CRK10_ARATH
ID CRK10_ARATH Reviewed; 669 AA.
AC Q8GYA4; O65470; Q8H785; Q9C5T0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 10;
DE Short=Cysteine-rich RLK10;
DE EC=2.7.11.-;
DE AltName: Full=Receptor-like protein kinase 4;
DE Flags: Precursor;
GN Name=CRK10; Synonyms=RLK4; OrderedLocusNames=At4g23180; ORFNames=F21P8.70;
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 MRNA] (ISOFORM 2).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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 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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-669 (ISOFORM 1), AND 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 [7]
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 [8]
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 [9]
RP INTERACTION WITH CRKIPS.
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 -!- SUBUNIT: Interacts with CRKIP1 (KAPP), CRKIP2 and CRKIP3, three kinase-
CC associated type 2C proteins. {ECO:0000269|PubMed:15604743}.
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=Q8GYA4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GYA4-2; Sequence=VSP_041302;
CC -!- INDUCTION: By salicylic acid (SA) or by a bacterial pathogen infection.
CC May be regulated by WRKY DNA-binding proteins at the transcriptional
CC level. {ECO:0000269|PubMed:11100776, 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=AAK28315.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA18465.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79273.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF083790; AAN60348.1; -; mRNA.
DR EMBL; AL022347; CAA18465.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161558; CAB79273.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84719.1; -; Genomic_DNA.
DR EMBL; AK117765; BAC42412.1; -; mRNA.
DR EMBL; BT005954; AAO64889.1; -; mRNA.
DR EMBL; AF224705; AAK28315.1; ALT_INIT; mRNA.
DR PIR; T04835; T04835.
DR RefSeq; NP_567679.2; NM_118447.3. [Q8GYA4-1]
DR AlphaFoldDB; Q8GYA4; -.
DR SMR; Q8GYA4; -.
DR BioGRID; 13706; 14.
DR IntAct; Q8GYA4; 16.
DR STRING; 3702.AT4G23180.1; -.
DR iPTMnet; Q8GYA4; -.
DR PaxDb; Q8GYA4; -.
DR PRIDE; Q8GYA4; -.
DR ProteomicsDB; 222677; -. [Q8GYA4-1]
DR EnsemblPlants; AT4G23180.1; AT4G23180.1; AT4G23180. [Q8GYA4-1]
DR GeneID; 828417; -.
DR Gramene; AT4G23180.1; AT4G23180.1; AT4G23180. [Q8GYA4-1]
DR KEGG; ath:AT4G23180; -.
DR Araport; AT4G23180; -.
DR TAIR; locus:2121676; AT4G23180.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; Q8GYA4; -.
DR OMA; MPKYFSG; -.
DR OrthoDB; 345452at2759; -.
DR PRO; PR:Q8GYA4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GYA4; baseline and differential.
DR Genevisible; Q8GYA4; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Disulfide bond; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..669
FT /note="Cysteine-rich receptor-like protein kinase 10"
FT /id="PRO_0000295057"
FT TOPO_DOM 35..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..142
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 148..252
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 348..634
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 260..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 354..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 421
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 513
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 521
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
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 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 108..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 209..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DISULFID 221..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_041302"
FT CONFLICT 268
FT /note="S -> C (in Ref. 1; AAN60348)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..281
FT /note="GKD -> EKE (in Ref. 6; AAK28315)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="L -> R (in Ref. 6; AAK28315)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Y -> S (in Ref. 6; AAK28315)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="N -> T (in Ref. 6; AAK28315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 74283 MW; E2CCD6AAC5F87BF7 CRC64;
MRRNTDQESP IMSYYSSFFF LFLFSFLTSF RVSAQDPTYV YHTCQNTANY TSNSTYNNNL
KTLLASLSSR NASYSTGFQN ATVGQAPDRV TGLFNCRGDV STEVCRRCVS FAVNDTLTRC
PNQKEATLYY DECVLRYSNQ NILSTLITTG GVILVNTRNV TSNQLDLLSD LVLPTLNQAA
TVALNSSKKF GTRKNNFTAL QSFYGLVQCT PDLTRQDCSR CLQLVINQIP TDRIGARIIN
PSCTSRYEIY AFYTESAVPP PPPPPSISTP PVSAPPRSGK DGNSKVLVIA IVVPIIVAVL
LFIAGYCFLT RRARKSYYTP SAFAGDDITT ADSLQLDYRT IQTATDDFVE SNKIGQGGFG
EVYKGTLSDG TEVAVKRLSK SSGQGEVEFK NEVVLVAKLQ HRNLVRLLGF CLDGEERVLV
YEYVPNKSLD YFLFDPAKKG QLDWTRRYKI IGGVARGILY LHQDSRLTII HRDLKASNIL
LDADMNPKIA DFGMARIFGL DQTEENTSRI VGTYGYMSPE YAMHGQYSMK SDVYSFGVLV
LEIISGKKNS SFYQTDGAHD LVSYAWGLWS NGRPLELVDP AIVENCQRNE VVRCVHIGLL
CVQEDPAERP TLSTIVLMLT SNTVTLPVPR QPGLFFQSRI GKDPLDTDTT SKSLLGSVDD
ASITDIHPR
