IF2AH_ARATH
ID IF2AH_ARATH Reviewed; 344 AA.
AC Q9SIZ2; Q8LEV8;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit alpha homolog {ECO:0000305};
GN OrderedLocusNames=At2g40290 {ECO:0000312|Araport:AT2G40290};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
RN [6]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9SIZ2-1; Sequence=Displayed;
CC -!- PTM: Phosphorylated at Ser-56 by GCN2. {ECO:0000305|PubMed:22672016}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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DR EMBL; AC007020; AAD25664.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09807.1; -; Genomic_DNA.
DR EMBL; AY080668; AAL86344.1; -; mRNA.
DR EMBL; AY117188; AAM51263.1; -; mRNA.
DR EMBL; AY085202; AAM61752.1; -; mRNA.
DR PIR; F84827; F84827.
DR RefSeq; NP_565927.1; NM_129587.3. [Q9SIZ2-1]
DR AlphaFoldDB; Q9SIZ2; -.
DR SMR; Q9SIZ2; -.
DR IntAct; Q9SIZ2; 1.
DR STRING; 3702.AT2G40290.1; -.
DR iPTMnet; Q9SIZ2; -.
DR PaxDb; Q9SIZ2; -.
DR PRIDE; Q9SIZ2; -.
DR ProteomicsDB; 232148; -. [Q9SIZ2-1]
DR EnsemblPlants; AT2G40290.1; AT2G40290.1; AT2G40290. [Q9SIZ2-1]
DR GeneID; 818621; -.
DR Gramene; AT2G40290.1; AT2G40290.1; AT2G40290. [Q9SIZ2-1]
DR KEGG; ath:AT2G40290; -.
DR Araport; AT2G40290; -.
DR TAIR; locus:2063093; AT2G40290.
DR eggNOG; KOG2916; Eukaryota.
DR HOGENOM; CLU_033458_0_1_1; -.
DR InParanoid; Q9SIZ2; -.
DR OMA; DVNEHQR; -.
DR PhylomeDB; Q9SIZ2; -.
DR PRO; PR:Q9SIZ2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIZ2; 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:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
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 Alternative splicing; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..344
FT /note="Eukaryotic translation initiation factor 2 subunit
FT alpha homolog"
FT /id="PRO_0000437154"
FT DOMAIN 21..92
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 312..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 CONFLICT 93
FT /note="R -> K (in Ref. 4; AAM61752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38748 MW; 25B88DD8181BE108 CRC64;
MASQTPNLEC RMYEAKYPEV DMAVMIQVKN IADMGAYVSL LEYNNIEGMI LFSELSRRRI
RSVSSLIKVG RIEPVMVLRV DKEKGYIDLS KRRVSEEDIQ TCEERYNKSK LVHSIMRHVA
ETLSIDLEDL YVNIGWPLYR RHGHAFEAFK ILVTDPDSVL GPLTREIKEV GPDGQEVTKV
VPAVTEEVKD ALVKNIRRRM TPQPMKIRAD IELKCFQFDG VVHIKEAMKN AEAAGNEDCP
VKIKLVAPPL YVLTTQTLDK EQGIEILNKA IAACTETIET HKGKLVVKEG ARAVSERDEK
MLTEHMAKLR LDNEEMSGDE DSGDEEEDTG MGEVDLDAGA GIIE
