CARK1_ARATH
ID CARK1_ARATH Reviewed; 364 AA.
AC Q9LUT0; A0A178VE22;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Receptor-like cytoplasmic kinase 1 {ECO:0000303|PubMed:29928509, ECO:0000303|PubMed:29970817};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q41328};
GN Name=CARK1 {ECO:0000303|PubMed:29928509, ECO:0000303|PubMed:29970817};
GN OrderedLocusNames=At3g17410 {ECO:0000312|Araport:AT3G17410};
GN ORFNames=MGD8.25 {ECO:0000312|EMBL:BAB02745.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
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 FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=29970817; DOI=10.3390/ijms19071945;
RA Ge H., Li X., Chen S., Zhang M., Liu Z., Wang J., Li X., Yang Y.;
RT "The expression of CARK1 or RCAR11 driven by synthetic promoters increases
RT drought tolerance in Arabidopsis thaliana.";
RL Int. J. Mol. Sci. 19:1945-1945(2018).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 50-350 IN COMPLEX WITH ANP AND
RP MAGNESIUM ION, INTERACTION WITH PYL8/RCAR3 AND PYR1/RCAR11, FUNCTION,
RP MUTAGENESIS OF ASN-204; SER-221; SER-233; THR-234 AND THR-239, DISRUPTION
RP PHENOTYPE, COFACTOR, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, AND
RP PHOSPHORYLATION AT THR-234 AND THR-239.
RX PubMed=29928509; DOI=10.1038/s41421-018-0029-y;
RA Zhang L., Li X., Li D., Sun Y., Li Y., Luo Q., Liu Z., Wang J., Li X.,
RA Zhang H., Lou Z., Yang Y.;
RT "CARK1 mediates ABA signaling by phosphorylation of ABA receptors.";
RL Cell Discov. 4:30-30(2018).
CC -!- FUNCTION: Receptor-like cytoplasmic kinase (RLCK) that triggers
CC abscisic acid (ABA) signaling by phosphorylating and activating ABA
CC receptors (e.g. PYL8/RCAR3 and PYR1/RCAR11), which in turn repress
CC ABI1, a negative regulator of ABA responses (PubMed:29928509). Promotes
CC drought tolerance (PubMed:29970817). {ECO:0000269|PubMed:29928509,
CC ECO:0000269|PubMed:29970817}.
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:Q41328};
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:Q41328};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29928509};
CC -!- SUBUNIT: Interacts with PYL8/RCAR3 and PYR1/RCAR11 in the cytosol.
CC {ECO:0000269|PubMed:29928509}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}.
CC -!- PTM: Autophosphorylated at threonine residues and to a lesser extent at
CC serine residues. {ECO:0000269|PubMed:29928509}.
CC -!- DISRUPTION PHENOTYPE: Impaired kinase activity and reduced plant
CC sensitivity to abscisic acid (ABA). {ECO:0000269|PubMed:29928509}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB022216; BAB02745.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75950.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64774.1; -; Genomic_DNA.
DR EMBL; AY070413; AAL49909.1; -; mRNA.
DR EMBL; AY096595; AAM20245.1; -; mRNA.
DR RefSeq; NP_001326779.1; NM_001338288.1.
DR RefSeq; NP_188367.2; NM_112620.5.
DR PDB; 5XD6; X-ray; 1.90 A; A/B=50-350.
DR PDBsum; 5XD6; -.
DR AlphaFoldDB; Q9LUT0; -.
DR SMR; Q9LUT0; -.
DR IntAct; Q9LUT0; 2.
DR STRING; 3702.AT3G17410.1; -.
DR iPTMnet; Q9LUT0; -.
DR PaxDb; Q9LUT0; -.
DR PRIDE; Q9LUT0; -.
DR ProteomicsDB; 181293; -.
DR EnsemblPlants; AT3G17410.1; AT3G17410.1; AT3G17410.
DR EnsemblPlants; AT3G17410.2; AT3G17410.2; AT3G17410.
DR GeneID; 821005; -.
DR Gramene; AT3G17410.1; AT3G17410.1; AT3G17410.
DR Gramene; AT3G17410.2; AT3G17410.2; AT3G17410.
DR KEGG; ath:AT3G17410; -.
DR Araport; AT3G17410; -.
DR TAIR; locus:2088990; AT3G17410.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9LUT0; -.
DR OMA; CGGEDTQ; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LUT0; -.
DR PRO; PR:Q9LUT0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUT0; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; 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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 3D-structure; Abscisic acid signaling pathway; ATP-binding; Cytoplasm;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..364
FT /note="Receptor-like cytoplasmic kinase 1"
FT /id="PRO_0000447281"
FT DOMAIN 69..349
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 16..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 79
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29928509,
FT ECO:0007744|PDB:5XD6"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:29928509, ECO:0007744|PDB:5XD6"
FT BINDING 142..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29928509,
FT ECO:0007744|PDB:5XD6"
FT BINDING 199..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29928509,
FT ECO:0007744|PDB:5XD6"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29928509,
FT ECO:0007744|PDB:5XD6"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:29928509"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000305|PubMed:29928509"
FT MUTAGEN 204
FT /note="N->A: Impaired interactions with PYL8/RCAR3 and
FT PYR1/RCAR11, and loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 221
FT /note="S->A: Normal autophosphorylation."
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 233
FT /note="S->A: Normal autophosphorylation."
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 234
FT /note="T->A: Reduced autophosphorylation and lower kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:29928509"
FT MUTAGEN 239
FT /note="T->A: Reduced autophosphorylation and lower kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:29928509"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:5XD6"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 170..189
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5XD6"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5XD6"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 314..327
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 338..345
FT /evidence="ECO:0007829|PDB:5XD6"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:5XD6"
SQ SEQUENCE 364 AA; 39562 MW; 62A7FE8F249F332E CRC64;
MGCFGCCGGG EDFRRVSETG PKPVHNTGGY NGGHHQRADP PKNLPVIQMQ PISVAAIPAD
ELRDITDNYG SKSLIGEGSY GRVFYGILKS GKAAAIKKLD SSKQPDQEFL AQVSMVSRLR
QENVVALLGY CVDGPLRVLA YEYAPNGSLH DILHGRKGVK GAQPGPVLSW HQRVKIAVGA
ARGLEYLHEK ANPHVIHRDI KSSNVLLFDD DVAKIADFDL SNQAPDMAAR LHSTRVLGTF
GYHAPEYAMT GTLSTKSDVY SFGVVLLELL TGRKPVDHTL PRGQQSVVTW ATPKLSEDKV
KQCVDARLNG EYPPKAVAKL AAVAALCVQY EADFRPNMSI VVKALQPLLN PPRSAPQTPH
RNPY
