CRK5_ARATH
ID CRK5_ARATH Reviewed; 659 AA.
AC Q9C5S8; O65465; Q8H1S3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 5;
DE Short=Cysteine-rich RLK5;
DE EC=2.7.11.-;
DE AltName: Full=Receptor-like protein kinase 6;
DE Flags: Precursor;
GN Name=CRK5; Synonyms=RLK6; OrderedLocusNames=At4g23130;
GN ORFNames=F21P8.20, F7H19.320;
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] (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 [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 2).
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 [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=14756307; DOI=10.1023/b:plan.0000009265.72567.58;
RA Chen K., Du L., Chen Z.;
RT "Sensitization of defense responses and activation of programmed cell death
RT by a pathogen-induced receptor-like protein kinase in Arabidopsis.";
RL Plant Mol. Biol. 53:61-74(2003).
RN [8]
RP FUNCTION, INDUCTION, INTERACTION WITH CRKIPS, AND MUTAGENESIS OF LYS-368.
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 -!- FUNCTION: Involved in multiple distinct defense responses. May function
CC as a disease resistance (R) protein. {ECO:0000269|PubMed:14756307,
CC ECO:0000269|PubMed:15604743}.
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=Q9C5S8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C5S8-2; Sequence=VSP_026686;
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 ECO:0000269|PubMed:15604743}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor 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=CAA18460.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA19829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79268.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF224707; AAK28317.1; -; mRNA.
DR EMBL; AL022347; CAA18460.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL031018; CAA19829.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161558; CAB79268.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84712.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84713.1; -; Genomic_DNA.
DR EMBL; AY142496; AAN13047.1; -; mRNA.
DR PIR; T04830; T04830.
DR RefSeq; NP_567677.1; NM_118442.4. [Q9C5S8-1]
DR RefSeq; NP_849425.1; NM_179094.3. [Q9C5S8-2]
DR AlphaFoldDB; Q9C5S8; -.
DR SMR; Q9C5S8; -.
DR BioGRID; 13701; 1.
DR STRING; 3702.AT4G23130.2; -.
DR PaxDb; Q9C5S8; -.
DR PRIDE; Q9C5S8; -.
DR ProteomicsDB; 222766; -. [Q9C5S8-1]
DR EnsemblPlants; AT4G23130.1; AT4G23130.1; AT4G23130. [Q9C5S8-1]
DR EnsemblPlants; AT4G23130.2; AT4G23130.2; AT4G23130. [Q9C5S8-2]
DR GeneID; 828412; -.
DR Gramene; AT4G23130.1; AT4G23130.1; AT4G23130. [Q9C5S8-1]
DR Gramene; AT4G23130.2; AT4G23130.2; AT4G23130. [Q9C5S8-2]
DR KEGG; ath:AT4G23130; -.
DR Araport; AT4G23130; -.
DR TAIR; locus:2121611; AT4G23130.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; Q9C5S8; -.
DR OMA; PEACRDC; -.
DR OrthoDB; 345452at2759; -.
DR PhylomeDB; Q9C5S8; -.
DR PRO; PR:Q9C5S8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9C5S8; baseline and differential.
DR Genevisible; Q9C5S8; 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:0012501; P:programmed cell death; IMP: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; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..659
FT /note="Cysteine-rich receptor-like protein kinase 5"
FT /id="PRO_0000295052"
FT TOPO_DOM 25..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..132
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 138..243
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 340..619
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 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 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 315
FT /note="P -> PGAND (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026686"
FT MUTAGEN 368
FT /note="K->E: Abolishes the interaction with CRKIPs."
FT /evidence="ECO:0000269|PubMed:15604743"
SQ SEQUENCE 659 AA; 73402 MW; 5FE8E6A06FBC3D96 CRC64;
MSAYTSLNFL FLLTFFIGSL RVSAQLQDPT YVGHVCTNRI SRNSIYFSNL QTLLTSLSSN
NAYFSLGSHS LTKGQNSDMV FGLYLCKGDL SPESCRECVI FAAKDTRSRC PGGKEFLIQY
DECMLGYSDR NIFMDTVTTT TIITWNTQKV TADQSDRFND AVLSLMKKSA EEAANSTSKK
FAVKKSDFSS SQSLYASVQC IPDLTSEDCV MCLQQSIKEL YFNKVGGRFL VPSCNSRYEV
YPFYKETIEG TVLPPPVSAP PLPLVSTPSF PPGKGKNSTV IIIAIVVPVA ISVLICVAVF
SFHASKRAKK TYDTPEEDDI TTAGSLQFDF KVIEAATDKF SMCNKLGQGG FGQVYKGTLP
NGVQVAVKRL SKTSGQGEKE FKNEVVVVAK LQHRNLVKLL GFCLEREEKI LVYEFVSNKS
LDYFLFDSRM QSQLDWTTRY KIIGGIARGI LYLHQDSRLT IIHRDLKAGN ILLDADMNPK
VADFGMARIF EIDQTEAHTR RVVGTYGYMS PEYAMYGQFS MKSDVYSFGV LVLEIISGRK
NSSLYQMDAS FGNLVTYTWR LWSDGSPLDL VDSSFRDSYQ RNEIIRCIHI ALLCVQEDTE
NRPTMSAIVQ MLTTSSIALA VPQPPGFFFR SNHEQAGPSM DKSSLCSIDA ASITILAPR
