ID CRK13_ARATH Reviewed; 673 AA.
AC Q0PW40; O65473; Q8H0Y5; Q8H1R8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 13;
DE Short=Cysteine-rich RLK13;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK13; OrderedLocusNames=At4g23210; ORFNames=F21P8.100;
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).
RX PubMed=17419849; DOI=10.1111/j.1365-313x.2007.03064.x;
RA Acharya B.R., Raina S., Maqbool S.B., Jagadeeswaran G., Mosher S.L.,
RA Appel H.M., Schultz J.C., Klessig D.F., Raina R.;
RT "Overexpression of CRK13, an Arabidopsis cysteine-rich receptor-like
RT kinase, results in enhanced resistance to Pseudomonas syringae.";
RL Plant J. 50:488-499(2007).
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] (ISOFORMS 2 AND 3).
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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0PW40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0PW40-2; Sequence=VSP_026688;
CC Name=3;
CC IsoId=Q0PW40-3; Sequence=VSP_026689, VSP_026690;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {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=CAA18468.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ680080; ABG74916.1; -; mRNA.
DR EMBL; AL022347; CAA18468.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161558; CAB79276.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84722.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84723.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84724.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67416.1; -; Genomic_DNA.
DR EMBL; AY142503; AAN13054.1; -; mRNA.
DR EMBL; BT001110; AAN64174.1; -; mRNA.
DR PIR; T04838; T04838.
DR RefSeq; NP_001078435.1; NM_001084966.2. [Q0PW40-1]
DR RefSeq; NP_001329248.1; NM_001341586.1. [Q0PW40-2]
DR RefSeq; NP_194052.2; NM_118450.4. [Q0PW40-3]
DR RefSeq; NP_849427.1; NM_179096.3. [Q0PW40-2]
DR AlphaFoldDB; Q0PW40; -.
DR SMR; Q0PW40; -.
DR BioGRID; 13709; 21.
DR IntAct; Q0PW40; 21.
DR STRING; 3702.Q0PW40; -.
DR GlyCosmos; Q0PW40; 9 sites, No reported glycans.
DR PaxDb; 3702-AT4G23210-3; -.
DR ProteomicsDB; 222641; -. [Q0PW40-1]
DR EnsemblPlants; AT4G23210.1; AT4G23210.1; AT4G23210. [Q0PW40-3]
DR EnsemblPlants; AT4G23210.2; AT4G23210.2; AT4G23210. [Q0PW40-2]
DR EnsemblPlants; AT4G23210.3; AT4G23210.3; AT4G23210. [Q0PW40-1]
DR EnsemblPlants; AT4G23210.4; AT4G23210.4; AT4G23210. [Q0PW40-2]
DR GeneID; 828420; -.
DR Gramene; AT4G23210.1; AT4G23210.1; AT4G23210. [Q0PW40-3]
DR Gramene; AT4G23210.2; AT4G23210.2; AT4G23210. [Q0PW40-2]
DR Gramene; AT4G23210.3; AT4G23210.3; AT4G23210. [Q0PW40-1]
DR Gramene; AT4G23210.4; AT4G23210.4; AT4G23210. [Q0PW40-2]
DR KEGG; ath:AT4G23210; -.
DR Araport; AT4G23210; -.
DR TAIR; AT4G23210; CRK13.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; Q0PW40; -.
DR OMA; HESCCHR; -.
DR OrthoDB; 687002at2759; -.
DR PhylomeDB; Q0PW40; -.
DR PRO; PR:Q0PW40; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0PW40; baseline and differential.
DR Genevisible; Q0PW40; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:TAIR.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.30.430.20; Gnk2 domain, C-X8-C-X2-C motif; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR27002:SF1064; CYSTEINE-RICH RECEPTOR-LIKE PROTEIN KINASE 13; 1.
DR PANTHER; PTHR27002; RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE SD1-8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01657; Stress-antifung; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..673
FT /note="Cysteine-rich receptor-like protein kinase 13"
FT /id="PRO_0000295060"
FT TOPO_DOM 25..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..128
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 137..250
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 358..633
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 264..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 483
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 364..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 531
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 37
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 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 525..673
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026688"
FT VAR_SEQ 574..610
FT /note="WRLWKSGTPLNLVDATIAENYKSEEVIRCIHIALLCV -> STIIVSHCCCN
FT CKIWIRSLNFVSGLEVMEKRDTIKPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026689"
FT VAR_SEQ 611..673
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_026690"
SQ SEQUENCE 673 AA; 75295 MW; 9413AE37741DDCDB CRC64;
MKQRSLLSIL CFILLASGVA SVSAQTCIEN RKYFTPNGTY DSNRRLILSS LPNNTASRDG
FYYGSIGEEQ DRVYALGMCI PKSTPSDCSN CIKGAAGWLI QDCVNQTDAY YWALDPTLCL
VRYSNISFSG SAAFWEIEPQ YLVLNTATIA SNLTEFKTIW EDLTSRTITA ASAARSTPSS
SDNHYRVDFA NLTKFQNIYA LMQCTPDISS DECNNCLQRG VLEYQSCCGN NTGGYVMRPI
CFFRWQLFTF SKAFHNITLA TTPPLSPPPL QRPVVASQPP SADNRDKKRD NSSGKISMKT
ILAIVVVGIV ILIIISGILA RRFARKEKPY QEVELNQTGI TSVRSLQYKF KTIETATNNF
SERLGHGGSG HVFKGRLPDG KEIAVKRLSE KTEQSKKEFK NEVVLVAKLQ HRNLVRLLGF
SVKGEEKIIV YEYLPNRSLD YILFDPTKQG ELDWKKRYKI IGGTARGILY LHQDSQPTII
HRDLKAGNIL LDAHMNPKVA DFGTARIFGM DQSVAITANA AGTPGYMAPE YMELGEFSMK
SDVYSYGVLV LEIICGKRNT SFSSPVQNFV TYVWRLWKSG TPLNLVDATI AENYKSEEVI
RCIHIALLCV QEEPTDRPDF SIIMSMLTSN SLILPVPKPP PSFIPGRPNQ STTRPSSQNI
NDGRWSLLKM MFH
//
