plant translation initiation factors by CK2 enhances
RT the in vitro interaction of multifactor complex components.";
RL J. Biol. Chem. 284:20615-20628(2009).
RN [9]
RP PHOSPHORYLATION AT SER-56.
RX PubMed=22672016; DOI=10.1111/j.1438-8677.2012.00606.x;
RA Li M.W., Auyeung W.K., Lam H.M.;
RT "The GCN2 homologue in Arabidopsis thaliana interacts with uncharged tRNA
RT and uses Arabidopsis eIF2alpha molecules as direct substrates.";
RL Plant Biol. 15:13-18(2013).
CC -!- FUNCTION: Functions in the early steps of protein synthesis by forming
CC a ternary complex with GTP and initiator tRNA. This complex binds to a
CC 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-
CC initiation complex. Junction of the 60S ribosomal subunit to form the
CC 80S initiation complex is preceded by hydrolysis of the GTP bound to
CC eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.
CC {ECO:0000250|UniProtKB:P20459}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000250|UniProtKB:P20459}.
CC -!- PTM: Phosphorylated at Ser-56 by GCN2 (Probable). Phosphorylated at
CC Ser-317 and Ser-322 by CK2 (Probable). {ECO:0000305|PubMed:19509420,
CC ECO:0000305|PubMed:22672016}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF353096; AAK29673.1; -; mRNA.
DR EMBL; AB005241; BAB11536.1; -; Genomic_DNA.
DR EMBL; AB010692; BAB11536.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED90877.1; -; Genomic_DNA.
DR EMBL; AK117513; BAC42176.1; -; mRNA.
DR EMBL; AF324988; AAG40340.1; -; mRNA.
DR EMBL; BT024879; ABD85150.1; -; mRNA.
DR RefSeq; NP_196166.1; NM_120629.3.
DR AlphaFoldDB; Q9FE78; -.
DR SMR; Q9FE78; -.
DR IntAct; Q9FE78; 1.
DR STRING; 3702.AT5G05470.1; -.
DR iPTMnet; Q9FE78; -.
DR PaxDb; Q9FE78; -.
DR PRIDE; Q9FE78; -.
DR ProteomicsDB; 232222; -.
DR EnsemblPlants; AT5G05470.1; AT5G05470.1; AT5G05470.
DR GeneID; 830430; -.
DR Gramene; AT5G05470.1; AT5G05470.1; AT5G05470.
DR KEGG; ath:AT5G05470; -.
DR Araport; AT5G05470; -.
DR TAIR; locus:2153464; AT5G05470.
DR eggNOG; KOG2916; Eukaryota.
DR HOGENOM; CLU_033458_0_1_1; -.
DR InParanoid; Q9FE78; -.
DR OMA; YKKHGHA; -.
DR OrthoDB; 1093186at2759; -.
DR PhylomeDB; Q9FE78; -.
DR PRO; PR:Q9FE78; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FE78; baseline and differential.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IBA:GO_Central.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IBA:GO_Central.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 1.10.150.190; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.1130; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; PTHR10602; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; SSF110993; 1.
DR SUPFAM; SSF116742; SSF116742; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..344
FT /note="Eukaryotic translation initiation factor 2 subunit
FT alpha"
FT /id="PRO_0000437153"
FT DOMAIN 21..92
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 309..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..333
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphoserine; by GCN2"
FT /evidence="ECO:0000305|PubMed:22672016"
FT MOD_RES 317
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000305|PubMed:19509420"
FT MOD_RES 322
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000305|PubMed:19509420"
FT CONFLICT 61
FT /note="R -> G (in Ref. 1; AAK29673)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="Missing (in Ref. 1; AAK29673)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38801 MW; 7D740D60FBC04514 CRC64;
MANPAPNLEC RMYESRYPDV DMAVMIQVKT IADMGAYVSL LEYNNIEGMI LFSELSRRRI
RSISSLIKVG RTEPVMVLRV DRERGYIDLS KRRVSDEDKE ACEERYNKSK LVHSIMRHVA
ETVGVDLEEL YVNIGWPLYK KHGHAFEAFK IVVTDPDSVF DALTREVKET GPDGVEVTKV
VPAVSEELKD AFLKDIRRRM TPQPMKIRAD IELKCFQFDG VLHIKEAMKK AEAVGTDDCP
VKIKLVAPPL YVLTTHTHYK EKGIVTLNKA IEACITAIEE HKGKLVVKEG ARAVSERDDK
LLAEHMAKLR MDNEEMSGDE GSEDEEEDTG MGEVDIDGGS GIIE
