CRK19_ARATH
ID CRK19_ARATH Reviewed; 645 AA.
AC Q8GWJ7; O65478;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 19;
DE Short=Cysteine-rich RLK19;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK19; OrderedLocusNames=At4g23270; ORFNames=F21P8.160;
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 2).
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 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).
RN [6]
RP INTERACTION WITH MWL1.
RC STRAIN=cv. Columbia;
RX PubMed=26930070; DOI=10.1371/journal.pone.0150254;
RA Mewalal R., Mizrachi E., Coetzee B., Mansfield S.D., Myburg A.A.;
RT "The Arabidopsis domain of unknown function 1218 (DUF1218) containing
RT proteins, MODIFYING WALL LIGNIN-1 and 2 (At1g31720/MWL-1 and At4g19370/MWL-
RT 2) function redundantly to alter secondary cell wall lignin content.";
RL PLoS ONE 11:E0150254-E0150254(2016).
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 -!- SUBUNIT: Interacts with MWL1. {ECO:0000269|PubMed:26930070}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GWJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GWJ7-2; Sequence=VSP_026693, VSP_026694;
CC -!- INDUCTION: By salicylic acid (SA) or by a bacterial pathogen infection.
CC {ECO:0000269|PubMed:15604743}.
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:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18474.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL022347; CAA18474.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161559; CAB79282.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84731.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67713.1; -; Genomic_DNA.
DR EMBL; AK118799; BAC43390.1; -; mRNA.
DR PIR; T04844; T04844.
DR RefSeq; NP_001329528.1; NM_001341593.1. [Q8GWJ7-1]
DR RefSeq; NP_194058.2; NM_118456.3. [Q8GWJ7-1]
DR AlphaFoldDB; Q8GWJ7; -.
DR SMR; Q8GWJ7; -.
DR BioGRID; 13715; 24.
DR IntAct; Q8GWJ7; 24.
DR STRING; 3702.AT4G23270.1; -.
DR iPTMnet; Q8GWJ7; -.
DR PaxDb; Q8GWJ7; -.
DR PRIDE; Q8GWJ7; -.
DR ProteomicsDB; 220451; -. [Q8GWJ7-1]
DR EnsemblPlants; AT4G23270.1; AT4G23270.1; AT4G23270. [Q8GWJ7-1]
DR EnsemblPlants; AT4G23270.2; AT4G23270.2; AT4G23270. [Q8GWJ7-1]
DR GeneID; 828426; -.
DR Gramene; AT4G23270.1; AT4G23270.1; AT4G23270. [Q8GWJ7-1]
DR Gramene; AT4G23270.2; AT4G23270.2; AT4G23270. [Q8GWJ7-1]
DR KEGG; ath:AT4G23270; -.
DR Araport; AT4G23270; -.
DR TAIR; locus:2121686; AT4G23270.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_3_1; -.
DR InParanoid; Q8GWJ7; -.
DR OMA; QDDYQTN; -.
DR PhylomeDB; Q8GWJ7; -.
DR PRO; PR:Q8GWJ7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GWJ7; baseline and differential.
DR Genevisible; Q8GWJ7; 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; IEP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009751; P:response to salicylic acid; IEP: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 Alternative splicing; ATP-binding; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..645
FT /note="Cysteine-rich receptor-like protein kinase 19"
FT /id="PRO_0000295066"
FT TOPO_DOM 21..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..129
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 135..239
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 326..603
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 616..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 332..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 399
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 491
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 302..308
FT /note="DGNDITT -> VFFSRWE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_026693"
FT VAR_SEQ 309..645
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_026694"
SQ SEQUENCE 645 AA; 71620 MW; C810370003FED0ED CRC64;
MSSLISFIFL FLFSSITASA QNTFYLYHNC SVTTTFSSNS TYSTNLKTLL SSLSSLNASS
YSTGFQTATA GQAPDRVTGL FLCRVDVSSE VCRSCVTFAV NETLTRCPKD KEGVFYYEQC
LLRYSNRNIV ATLNTDGGMF MQSARNPLSV KQDQFRDLVL TPMNLAAVEA ARSFKKWAVR
KIDLNASQSL YGMVRCTPDL REQDCLDCLK IGINQVTYDK IGGRILLPSC ASRYDNYAFY
NESNVGTPQD SSPRPGKGGN SSVIIIAVVV PITVLFLLLV AVFSVRAKNK RTLNEKEPVA
EDGNDITTAG SLQFDFKAIE AATNCFLPIN KLGQGGFGEV YKGTLSSGLQ VAVKRLSKTS
GQGEKEFENE VVVVAKLQHR NLVKLLGYCL EGEEKILVYE FVPNKSLDHF LFDSTMKMKL
DWTRRYKIIG GIARGILYLH QDSRLTIIHR DLKAGNILLD DDMNPKIADF GMARIFGMDQ
TEAMTRRVVG TYGYMSPEYA MYGQFSMKSD VYSFGVLVLE IISGMKNSSL YQMDESVGNL
VTYTWRLWSN GSPSELVDPS FGDNYQTSEI TRCIHIALLC VQEDAEDRPT MSSIVQMLTT
SLIALAEPRP PGFFFRSKQE QAGPSIDSST HCSVDEASIT RVTPR
