GCN2_ARATH
ID GCN2_ARATH Reviewed; 1241 AA.
AC Q9LX30; Q8H2D3;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=eIF-2-alpha kinase GCN2 {ECO:0000250|UniProtKB:Q9HGN1};
DE AltName: Full=serine/threonine-protein kinase GCN2 {ECO:0000250|UniProtKB:P15442};
DE EC=2.7.11.1;
GN Name=GCN2 {ECO:0000250|UniProtKB:Q9HGN1}; OrderedLocusNames=At3g59410;
GN ORFNames=F25L23_270;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=12905023; DOI=10.1007/s00425-003-1025-4;
RA Zhang Y., Dickinson R., Paul M.J., Halford N.G.;
RT "Molecular cloning of an Arabidopsis homologue of GCN2, a protein kinase
RT involved in co-ordinated response to amino acid starvation.";
RL Planta 217:668-675(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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).
CC -!- FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates
CC the alpha subunit of eukaryotic translation initiation factor 2 eIF-2-
CC alpha in response to low amino acid availability. Plays a role as an
CC activator of the general amino acid control pathway required for
CC adapatation to amino acid starvation. Converts phosphorylated eIF-2-
CC alpha either to a competitive inhibitor of translation initiation,
CC leading to a global protein synthesis repression, and thus to a reduced
CC overall utilization of amino acids, or to a translational initiation
CC activation of specific mRNAs, and hence allowing reprogramming of amino
CC acid biosynthetic gene expression to alleviate nutrient depletion.
CC Binds uncharged tRNAs. {ECO:0000250|UniProtKB:P15442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P15442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P15442};
CC -!- ACTIVITY REGULATION: The kinase activity is stimulated upon binding to
CC uncharged tRNAs. {ECO:0000250|UniProtKB:P15442}.
CC -!- SUBUNIT: Homodimer; homodimerization is important for kinase activation
CC by uncharged tRNAs. {ECO:0000250|UniProtKB:P15442}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15442}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9LX30-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, buds, flowers,
CC siliques and seedlings. {ECO:0000269|PubMed:12905023}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Although it is unknown whether it is a serine/threonine or a
CC tyrosine protein kinase, it is strongly related to the
CC serine/threonine-protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB91611.1; Type=Erroneous gene model prediction; Evidence={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; AJ459823; CAD30860.1; -; mRNA.
DR EMBL; AL356014; CAB91611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79918.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63987.1; -; Genomic_DNA.
DR PIR; T49009; T49009.
DR RefSeq; NP_001326041.1; NM_001339969.1. [Q9LX30-1]
DR RefSeq; NP_191500.2; NM_115803.3. [Q9LX30-1]
DR AlphaFoldDB; Q9LX30; -.
DR SMR; Q9LX30; -.
DR STRING; 3702.AT3G59410.2; -.
DR iPTMnet; Q9LX30; -.
DR PaxDb; Q9LX30; -.
DR PRIDE; Q9LX30; -.
DR ProteomicsDB; 222173; -. [Q9LX30-1]
DR DNASU; 825110; -.
DR EnsemblPlants; AT3G59410.1; AT3G59410.1; AT3G59410. [Q9LX30-1]
DR EnsemblPlants; AT3G59410.3; AT3G59410.3; AT3G59410. [Q9LX30-1]
DR GeneID; 825110; -.
DR Gramene; AT3G59410.1; AT3G59410.1; AT3G59410. [Q9LX30-1]
DR Gramene; AT3G59410.3; AT3G59410.3; AT3G59410. [Q9LX30-1]
DR KEGG; ath:AT3G59410; -.
DR Araport; AT3G59410; -.
DR eggNOG; KOG1035; Eukaryota.
DR InParanoid; Q9LX30; -.
DR OMA; IVIKLRP; -.
DR PhylomeDB; Q9LX30; -.
DR PRO; PR:Q9LX30; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX30; baseline and differential.
DR Genevisible; Q9LX30; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:0072755; P:cellular response to benomyl; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:1990451; P:cellular stress response to acidic pH; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.10.110.10; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR024435; HisRS-related_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF12745; HGTP_anticodon2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SMART; SM00591; RWD; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50908; RWD; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Translation regulation; tRNA-binding.
FT CHAIN 1..1241
FT /note="eIF-2-alpha kinase GCN2"
FT /id="PRO_0000085961"
FT DOMAIN 37..148
FT /note="RWD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00179"
FT DOMAIN 425..731
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..1219
FT /note="Histidyl-tRNA synthetase-like"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 586
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 431..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1241 AA; 140322 MW; D098A1B7B01E1E0D CRC64;
MGRSSSKKKK KRGGSGRRGQ LKDHGSNADE DNELLSEEIT ALSAIFQEDC KVVSDSRSPP
QIAIKLRPYS KDMGYEDTDI SAMLIVRCLP GYPYKCPKLQ ITPEQGLTTA DAEKLLSLLE
DQANSNAREG RVMIFNLVEA AQEFLSEIIP ESHDEESVPC LTAHRSTQFI EQPMLSNIAK
SCSGGPFVYG FIDLFSGLED ARNWSLTPDE NRGIVSSVQS HPLDTSRILH QKPDKNLKRF
EDHAKEEVAL PAPIAKLNTV QEENVDDTSI SSFDSSKSTD DVESGLFQNE KKESNLQDDT
AEDDSTNSES ESLGSWSSDS LAQDQVPQIS KKDLLMVHLL RVACTSRGPL ADALPQITDE
LHELGILSEE VLDLASKSSP DFNRTFEHAF NQNMASTSVP QFWEPPSDSC EPNASLPSSR
YLNDFEELKP LGQGGFGHVV LCKNKLDGRQ YAVKKIRLKD KEIPVNSRIV REVATLSRLQ
HQHVVRYYQA WFETGVVDPF AGANWGSKTA GSSMFSYSGA VSTEIPEQDN NLESTYLYIQ
MEYCPRTLRQ VFESYNHFDK DFAWHLIRQI VEGLAHIHGQ GIIHRDFTPN NIFFDARNDI
KIGDFGLAKF LKLEQLDQDG GFSTDVAGSG VDSTGQAGTY FYTAPEIEQD WPKIDEKADM
YSLGVVFFEL WHPFGTAMER HVILTNLKLK GELPLKWVNE FPEQASLLRR LMSPSPSDRP
SATELLKHAF PPRMESELLD NILRIMQTSE DSSVYDRVVS VIFDEEVLEM KSHQSSRSRL
CADDSYIQYT EINTELRDYV VEITKEVFRQ HCAKHLEVIP MRLLSDCPQF SRKTVKLLTN
GGDMLELCYE LRLPFVHWIS VNQKSSFKRY EISHVYRRAI GHSPPNPCLQ ADFDIVGGTL
SLTEAEVLKV IVDITTHIFH RGSCDIHLNH GDLLDAIWSW AGIKAEHRRK VAELLSMMGS
LRPQSSERKL KWVFIRRQLL QELKLPEAVV NRLQTVASRF CGDADQALPR LRGALRADRP
TRKALDELSN LLTYLRVWRI EEHVHIDVLM PPTESYHRNL FFQVFLTKEN SSGTSNDGVL
LAVGGRYDWL VQEVCDREHK MNLPGAVGVS LALETIFQHL PMDLRPIRNE VSTSVLVCSR
GGGGLLVQRM ELVAELWEKS IKAEFVPTPD PSLTEQYEYA NEHEIKCLVI ITESGVAQNQ
IEFVKVRHLE LKKEKVVGRE ELVKFLLDAM AVQFRNPSVW S
