CRK20_ARATH
ID CRK20_ARATH Reviewed; 666 AA.
AC O65479; F4JNH5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Putative cysteine-rich receptor-like protein kinase 20;
DE Short=Cysteine-rich RLK20;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK20; OrderedLocusNames=At4g23280; ORFNames=F21P8.170;
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 INDUCTION.
RX PubMed=11100776; DOI=10.1093/pcp/pcd028;
RA Ohtake Y., Takahashi T., Komeda Y.;
RT "Salicylic acid induces the expression of a number of receptor-like kinase
RT genes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 41:1038-1044(2000).
RN [4]
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 [5]
RP INDUCTION.
RX PubMed=15604743; DOI=10.1007/s11103-004-3381-2;
RA Chen K., Fan B., Du L., Chen Z.;
RT "Activation of hypersensitive cell death by pathogen-induced receptor-like
RT protein kinases from Arabidopsis.";
RL Plant Mol. Biol. 56:271-283(2004).
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;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By salicylic acid (SA) or by a bacterial pathogen infection.
CC {ECO:0000269|PubMed:11100776, ECO:0000269|PubMed:15604743}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL022347; CAA18475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79283.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84733.2; -; Genomic_DNA.
DR PIR; T04845; T04845.
DR RefSeq; NP_001320044.1; NM_001341595.1.
DR AlphaFoldDB; O65479; -.
DR SMR; O65479; -.
DR STRING; 3702.AT4G23280.1; -.
DR iPTMnet; O65479; -.
DR PaxDb; O65479; -.
DR PRIDE; O65479; -.
DR ProteomicsDB; 222681; -.
DR EnsemblPlants; AT4G23280.1; AT4G23280.1; AT4G23280.
DR GeneID; 828427; -.
DR Gramene; AT4G23280.1; AT4G23280.1; AT4G23280.
DR KEGG; ath:AT4G23280; -.
DR Araport; AT4G23280; -.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; O65479; -.
DR OrthoDB; 345452at2759; -.
DR PhylomeDB; O65479; -.
DR PRO; PR:O65479; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65479; baseline and differential.
DR Genevisible; O65479; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..666
FT /note="Putative cysteine-rich receptor-like protein kinase
FT 20"
FT /id="PRO_0000295067"
FT TOPO_DOM 24..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..131
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 137..241
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 344..623
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 350..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 417
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 517
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 666 AA; 74058 MW; 0225F9093C86EF0D CRC64;
MSSLICFIFL FLFSFITSFT ASAQNPFYLY HNCSITTTYS SNSTYSTNLK TLLSSLSSRN
ASYSTGFQNA TAGQAPDMVT GLFLCRGNVS PEVCRSCIAL SVNESLSRCP NEREAVFYYE
QCMLRYSNRN ILSTLNTDGG VFMQNARNPI SVKQDRFRDL VLNPMNLAAI EAARSIKRFA
VTKFDLNALQ SLYGMVQCTP DLTEQDCLDC LQQSINQVTY DKIGGRTFLP SCTSRYDNYE
FYNEFNVGTP QDSSPRPGKG GNSSVIVIAV VVPITVLFLL FVAFFSVRRA KRKKTIGAIP
LFKVKRKETE VTEPPAETTD GDDITTAGSL QFDFKAIVAA TDIFLPINKL GQGGFGEVYK
GTFPSGVQVA VKRLSKNSGQ GEKEFENEVV VVAKLQHRNL VKLLGYCLEG EEKILVYEFV
PNKSLDYFLF DPTMQGQLDW SRRYKIIGGI ARGILYLHQD SRLTIIHRDL KAGNILLDAD
MNPKVADFGM ARIFGMDQTE ANTRRVVGTY GYMAPEYAMY GKFSMKSDVY SFGVLVLEIV
SGMKNSSLDQ MDGSISNLVT YTWRLWSNGS PSELVDPSFG DNYQTSEITR CIHIALLCVQ
EDANDRPTMS AIVQMLTTSS IALAVPRPPG FFLRSKQEQA ERACPSMDTS DLFSIDEASI
TSVAPR
