CRK4_ARATH
ID CRK4_ARATH Reviewed; 676 AA.
AC Q9LZU4;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cysteine-rich receptor-like protein kinase 4;
DE Short=Cysteine-rich RLK4;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=CRK4; OrderedLocusNames=At3g45860; ORFNames=F16L2_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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
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).
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 -!- INDUCTION: By salicylic acid (SA) or by a bacterial pathogen infection.
CC {ECO:0000269|PubMed:15604743}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CRK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AL162459; CAB82810.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78083.1; -; Genomic_DNA.
DR PIR; T47526; T47526.
DR RefSeq; NP_190172.1; NM_114455.2.
DR AlphaFoldDB; Q9LZU4; -.
DR SMR; Q9LZU4; -.
DR BioGRID; 9049; 1.
DR STRING; 3702.AT3G45860.1; -.
DR PaxDb; Q9LZU4; -.
DR PRIDE; Q9LZU4; -.
DR ProteomicsDB; 224512; -.
DR EnsemblPlants; AT3G45860.1; AT3G45860.1; AT3G45860.
DR GeneID; 823729; -.
DR Gramene; AT3G45860.1; AT3G45860.1; AT3G45860.
DR KEGG; ath:AT3G45860; -.
DR Araport; AT3G45860; -.
DR TAIR; locus:2077147; AT3G45860.
DR eggNOG; ENOG502QWDY; Eukaryota.
DR HOGENOM; CLU_000288_35_2_1; -.
DR InParanoid; Q9LZU4; -.
DR OMA; NASACQS; -.
DR OrthoDB; 345452at2759; -.
DR PhylomeDB; Q9LZU4; -.
DR PRO; PR:Q9LZU4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZU4; baseline and differential.
DR Genevisible; Q9LZU4; 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 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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..676
FT /note="Cysteine-rich receptor-like protein kinase 4"
FT /id="PRO_0000295051"
FT TOPO_DOM 17..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..135
FT /note="Gnk2-homologous 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 146..246
FT /note="Gnk2-homologous 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00806"
FT DOMAIN 351..631
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 252..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 476
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 357..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 424
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 516
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 524
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
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 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 676 AA; 75923 MW; 46DB72413084CC89 CRC64;
MSFFWLFPFL LHLSFADSLS PLSAPVQNFI HLNHSCPSSI LTYSRNSTYF TNLKTLLSSL
SSRNASYSTG FQTATAGQAP DRVTGLFLCR GDVSQEVCRN CVAFSVKETL YWCPYNKEVV
LYYDECMLRY SHRNILSTVT YDGSAILLNG ANISSSNQNQ VDEFRDLVSS TLNLAAVEAA
NSSKKFYTRK VITPQPLYLL VQCTPDLTRQ DCLRCLQKSI KGMSLYRIGG RFFYPSCNSR
YENYSFYNET ATRSSSPPSL PPRSTPQQQL KLAPPPLISE RGKGRNSSVI IVVVVPIIAL
LLLFVAFFSL RAKKTRTNYE REPLTEESDD ITTAGSLQFD FKAIEAATNK FCETNKLGQG
GFGEVYKGIF PSGVQVAVKR LSKTSGQGER EFANEVIVVA KLQHRNLVRL LGFCLERDER
ILVYEFVPNK SLDYFIFDST MQSLLDWTRR YKIIGGIARG ILYLHQDSRL TIIHRDLKAG
NILLGDDMNA KIADFGMARI FGMDQTEANT RRIVGTYGYM SPEYAMYGQF SMKSDVYSFG
VLVLEIISGK KNSNVYQMDG TSAGNLVTYT WRLWSNGSPL ELVDPSFRDN YRINEVSRCI
HIALLCVQEE AEDRPTMSAI VQMLTTSSIA LAVPQRPGFF FRSSKHEQVG LVDRLSINTS
ALCSVDDASI TNVTPR
