ID GRIK2_ARATH Reviewed; 407 AA.
AC Q5HZ38; Q8LPG6; Q9FKJ2;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 146.
DE RecName: Full=Serine/threonine-protein kinase GRIK2;
DE EC=2.7.11.1;
DE AltName: Full=Protein GEMINIVIRUS REP INTERACTING KINASE 2;
DE Short=Protein GRIK2;
DE AltName: Full=SnRK1-activating protein kinase 1;
DE Short=AtSnAK1;
GN Name=GRIK2; Synonyms=SNAK1; OrderedLocusNames=At5g60550; ORFNames=MUF9.18;
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 [MRNA], AND FUNCTION.
RC TISSUE=Seedling;
RX PubMed=17237223; DOI=10.1074/jbc.m611244200;
RA Hey S.J., Mayerhofer H., Halford N.G., Dickinson J.R.;
RT "DNA sequences from Arabidopsis, which encode protein kinases and function
RT as upstream regulators of Snf1 in yeast.";
RL J. Biol. Chem. 282:10472-10479(2007).
RN [2]
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 [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).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, INTERACTION WITH GEMINIVIRUS AL1, INDUCTION, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RX PubMed=17041027; DOI=10.1104/pp.106.088476;
RA Shen W., Hanley-Bowdoin L.;
RT "Geminivirus infection up-regulates the expression of two Arabidopsis
RT protein kinases related to yeast SNF1- and mammalian AMPK-activating
RT kinases.";
RL Plant Physiol. 142:1642-1655(2006).
RN [8]
RP FUNCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-136.
RX PubMed=19339507; DOI=10.1104/pp.108.132787;
RA Shen W., Reyes M.I., Hanley-Bowdoin L.;
RT "Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by
RT phosphorylating its activation loop.";
RL Plant Physiol. 150:996-1005(2009).
RN [9]
RP FUNCTION, PHOSPHORYLATION AT THR-153 AND SER-260, MUTAGENESIS OF THR-153
RP AND SER-260, AND ACTIVITY REGULATION.
RX PubMed=20164192; DOI=10.1074/jbc.m109.079194;
RA Crozet P., Jammes F., Valot B., Ambard-Bretteville F., Nessler S.,
RA Hodges M., Vidal J., Thomas M.;
RT "Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting
RT 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK)
RT determines their catalytic activities.";
RL J. Biol. Chem. 285:12071-12077(2010).
CC -!- FUNCTION: Activates SnRK1.1/KIN10 and SnRK1.2/KIN11 by phosphorylation
CC of their activation-loop 'Thr-198' and 'Thr-176', respectively.
CC Required for the regulation by SnRK1 kinases of the transcription of a
CC large set of genes, the modification the activity of metabolic enzymes,
CC and the control of various nutrient-responsive cellular developmental
CC processes. {ECO:0000269|PubMed:17041027, ECO:0000269|PubMed:17237223,
CC ECO:0000269|PubMed:19339507, ECO:0000269|PubMed:20164192}.
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 -!- 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;
CC -!- ACTIVITY REGULATION: Activated when autophosphorylated at Thr-153 and
CC inactivated when phosphorylated at Ser-260 by SnRK1.1/KIN10.
CC {ECO:0000269|PubMed:20164192}.
CC -!- SUBUNIT: Associates with the SNF1-related protein kinase (SnRK) complex
CC (By similarity). Interacts with AL1, a geminivirus (TGMV) protein
CC essential for viral replication. {ECO:0000250,
CC ECO:0000269|PubMed:17041027}.
CC -!- INTERACTION:
CC Q5HZ38; Q38997-2: KIN10; NbExp=2; IntAct=EBI-6399237, EBI-20798606;
CC -!- TISSUE SPECIFICITY: Expressed in shoot apical meristem, leaf primordium
CC and emerging petiole (at protein level). {ECO:0000269|PubMed:17041027}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in young leaf and floral tissues
CC but not expressed in mature tissues (at protein level).
CC {ECO:0000269|PubMed:17041027}.
CC -!- INDUCTION: By geminivirus (CaLCuV or BCTV) infection (at the protein
CC level). {ECO:0000269|PubMed:17041027}.
CC -!- MISCELLANEOUS: Functionally able to complement the yeast elm1 sak1 tos3
CC triple mutant.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08238.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM489730; CAM32014.1; -; mRNA.
DR EMBL; AB011483; BAB08238.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97343.1; -; Genomic_DNA.
DR EMBL; AY099846; AAM20697.1; -; mRNA.
DR EMBL; BT020486; AAW38987.1; -; mRNA.
DR EMBL; BT025976; ABG25065.1; -; mRNA.
DR RefSeq; NP_200863.2; NM_125448.4.
DR AlphaFoldDB; Q5HZ38; -.
DR SMR; Q5HZ38; -.
DR BioGRID; 21420; 2.
DR IntAct; Q5HZ38; 3.
DR STRING; 3702.Q5HZ38; -.
DR iPTMnet; Q5HZ38; -.
DR PaxDb; 3702-AT5G60550-1; -.
DR ProteomicsDB; 247293; -.
DR EnsemblPlants; AT5G60550.1; AT5G60550.1; AT5G60550.
DR GeneID; 836176; -.
DR Gramene; AT5G60550.1; AT5G60550.1; AT5G60550.
DR KEGG; ath:AT5G60550; -.
DR Araport; AT5G60550; -.
DR TAIR; AT5G60550; GRIK2.
DR eggNOG; KOG0585; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q5HZ38; -.
DR OMA; FACFRQP; -.
DR OrthoDB; 5475498at2759; -.
DR PhylomeDB; Q5HZ38; -.
DR PRO; PR:Q5HZ38; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5HZ38; baseline and differential.
DR Genevisible; Q5HZ38; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR CDD; cd14008; STKc_LKB1_CaMKK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF39; SERINE_THREONINE-PROTEIN KINASE GRIK1-RELATED; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Host-virus interaction; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..407
FT /note="Serine/threonine-protein kinase GRIK2"
FT /id="PRO_0000421035"
FT DOMAIN 107..370
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 21..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 113..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 153
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:20164192"
FT MOD_RES 260
FT /note="Phosphoserine; by KIN10"
FT /evidence="ECO:0000269|PubMed:20164192"
FT MUTAGEN 136
FT /note="K->A: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19339507"
FT MUTAGEN 153
FT /note="T->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:20164192"
FT MUTAGEN 260
FT /note="S->D: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:20164192"
FT CONFLICT 243
FT /note="N -> I (in Ref. 4; AAM20697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 45652 MW; FD7832EE2990BB11 CRC64;
MFRDSFLFAR TIGCFGCFGS SGSRNQQSPK PYDDDTHSCD SDVTSTARGE EEEDEEEVEQ
KSRSKRSEEI LKYRLDNGLI CRHIPVRETN ELIRGEDENG DKTINEYVRV CKIGSGSYGK
VVLYRSTLDG QYYAIKAFHK SHLLRLRVAP SETAMSDVLR EVMIMKILEH PNIVNLIEVI
DDPETDHFYM VLEYVDGKWV YDGSGPPGAL GEKTARKYLR DIVTGLMYLH AHDVIHGDIK
PDNLLVTSSG TVKIGDFSVS QVFKDDDDQL RRSPGTPVFT APECCLVSGI TYSGRAADTW
AVGVTLYCMI LGQYPFLADT LQDTYDKIVN NPLIIPDGLN PLLRDLIEGL LCKDPSQRMT
LKNVSEHPWV IGEDGHVPEY FCWCKRNAAS KIEEGEANGI SETSDPN
//
