CRK36_ARATH
ID CRK36_ARATH Reviewed; 658 AA.
AC Q9XEC6;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 36 {ECO:0000305};
DE Short=Cysteine-rich RLK36 {ECO:0000303|PubMed:11402176};
DE EC=2.7.11.1 {ECO:0000269|PubMed:22225700};
DE Flags: Precursor;
GN Name=CRK36 {ECO:0000303|PubMed:11402176}; OrderedLocusNames=At4g04490;
GN ORFNames=T26N6.10;
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 GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11402176; DOI=10.1104/pp.126.2.473;
RA Chen Z.;
RT "A superfamily of proteins with novel cysteine-rich repeats.";
RL Plant Physiol. 126:473-476(2001).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CRK45, SUBCELLULAR LOCATION,
RP INDUCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-368.
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).
CC -!- FUNCTION: Forms a complex with CRK45 that may negatively control
CC abscisic acid (ABA) and osmotic stress signal transduction. Can
CC phosphorylate CRK45 in vitro (PubMed:22225700).
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 CRK45. {ECO:0000269|PubMed:22225700}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22225700};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: By ozone and light stress (PubMed:20500828). Induced by salt
CC stress, drought stress and abscisic acid (ABA) (PubMed:22225700).
CC {ECO:0000269|PubMed:20500828, ECO:0000269|PubMed:22225700}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:22225700}.
CC -!- MISCELLANEOUS: Seedlings silencing CRK36 show increased sensitivity to
CC abscisic acid (ABA) and salt stress during post-germinative growth.
CC {ECO:0000269|PubMed:22225700}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AF076243; AAD29761.1; -; Genomic_DNA.
DR EMBL; AL161500; CAB77917.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82394.1; -; Genomic_DNA.
DR RefSeq; NP_192358.1; NM_116687.2.
DR AlphaFoldDB; Q9XEC6; -.
DR SMR; Q9XEC6; -.
DR BioGRID; 11090; 2.
DR STRING; 3702.AT4G04490.1; -.
DR PaxDb; Q9XEC6; -.
DR PRIDE; Q9XEC6; -.
DR ProteomicsDB; 224416; -.
DR EnsemblPlants; AT4G04490.1; AT4G04490.1; AT4G04490.
DR GeneID; 825779; -.
DR Gramene; AT4G04490.1; AT4G04490.1; AT4G04490.
DR KEGG; ath:AT4G04490; -.
DR Araport; AT4G04490; -.
DR TAIR; locus:2137134; AT4G04490.
DR eggNOG; ENOG502SE86; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; Q9XEC6; -.
DR OMA; WDSENDA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9XEC6; -.
DR PRO; PR:Q9XEC6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XEC6; baseline and differential.
DR Genevisible; Q9XEC6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR Gene3D; 3.30.430.20; -; 2.
DR InterPro; IPR002902; GNK2.
DR InterPro; IPR038408; GNK2_sf.
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 Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51473; GNK2; 2.
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; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Stress response; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..658
FT /note="Cysteine-rich receptor-like protein kinase 36"
FT /id="PRO_0000295083"
FT TOPO_DOM 27..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..128
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 139..246
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 340..612
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 465
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 346..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 413
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 513
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 368
FT /note="K->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:22225700"
SQ SEQUENCE 658 AA; 74978 MW; A31CDC032BA1B788 CRC64;
MERSNLFHIP CFLLLFLLFN INGVHTTFVC GDEDFSPNTS YVENLESLLP SLASNVIRER
GFYNVSLDGV YALALCRKHY EVQACRRCVD RASRTLLTQC RGKTEAYHWD SENDANVSCL
VRYSNIHRFG KLKLEPIGNV PHSSLDPSSN LTRISQEFAA RANRTVEVAS TADESSVLKY
YGVSSAEFTD TPEVNMLMQC TPDLSSSDCN HCLRENVRYN QEHNWDRVGG TVARPSCYFR
WDDYRFAGAF DNLERVPAPP RSPQTRQDYR VKKGRMFQPW SVVVVVFPTG INLAVFVAFV
LAYRRMRRRI YTEINKNSDS DGQATLRFDL GMILIATNEF SLENKLGQGG FGSVYKGILP
SGQEIAVKRL AGGSGQGELE FKNEVLLLTR LQHRNLVKLL GFCNEGNEEI LVYEHVPNSS
LDHFIFDEDK RWLLTWDVRY RIIEGVARGL LYLHEDSQLR IIHRDLKASN ILLDAEMNPK
VADFGMARLF NMDETRGETS RVVGTYGYMA PEYVRHGQFS AKSDVYSFGV MLLEMISGEK
NKNFETEGLP AFAWKRWIEG ELESIIDPYL NENPRNEIIK LIQIGLLCVQ ENAAKRPTMN
SVITWLARDG TFTIPKPTEA AFVTLPLSVK PENRSMSERK DKDPFSVDEV SITVLYPR
