CRK11_ARATH
ID CRK11_ARATH Reviewed; 667 AA.
AC Q9ZP16; O65471;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 11;
DE Short=Cysteine-rich RLK11;
DE EC=2.7.11.-;
DE AltName: Full=Receptor-like protein kinase 3;
DE Flags: Precursor;
GN Name=CRK11; Synonyms=RLK3; OrderedLocusNames=At4g23190; ORFNames=F21P8.80;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10377997; DOI=10.1046/j.1365-313x.1999.00447.x;
RA Czernic P., Visser B., Sun W., Savoure A., Deslandes L., Marco Y.,
RA van Montagu M., Verbruggen N.;
RT "Characterization of an Arabidopsis thaliana receptor-like protein kinase
RT gene activated by oxidative stress and pathogen attack.";
RL Plant J. 18:321-327(1999).
RN [2]
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 [3]
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 [4]
RP INDUCTION.
RX PubMed=11135117; DOI=10.1046/j.1365-313x.2000.00923.x;
RA Du L., Chen Z.;
RT "Identification of genes encoding receptor-like protein kinases as possible
RT targets of pathogen- and salicylic acid-induced WRKY DNA-binding proteins
RT in Arabidopsis.";
RL Plant J. 24:837-847(2000).
RN [5]
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).
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 -!- TISSUE SPECIFICITY: Detected in root, stem, leaf and flower.
CC {ECO:0000269|PubMed:10377997}.
CC -!- INDUCTION: By salicylic acid (SA), by a bacterial pathogen infection or
CC by oxidative stress. May be regulated by WRKY DNA-binding proteins at
CC the transcriptional level. {ECO:0000269|PubMed:10377997,
CC ECO:0000269|PubMed:11135117}.
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=CAA18466.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79274.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ011674; CAA09731.1; -; mRNA.
DR EMBL; AL022347; CAA18466.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161558; CAB79274.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84720.1; -; Genomic_DNA.
DR PIR; T04836; T04836.
DR RefSeq; NP_194050.2; NM_118448.4.
DR AlphaFoldDB; Q9ZP16; -.
DR SMR; Q9ZP16; -.
DR BioGRID; 13707; 8.
DR IntAct; Q9ZP16; 8.
DR STRING; 3702.AT4G23190.1; -.
DR PaxDb; Q9ZP16; -.
DR ProteomicsDB; 222678; -.
DR EnsemblPlants; AT4G23190.1; AT4G23190.1; AT4G23190.
DR GeneID; 828418; -.
DR Gramene; AT4G23190.1; AT4G23190.1; AT4G23190.
DR KEGG; ath:AT4G23190; -.
DR Araport; AT4G23190; -.
DR TAIR; locus:2121691; AT4G23190.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; Q9ZP16; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZP16; -.
DR PRO; PR:Q9ZP16; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZP16; baseline and differential.
DR Genevisible; Q9ZP16; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:TAIR.
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:0006979; P:response to oxidative stress; 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 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..667
FT /note="Cysteine-rich receptor-like protein kinase 11"
FT /id="PRO_0000295058"
FT TOPO_DOM 25..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..667
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..129
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 135..248
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 350..629
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 259..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 356..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 423
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 515
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 523
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
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 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
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 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 264
FT /note="P -> S (in Ref. 1; CAA09731)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Y -> N (in Ref. 1; CAA09731)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="EA -> DS (in Ref. 1; CAA09731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 74139 MW; E449784ADF0D9717 CRC64;
MKQRSLFSVL CFFFISFGVA SVSAQTCTTD KGTFRPNGTY DVNRRLILSS LPSNVTDQDG
LYYNGSIGQQ PNRVYAIGMC IPGSTSEDCS DCIKKESEFF LKNCPNQTEA YSWPGEPTLC
YVRYSNTSFS GSADLNPRNW LTNTGDLDSN LTEFTKIWEG LMGRMISAAS TAKSTPSSSD
NHYSADSAVL TPLLNIYALM QCTPDLSSGD CENCLRQSAI DYQSCCSQKR GGVVMRPSCF
LRWDLYTYSN AFDNLTVASP PPEPPVTVPQ PAGDQDNPTN NDSKGISAGV VVAITVPTVI
AILILLVLGF VLFRRRKSYQ RTKTESESDI STTDSLVYDF KTIEAATNKF STSNKLGEGG
FGAVYKGKLS NGTDVAVKRL SKKSGQGTRE FRNEAVLVTK LQHRNLVRLL GFCLEREEQI
LIYEFVHNKS LDYFLFDPEK QSQLDWTRRY KIIGGIARGI LYLHQDSRLK IIHRDLKASN
ILLDADMNPK IADFGLATIF GVEQTQGNTN RIAGTYAYMS PEYAMHGQYS MKSDIYSFGV
LVLEIISGKK NSGVYQMDET STAGNLVTYA SRLWRNKSPL ELVDPTFGRN YQSNEVTRCI
HIALLCVQEN PEDRPMLSTI ILMLTSNTIT LPVPRLPGFF PRSRQLKLVS EGSESDQYTS
KSSSFSS
