CRLK1_ARATH
ID CRLK1_ARATH Reviewed; 440 AA.
AC Q9FIU5; F4K1S6; Q93ZP7;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Calcium/calmodulin-regulated receptor-like kinase 1 {ECO:0000303|PubMed:21056039};
DE Short=AtCRLK1 {ECO:0000303|PubMed:21056039};
DE EC=2.7.11.1 {ECO:0000269|PubMed:20026608};
GN Name=CRLK1 {ECO:0000303|PubMed:21056039};
GN OrderedLocusNames=At5g54590 {ECO:0000312|Araport:AT5G54590};
GN ORFNames=MRB17.9 {ECO:0000312|EMBL:BAB09338.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(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] (ISOFORM 3).
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 GENE FAMILY.
RX PubMed=21056039; DOI=10.1016/j.febslet.2010.10.059;
RA DeFalco T.A., Chiasson D., Munro K., Kaiser B.N., Snedden W.A.;
RT "Characterization of GmCaMK1, a member of a soybean calmodulin-binding
RT receptor-like kinase family.";
RL FEBS Lett. 584:4717-4724(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CALMODULIN, ACTIVITY
RP REGULATION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY COLD AND
RP HYDROGEN PEROXIDE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=20026608; DOI=10.1074/jbc.m109.035659;
RA Yang T., Chaudhuri S., Yang L., Du L., Poovaiah B.W.;
RT "A calcium/calmodulin-regulated member of the receptor-like kinase family
RT confers cold tolerance in plants.";
RL J. Biol. Chem. 285:7119-7126(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MEKK1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20724845; DOI=10.4161/psb.5.8.12225;
RA Yang T., Shad Ali G., Yang L., Du L., Reddy A.S., Poovaiah B.W.;
RT "Calcium/calmodulin-regulated receptor-like kinase CRLK1 interacts with
RT MEKK1 in plants.";
RL Plant Signal. Behav. 5:991-994(2010).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=23857079; DOI=10.1007/s10265-013-0576-0;
RA Furuya T., Matsuoka D., Nanmori T.;
RT "Phosphorylation of Arabidopsis thaliana MEKK1 via Ca(2+) signaling as a
RT part of the cold stress response.";
RL J. Plant Res. 126:833-840(2013).
CC -!- FUNCTION: Required for cold tolerance, via the activation of MAP
CC kinases activity (PubMed:20026608, PubMed:20724845). Phosphorylates and
CC activates MEKK1 in response to cold in a calcium-dependent manner
CC (PubMed:23857079). {ECO:0000269|PubMed:20026608,
CC ECO:0000269|PubMed:20724845, ECO:0000269|PubMed:23857079}.
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:0000269|PubMed:20026608};
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:0000269|PubMed:20026608};
CC -!- ACTIVITY REGULATION: Kinase activity is stimulated by
CC calcium/calmodulin, but blocked by chlorpromazine.
CC {ECO:0000269|PubMed:20026608}.
CC -!- SUBUNIT: Interacts with calmodulin (CaM) in a calcium- (Ca(2+)-)
CC dependent manner (PubMed:20026608). Binds to MEKK1 (PubMed:20724845).
CC {ECO:0000269|PubMed:20026608, ECO:0000269|PubMed:20724845}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20026608,
CC ECO:0000269|PubMed:20724845}; Single-pass membrane protein
CC {ECO:0000269|PubMed:20026608}. Endosome membrane
CC {ECO:0000269|PubMed:20724845}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FIU5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FIU5-2; Sequence=VSP_058096;
CC Name=3;
CC IsoId=Q9FIU5-3; Sequence=VSP_058095, VSP_058096;
CC -!- TISSUE SPECIFICITY: Similar transcript expression levels in seedlings,
CC roots, leaves, stems and flowers, and lower levels in siliques, but
CC protein accumulates mostly in 7-day-old seedlings, old roots and young
CC leaves and, to a lower extent, in young roots, old leaves, flowers and
CC siliques (at protein level). {ECO:0000269|PubMed:20026608}.
CC -!- INDUCTION: Differential expression between transcripts and proteins.
CC Induced transiently by cold and hydrogen peroxide H(2)O(2) treatments
CC despite stable transcript level (at protein level).
CC {ECO:0000269|PubMed:20026608}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to chilling and freezing
CC temperatures, associated with a delayed induction of cold-responsive
CC genes (PubMed:20026608, PubMed:20724845). Impaired MAP kinases
CC activation in response to cold (PubMed:20724845).
CC {ECO:0000269|PubMed:20026608, ECO:0000269|PubMed:20724845}.
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; AB016879; BAB09338.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96514.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96515.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71003.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71004.1; -; Genomic_DNA.
DR EMBL; AY056402; AAL08258.1; -; mRNA.
DR EMBL; AY081708; AAL87361.1; -; mRNA.
DR RefSeq; NP_001318798.1; NM_001345091.1. [Q9FIU5-1]
DR RefSeq; NP_001332565.1; NM_001345092.1. [Q9FIU5-1]
DR RefSeq; NP_568809.2; NM_124840.3. [Q9FIU5-1]
DR RefSeq; NP_851189.1; NM_180858.1. [Q9FIU5-2]
DR AlphaFoldDB; Q9FIU5; -.
DR SMR; Q9FIU5; -.
DR STRING; 3702.AT5G54590.2; -.
DR PaxDb; Q9FIU5; -.
DR PRIDE; Q9FIU5; -.
DR ProteomicsDB; 224408; -. [Q9FIU5-1]
DR EnsemblPlants; AT5G54590.1; AT5G54590.1; AT5G54590. [Q9FIU5-2]
DR EnsemblPlants; AT5G54590.2; AT5G54590.2; AT5G54590. [Q9FIU5-1]
DR EnsemblPlants; AT5G54590.3; AT5G54590.3; AT5G54590. [Q9FIU5-1]
DR EnsemblPlants; AT5G54590.4; AT5G54590.4; AT5G54590. [Q9FIU5-1]
DR GeneID; 835548; -.
DR Gramene; AT5G54590.1; AT5G54590.1; AT5G54590. [Q9FIU5-2]
DR Gramene; AT5G54590.2; AT5G54590.2; AT5G54590. [Q9FIU5-1]
DR Gramene; AT5G54590.3; AT5G54590.3; AT5G54590. [Q9FIU5-1]
DR Gramene; AT5G54590.4; AT5G54590.4; AT5G54590. [Q9FIU5-1]
DR KEGG; ath:AT5G54590; -.
DR Araport; AT5G54590; -.
DR TAIR; locus:2172149; AT5G54590.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q9FIU5; -.
DR OMA; SFWLEGF; -.
DR PhylomeDB; Q9FIU5; -.
DR PRO; PR:Q9FIU5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIU5; baseline and differential.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045271; SRF-like.
DR PANTHER; PTHR27001; PTHR27001; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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; Calmodulin-binding; Cell membrane;
KW Endosome; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..440
FT /note="Calcium/calmodulin-regulated receptor-like kinase 1"
FT /id="PRO_0000435446"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 113..380
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 28..228
FT /note="Calmodulin binding"
FT /evidence="ECO:0000269|PubMed:20026608"
FT REGION 369..440
FT /note="Calmodulin binding"
FT /evidence="ECO:0000269|PubMed:20026608"
FT REGION 386..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 237
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 119..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 186
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 282
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 3)"
FT /id="VSP_058095"
FT VAR_SEQ 229..439
FT /note="AVPPVIHRDIKSSNILLDQSMRARVADFGLSREEMVDKHAANIRGTFGYLDP
FT EYISTRTFTKKSDVYGFGVLLFELIAGRNPQQGLMELVELAAMNAEEKVGWEEIVDSRL
FT DGRYDLQEVNEVAAFAYKCISRAPRKRPNMRDIVQVLTRVIKVRHCRKRQKNSPSPSPR
FT LPPPPPIVEESEGELTANGSLRSEIHRRDNSLDSSIAEDVI -> VSCLLKPFTILMHL
FT LNNNFKTHVLINCSRLFL (in isoform 2 and isoform 3)"
FT /id="VSP_058096"
SQ SEQUENCE 440 AA; 48970 MW; 4135F239893B81CA CRC64;
MEGESKGLIV GISLGLVIGV VLAISALFCF RYHRKKSQIV NSGSRRSATI PIRENGADSC
NIMSDSTIGP DSPVKSSKNG RSVWLEGFSK RSNVISASGI LEYSYRDLQK ATCNFTTLIG
QGAFGPVYKA QMSTGEIVAV KVLATDSKQG EKEFQTEVML LGRLHHRNLV NLIGYCAEKG
QHMLIYVYMS KGSLASHLYS EKHEPLSWDL RVYIALDVAR GLEYLHDGAV PPVIHRDIKS
SNILLDQSMR ARVADFGLSR EEMVDKHAAN IRGTFGYLDP EYISTRTFTK KSDVYGFGVL
LFELIAGRNP QQGLMELVEL AAMNAEEKVG WEEIVDSRLD GRYDLQEVNE VAAFAYKCIS
RAPRKRPNMR DIVQVLTRVI KVRHCRKRQK NSPSPSPRLP PPPPIVEESE GELTANGSLR
SEIHRRDNSL DSSIAEDVIL
