ID CRCK1_ARATH Reviewed; 470 AA.
AC Q9FIL7; Q5YCZ4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Calmodulin-binding receptor-like cytoplasmic kinase 1;
DE EC=2.7.11.1;
GN Name=CRCK1; OrderedLocusNames=At5g58940; ORFNames=K19M22.13;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-470, INTERACTION WITH CALMODULIN,
RP AUTOPHOSPHORYLATION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP COFACTOR, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=15292241; DOI=10.1074/jbc.m402830200;
RA Yang T., Chaudhuri S., Yang L., Chen Y., Poovaiah B.W.;
RT "Calcium/calmodulin up-regulates a cytoplasmic receptor-like kinase in
RT plants.";
RL J. Biol. Chem. 279:42552-42559(2004).
RN [5]
RP GENE FAMILY.
RX PubMed=12805585; DOI=10.1104/pp.103.021964;
RA Shiu S.H., Bleecker A.B.;
RT "Expansion of the receptor-like kinase/Pelle gene family and receptor-like
RT proteins in Arabidopsis.";
RL Plant Physiol. 132:530-543(2003).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15292241};
CC -!- ACTIVITY REGULATION: Up-regulated by Ca(2+)/CaM.
CC {ECO:0000269|PubMed:15292241}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for ATP with or without CaM {ECO:0000269|PubMed:15292241};
CC Vmax=33.6 pmol/min/mg enzyme toward ATP without CaM
CC {ECO:0000269|PubMed:15292241};
CC Vmax=289 pmol/min/mg enzyme toward ATP with CaM
CC {ECO:0000269|PubMed:15292241};
CC -!- SUBUNIT: Interacts with calmodulin (CaM) in a Ca(2+)-dependent manner.
CC {ECO:0000269|PubMed:15292241}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By cold, salt, abscisic acid (ABA) and hydrogen peroxide.
CC {ECO:0000269|PubMed:15292241}.
CC -!- PTM: Autophosphorylated.
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; AB016885; BAB09637.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97119.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70474.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70475.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70476.1; -; Genomic_DNA.
DR EMBL; BT015092; AAT71964.1; -; mRNA.
DR EMBL; BT015906; AAU95442.1; -; mRNA.
DR EMBL; AY568379; AAT71312.1; -; mRNA.
DR RefSeq; NP_001318835.1; NM_001345330.1.
DR RefSeq; NP_001332082.1; NM_001345331.1.
DR RefSeq; NP_001332083.1; NM_001345332.1.
DR RefSeq; NP_200702.2; NM_125284.4.
DR AlphaFoldDB; Q9FIL7; -.
DR SMR; Q9FIL7; -.
DR BioGRID; 21255; 1.
DR STRING; 3702.Q9FIL7; -.
DR PaxDb; 3702-AT5G58940-1; -.
DR EnsemblPlants; AT5G58940.1; AT5G58940.1; AT5G58940.
DR EnsemblPlants; AT5G58940.2; AT5G58940.2; AT5G58940.
DR EnsemblPlants; AT5G58940.3; AT5G58940.3; AT5G58940.
DR EnsemblPlants; AT5G58940.4; AT5G58940.4; AT5G58940.
DR GeneID; 836011; -.
DR Gramene; AT5G58940.1; AT5G58940.1; AT5G58940.
DR Gramene; AT5G58940.2; AT5G58940.2; AT5G58940.
DR Gramene; AT5G58940.3; AT5G58940.3; AT5G58940.
DR Gramene; AT5G58940.4; AT5G58940.4; AT5G58940.
DR KEGG; ath:AT5G58940; -.
DR Araport; AT5G58940; -.
DR TAIR; AT5G58940; CRCK1.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9FIL7; -.
DR OMA; ECAEVLW; -.
DR OrthoDB; 1217857at2759; -.
DR PhylomeDB; Q9FIL7; -.
DR SABIO-RK; Q9FIL7; -.
DR PRO; PR:Q9FIL7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIL7; baseline and differential.
DR Genevisible; Q9FIL7; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0004683; F:calmodulin-dependent 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; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR CDD; cd14066; STKc_IRAK; 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; PTHR47989:SF35; LRR RECEPTOR-LIKE SERINE_THREONINE-PROTEIN KINASE RKF3-RELATED; 1.
DR PANTHER; PTHR47989; OS01G0750732 PROTEIN; 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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..470
FT /note="Calmodulin-binding receptor-like cytoplasmic kinase
FT 1"
FT /id="PRO_0000420412"
FT DOMAIN 147..423
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..185
FT /note="CaM-binding"
FT COMPBIAS 79..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 153..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 322
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
SQ SEQUENCE 470 AA; 52879 MW; 89943F226E9C584C CRC64;
MPMRSKTPTP LRFSNGKHQR DDSEYSWTDV GTGEKARNVS VLGAIRRAAK KVFVIIFLGQ
RKLKPTECRS DPGESSTHDR ESTLSGWTGY SSPSSFGRST ERKVSGQYRF SGSRFQSPGK
DSSSSKSWHQ GPVIFSFGEL QRATANFSSV HQIGEGGFGT VFKGKLDDGT IVAIKRARKN
NYGKSWLLEF KNEIYTLSKI EHMNLVKLYG FLEHGDEKVI VVEYVANGNL REHLDGLRGN
RLEMAERLEI AIDVAHALTY LHTYTDSPII HRDIKASNIL ITNKLRAKVA DFGFARLVSE
DLGATHISTQ VKGSAGYVDP DYLRTFQLTD KSDVYSFGVL LVEILTGRRP IELKRPRKDR
LTVKWALRRL KDDEAVLIMD PFLKRNRAAI EVAEKMLRLA SECVTPTRAT RPAMKGIAEK
LWAIRREMKE TMICSSASNS SCSSTTHSFI GRDSDRYALP RIEDNENSIE
//
