GRIK1_ARATH
ID GRIK1_ARATH Reviewed; 396 AA.
AC Q93V58; Q9M1T5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase GRIK1;
DE EC=2.7.11.1;
DE AltName: Full=Protein GEMINIVIRUS REP INTERACTING KINASE 1;
DE Short=Protein GRIK1;
DE AltName: Full=SnRK1-activating protein kinase 2;
DE Short=AtSnAK2;
GN Name=GRIK1; Synonyms=SNAK2; OrderedLocusNames=At3g45240;
GN ORFNames=F18N11, T14D3.180;
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=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).
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 INTERACTION WITH GEMINIVIRUS AL1, AUTOPHOSPHORYLATION, FUNCTION,
RP SUBCELLULAR LOCATION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12172024; DOI=10.1105/tpc.003681;
RA Kong L.-J., Hanley-Bowdoin L.;
RT "A geminivirus replication protein interacts with a protein kinase and a
RT motor protein that display different expression patterns during plant
RT development and infection.";
RL Plant Cell 14:1817-1832(2002).
RN [6]
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 [7]
RP FUNCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-137, INDUCTION, AND
RP DEVELOPMENTAL STAGE.
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 [8]
RP FUNCTION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-154 AND SER-261, AND
RP 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:12172024, ECO:0000269|PubMed:17041027,
CC ECO:0000269|PubMed:17237223, ECO:0000269|PubMed:19339507,
CC 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-154 and
CC inactivated when phosphorylated at Ser-261 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:12172024, ECO:0000269|PubMed:17041027}.
CC -!- INTERACTION:
CC Q93V58; Q38997-2: KIN10; NbExp=2; IntAct=EBI-6399184, EBI-20798606;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12172024}. Nucleus
CC {ECO:0000269|PubMed:12172024}. Note=Restricted to the nucleus in cells
CC infected by geminivirus.
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=Q93V58-1; Sequence=Displayed;
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:12172024, ECO:0000269|PubMed:17041027,
CC ECO:0000269|PubMed:19339507}.
CC -!- INDUCTION: By geminivirus (TGMV, CaLCuV or BCTV) infection (at the
CC protein level). {ECO:0000269|PubMed:12172024,
CC ECO:0000269|PubMed:17041027, ECO:0000269|PubMed:19339507}.
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=CAB72162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM489731; CAM32015.1; -; mRNA.
DR EMBL; AL132953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138649; CAB72162.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78007.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78008.1; -; Genomic_DNA.
DR EMBL; AY035070; AAK59575.1; -; mRNA.
DR EMBL; AY056309; AAL07158.1; -; mRNA.
DR PIR; T47464; T47464.
DR RefSeq; NP_001030811.1; NM_001035734.2. [Q93V58-1]
DR RefSeq; NP_566876.3; NM_114393.4. [Q93V58-1]
DR AlphaFoldDB; Q93V58; -.
DR SMR; Q93V58; -.
DR BioGRID; 8980; 8.
DR IntAct; Q93V58; 3.
DR STRING; 3702.AT3G45240.1; -.
DR iPTMnet; Q93V58; -.
DR SwissPalm; Q93V58; -.
DR PaxDb; Q93V58; -.
DR PRIDE; Q93V58; -.
DR ProteomicsDB; 247219; -. [Q93V58-1]
DR EnsemblPlants; AT3G45240.1; AT3G45240.1; AT3G45240. [Q93V58-1]
DR EnsemblPlants; AT3G45240.2; AT3G45240.2; AT3G45240. [Q93V58-1]
DR GeneID; 823660; -.
DR Gramene; AT3G45240.1; AT3G45240.1; AT3G45240. [Q93V58-1]
DR Gramene; AT3G45240.2; AT3G45240.2; AT3G45240. [Q93V58-1]
DR KEGG; ath:AT3G45240; -.
DR Araport; AT3G45240; -.
DR TAIR; locus:2096930; AT3G45240.
DR eggNOG; KOG0585; Eukaryota.
DR InParanoid; Q93V58; -.
DR OMA; SHEDNCH; -.
DR OrthoDB; 1044255at2759; -.
DR PhylomeDB; Q93V58; -.
DR PRO; PR:Q93V58; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93V58; baseline and differential.
DR Genevisible; Q93V58; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F: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; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 Alternative splicing; ATP-binding; Cytoplasm; Host-virus interaction;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..396
FT /note="Serine/threonine-protein kinase GRIK1"
FT /id="PRO_0000421034"
FT DOMAIN 108..369
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 22..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 114..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 154
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20164192"
FT MOD_RES 261
FT /note="Phosphoserine; by KIN10"
FT /evidence="ECO:0000269|PubMed:20164192"
FT MUTAGEN 137
FT /note="K->A: Abolishes autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19339507"
SQ SEQUENCE 396 AA; 44573 MW; F3C56641D73006B4 CRC64;
MFCDSFAFAQ VMSCFGCFGG SERSRHSPNP YDDDTYSHDS GETSNPGGDD EEGEEEEEVE
ELSRSKRSEE ILKCKLQNGL VCRQFPVKET NKLTRGEDED GNKTINEFVR ERKIGSGSYG
KVVLYRSTVD DKHYAIKAFH KSHLSRLRVA PSETAMGDVL REVMIMKTLE HPNIVNLIEV
IDDPEFDDFY MVLEYVDGKW AYDDSGPPGA LGEITARKYL RDVVAGLMYL HAHNVIHGDI
KPDNLLVTST GRVKIGDFSV SQVFKDDDDQ LRRSPGTPVF TAPECCLGIT YSGRSADTWA
VGVTLYCMIL GQYPFLGDTL QDTYDKIVHN PLIIPEGLNP RLRDLIEGLL CKDPNQRMTL
KAVAEHPWIT GEDGAISEYC CWCKRKAEEE EDQNHS
