CRK45_ARATH
ID CRK45_ARATH Reviewed; 351 AA.
AC Q8GY82; Q9T057;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 45 {ECO:0000305};
DE Short=Cysteine-rich RLK45 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22225700};
DE AltName: Full=ABA- and osmotic stress-inducible receptor-like cytosolic kinase 1 {ECO:0000303|PubMed:22225700};
GN Name=CRK45 {ECO:0000303|PubMed:20500828};
GN Synonyms=ARCK1 {ECO:0000303|PubMed:22225700};
GN OrderedLocusNames=At4g11890 {ECO:0000312|Araport:AT4G11890};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 INDUCTION.
RX PubMed=20500828; DOI=10.1186/1471-2229-10-95;
RA Wrzaczek M., Brosche M., Salojarvi J., Kangasjarvi S., Idanheimo N.,
RA Mersmann S., Robatzek S., Karpinski S., Karpinska B., Kangasjarvi J.;
RT "Transcriptional regulation of the CRK/DUF26 group of receptor-like protein
RT kinases by ozone and plant hormones in Arabidopsis.";
RL BMC Plant Biol. 10:95-95(2010).
RN [6]
RP INDUCTION.
RX PubMed=21711359; DOI=10.1111/j.1365-3040.2011.02390.x;
RA Hok S., Danchin E.G., Allasia V., Panabieres F., Attard A., Keller H.;
RT "An Arabidopsis (malectin-like) leucine-rich repeat receptor-like kinase
RT contributes to downy mildew disease.";
RL Plant Cell Environ. 34:1944-1957(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CRK36, SUBCELLULAR LOCATION,
RP INDUCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-65 AND 180-GLY--GLU-182,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=22225700; DOI=10.1111/j.1365-313x.2012.04901.x;
RA Tanaka H., Osakabe Y., Katsura S., Mizuno S., Maruyama K., Kusakabe K.,
RA Mizoi J., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Abiotic stress-inducible receptor-like kinases negatively control ABA
RT signaling in Arabidopsis.";
RL Plant J. 70:599-613(2012).
RN [8]
RP FUNCTION.
RX PubMed=23583936; DOI=10.1016/j.plaphy.2013.03.013;
RA Zhang X., Yang G., Shi R., Han X., Qi L., Wang R., Xiong L., Li G.;
RT "Arabidopsis cysteine-rich receptor-like kinase 45 functions in the
RT responses to abscisic acid and abiotic stresses.";
RL Plant Physiol. Biochem. 67:189-198(2013).
RN [9]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24215930; DOI=10.1016/j.plaphy.2013.10.024;
RA Zhang X., Han X., Shi R., Yang G., Qi L., Wang R., Li G.;
RT "Arabidopsis cysteine-rich receptor-like kinase 45 positively regulates
RT disease resistance to Pseudomonas syringae.";
RL Plant Physiol. Biochem. 73:383-391(2013).
CC -!- FUNCTION: Forms a complex with CRK36 that may negatively control
CC abscisic acid (ABA) and osmotic stress signal transduction
CC (PubMed:22225700). Involved in plant response to ABA during seed
CC germination, early seedling growth and responses to abiotic stresses by
CC inducing the expression of ABA-responsive genes and stress-inducible
CC genes (PubMed:23583936). Acts as positive regulator in disease
CC resistance, downstream of NPR1 and WRKY70 (PubMed:24215930).
CC {ECO:0000269|PubMed:22225700, ECO:0000269|PubMed:23583936,
CC ECO:0000269|PubMed:24215930}.
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:22225700};
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:22225700};
CC -!- SUBUNIT: Interacts with CRK36. {ECO:0000269|PubMed:22225700}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:22225700}.
CC Note=Interacts with CRK36 at the cell surface.
CC {ECO:0000269|PubMed:22225700}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GY82-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GY82-2; Sequence=VSP_057613;
CC -!- INDUCTION: By ozone. Down-regulated by light stress (PubMed:20500828).
CC Induced by infection with Hyaloperonospora arabidopsidis
CC (PubMed:21711359). Induced by salt stress, drought stress and abscisic
CC acid (ABA) (PubMed:22225700). Induced by salicylic acid (SA) and
CC infection with the bacterial pathogen P.syringae and the necrotrophic
CC fungal pathogen B.cinerea (PubMed:24215930).
CC {ECO:0000269|PubMed:20500828, ECO:0000269|PubMed:21711359,
CC ECO:0000269|PubMed:22225700, ECO:0000269|PubMed:24215930}.
CC -!- PTM: Autophosphorylated and phosphorylated by CRK36.
CC {ECO:0000269|PubMed:22225700}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant seedlings show increased sensitivity to abscisic
CC acid (ABA) and salt stress during post-germinative growth
CC (PubMed:22225700). Increased susceptibility to P.syringae infection.
CC Weak expression of pathogenesis-related (PR) genes after infection with
CC P.syringae or salicylic acid (SA) treatment (PubMed:24215930).
CC {ECO:0000269|PubMed:22225700, ECO:0000269|PubMed:24215930}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000305}.
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DR EMBL; AL078606; CAB44327.1; -; Genomic_DNA.
DR EMBL; AL161533; CAB78232.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83063.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83065.1; -; Genomic_DNA.
DR EMBL; BT006243; AAP12892.1; -; mRNA.
DR EMBL; AK117801; BAC42446.1; -; mRNA.
DR PIR; T09348; T09348.
DR RefSeq; NP_192926.1; NM_117259.4. [Q8GY82-2]
DR RefSeq; NP_849362.1; NM_179031.2. [Q8GY82-1]
DR AlphaFoldDB; Q8GY82; -.
DR SMR; Q8GY82; -.
DR IntAct; Q8GY82; 5.
DR STRING; 3702.AT4G11890.3; -.
DR iPTMnet; Q8GY82; -.
DR PaxDb; Q8GY82; -.
DR PRIDE; Q8GY82; -.
DR ProteomicsDB; 224553; -. [Q8GY82-1]
DR EnsemblPlants; AT4G11890.1; AT4G11890.1; AT4G11890. [Q8GY82-1]
DR EnsemblPlants; AT4G11890.2; AT4G11890.2; AT4G11890. [Q8GY82-2]
DR GeneID; 826796; -.
DR Gramene; AT4G11890.1; AT4G11890.1; AT4G11890. [Q8GY82-1]
DR Gramene; AT4G11890.2; AT4G11890.2; AT4G11890. [Q8GY82-2]
DR KEGG; ath:AT4G11890; -.
DR Araport; AT4G11890; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR OMA; SWEMCRN; -.
DR PhylomeDB; Q8GY82; -.
DR PRO; PR:Q8GY82; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GY82; baseline and differential.
DR Genevisible; Q8GY82; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031349; P:positive regulation of defense response; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP: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; Kinase; Nucleotide-binding;
KW Phosphoprotein; Plant defense; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase.
FT CHAIN 1..351
FT /note="Cysteine-rich receptor-like protein kinase 45"
FT /id="PRO_0000432854"
FT DOMAIN 37..287
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 110
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 210
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT VAR_SEQ 24
FT /note="F -> SV (in isoform 2)"
FT /id="VSP_057613"
FT MUTAGEN 65
FT /note="K->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:22225700"
FT MUTAGEN 180..182
FT /note="GFE->DFG: Constitutively active form."
FT /evidence="ECO:0000269|PubMed:22225700"
SQ SEQUENCE 351 AA; 40231 MW; 9979DDF959A89466 CRC64;
MAVTSLLDTV FRRRKKKSTE FISFFEFDLD TIKAATNDFS ELVGRGGFGF VYKGRLQNGQ
EIAVKILSTS SIRTERQFHN ELIILSKLKH KNLINLLGFC TKRDQHGLVY EFMPNSSLDC
FILDPHRAAQ LNWEMCRNII DGIARGLRYL HEESGLWVVH RDIKPGNILL DSDLKPKIVG
FELARTMQQG ENAAETTEIV GTVGYLDPEY IRSGRVSVKS DVYAFGVTIL TIISRRKAWS
VDGDSLIKYV RRCWNRGEAI DVIHEVMREE EREYSISEIL RYIHIALLCV DENAERRPNI
DKVLHWFSCF STPLPDPTFG NRFLVEEETN WPWSPSLSPG HSSVTSPISS R
