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Calcium/calmodulin-regulated receptor-like kinase 1 (AtCRLK1) (EC 2.7.11.1)

 CRLK1_ARATH             Reviewed;         440 AA.
Q9FIU5; F4K1S6; Q93ZP7;
17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 129.
RecName: Full=Calcium/calmodulin-regulated receptor-like kinase 1 {ECO:0000303|PubMed:21056039};
Short=AtCRLK1 {ECO:0000303|PubMed:21056039};
EC=2.7.11.1 {ECO:0000269|PubMed:20026608};
Name=CRLK1 {ECO:0000303|PubMed:21056039};
OrderedLocusNames=At5g54590 {ECO:0000312|Araport:AT5G54590};
ORFNames=MRB17.9 {ECO:0000312|EMBL:BAB09338.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9872454; DOI=10.1093/dnares/5.5.297;
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VII.
Sequence features of the regions of 1,013,767 bp covered by sixteen
physically assigned P1 and TAC clones.";
DNA Res. 5:297-308(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
GENE FAMILY.
PubMed=21056039; DOI=10.1016/j.febslet.2010.10.059;
DeFalco T.A., Chiasson D., Munro K., Kaiser B.N., Snedden W.A.;
"Characterization of GmCaMK1, a member of a soybean calmodulin-binding
receptor-like kinase family.";
FEBS Lett. 584:4717-4724(2010).
[5]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH CALMODULIN, ACTIVITY
REGULATION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION BY
COLD AND HYDROGEN PEROXIDE, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=20026608; DOI=10.1074/jbc.M109.035659;
Yang T., Chaudhuri S., Yang L., Du L., Poovaiah B.W.;
"A calcium/calmodulin-regulated member of the receptor-like kinase
family confers cold tolerance in plants.";
J. Biol. Chem. 285:7119-7126(2010).
[6]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MEKK1, AND
SUBCELLULAR LOCATION.
PubMed=20724845; DOI=10.4161/psb.5.8.12225;
Yang T., Shad Ali G., Yang L., Du L., Reddy A.S., Poovaiah B.W.;
"Calcium/calmodulin-regulated receptor-like kinase CRLK1 interacts
with MEKK1 in plants.";
Plant Signal. Behav. 5:991-994(2010).
[7]
FUNCTION.
STRAIN=cv. Columbia;
PubMed=23857079; DOI=10.1007/s10265-013-0576-0;
Furuya T., Matsuoka D., Nanmori T.;
"Phosphorylation of Arabidopsis thaliana MEKK1 via Ca(2+) signaling as
a part of the cold stress response.";
J. Plant Res. 126:833-840(2013).
-!- FUNCTION: Required for cold tolerance, via the activation of MAP
kinases activity (PubMed:20026608, PubMed:20724845).
Phosphorylates and activates MEKK1 in response to cold in a
calcium-dependent manner (PubMed:23857079).
{ECO:0000269|PubMed:20026608, ECO:0000269|PubMed:20724845,
ECO:0000269|PubMed:23857079}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20026608}.
-!- ACTIVITY REGULATION: Kinase activity is stimulated by
calcium/calmodulin, but blocked by chlorpromazine.
{ECO:0000269|PubMed:20026608}.
-!- SUBUNIT: Interacts with calmodulin (CaM) in a calcium- (Ca(2+)-)
dependent manner (PubMed:20026608). Binds to MEKK1
(PubMed:20724845). {ECO:0000269|PubMed:20026608,
ECO:0000269|PubMed:20724845}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20026608,
ECO:0000269|PubMed:20724845}; Single-pass membrane protein
{ECO:0000269|PubMed:20026608}. Endosome membrane
{ECO:0000269|PubMed:20724845}; Single-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9FIU5-1; Sequence=Displayed;
Note=Derived from EST data. No experimental confirmation
available. {ECO:0000312|EMBL:AED96515.1};
Name=2;
IsoId=Q9FIU5-2; Sequence=VSP_058096;
Note=Derived from EST data. No experimental confirmation
available. {ECO:0000312|EMBL:AED96514.1};
Name=3;
IsoId=Q9FIU5-3; Sequence=VSP_058095, VSP_058096;
-!- TISSUE SPECIFICITY: Similar transcript expression levels in
seedlings, roots, leaves, stems and flowers,and lower levels in
siliques, but protein accumulates mostly in 7-day-old seedlings,
old roots and young leaves and, to a lower extent, in young roots,
old leaves, flowers and siliques (at protein level).
{ECO:0000269|PubMed:20026608}.
-!- INDUCTION: Differential expression between transcripts and
proteins. Induced transiently by cold and hydrogen peroxide
H(2)O(2) treatments despite stable transcript level (at protein
level). {ECO:0000269|PubMed:20026608}.
-!- DISRUPTION PHENOTYPE: Increased sensitivity to chilling and
freezing temperatures, associated with a delayed induction of
cold-responsive genes (PubMed:20026608, PubMed:20724845). Impaired
MAP kinases activation in response to cold (PubMed:20724845).
{ECO:0000269|PubMed:20026608, ECO:0000269|PubMed:20724845}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; AB016879; BAB09338.1; -; Genomic_DNA.
EMBL; CP002688; AED96514.1; -; Genomic_DNA.
EMBL; CP002688; AED96515.1; -; Genomic_DNA.
EMBL; CP002688; ANM71003.1; -; Genomic_DNA.
EMBL; CP002688; ANM71004.1; -; Genomic_DNA.
EMBL; AY056402; AAL08258.1; -; mRNA.
EMBL; AY081708; AAL87361.1; -; mRNA.
RefSeq; NP_001318798.1; NM_001345091.1. [Q9FIU5-1]
RefSeq; NP_001332565.1; NM_001345092.1. [Q9FIU5-1]
RefSeq; NP_568809.2; NM_124840.3. [Q9FIU5-1]
RefSeq; NP_851189.1; NM_180858.1. [Q9FIU5-2]
UniGene; At.26329; -.
ProteinModelPortal; Q9FIU5; -.
SMR; Q9FIU5; -.
STRING; 3702.AT5G54590.2; -.
PaxDb; Q9FIU5; -.
EnsemblPlants; AT5G54590.1; AT5G54590.1; AT5G54590. [Q9FIU5-2]
EnsemblPlants; AT5G54590.2; AT5G54590.2; AT5G54590. [Q9FIU5-1]
EnsemblPlants; AT5G54590.3; AT5G54590.3; AT5G54590. [Q9FIU5-1]
EnsemblPlants; AT5G54590.4; AT5G54590.4; AT5G54590. [Q9FIU5-1]
GeneID; 835548; -.
Gramene; AT5G54590.1; AT5G54590.1; AT5G54590. [Q9FIU5-2]
Gramene; AT5G54590.2; AT5G54590.2; AT5G54590. [Q9FIU5-1]
Gramene; AT5G54590.3; AT5G54590.3; AT5G54590. [Q9FIU5-1]
Gramene; AT5G54590.4; AT5G54590.4; AT5G54590. [Q9FIU5-1]
KEGG; ath:AT5G54590; -.
Araport; AT5G54590; -.
TAIR; locus:2172149; AT5G54590.
eggNOG; KOG1187; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000116550; -.
InParanoid; Q9FIU5; -.
OMA; HMLLYAY; -.
OrthoDB; EOG09360DDU; -.
PhylomeDB; Q9FIU5; -.
PRO; PR:Q9FIU5; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FIU5; baseline and differential.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0009631; P:cold acclimation; IDA:UniProtKB.
GO; GO:0009409; P:response to cold; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calmodulin-binding; Cell membrane;
Complete proteome; Endosome; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 440 Calcium/calmodulin-regulated receptor-
like kinase 1.
/FTId=PRO_0000435446.
TRANSMEM 8 28 Helical. {ECO:0000255}.
DOMAIN 113 380 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 119 127 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 28 228 Calmodulin binding.
{ECO:0000269|PubMed:20026608}.
REGION 369 440 Calmodulin binding.
{ECO:0000269|PubMed:20026608}.
COMPBIAS 393 404 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
ACT_SITE 237 237 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 141 141 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 186 186 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 274 274 Phosphothreonine.
{ECO:0000250|UniProtKB:O48814}.
MOD_RES 282 282 Phosphotyrosine.
{ECO:0000250|UniProtKB:O48814}.
VAR_SEQ 1 62 Missing (in isoform 3).
/FTId=VSP_058095.
VAR_SEQ 229 439 AVPPVIHRDIKSSNILLDQSMRARVADFGLSREEMVDKHAA
NIRGTFGYLDPEYISTRTFTKKSDVYGFGVLLFELIAGRNP
QQGLMELVELAAMNAEEKVGWEEIVDSRLDGRYDLQEVNEV
AAFAYKCISRAPRKRPNMRDIVQVLTRVIKVRHCRKRQKNS
PSPSPRLPPPPPIVEESEGELTANGSLRSEIHRRDNSLDSS
IAEDVI -> VSCLLKPFTILMHLLNNNFKTHVLINCSRLF
L (in isoform 2 and isoform 3).
/FTId=VSP_058096.
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


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