ZRK12_ARATH
ID ZRK12_ARATH Reviewed; 389 AA.
AC O64798; Q8GWC4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Inactive serine/threonine-protein kinase ZRK12 {ECO:0000303|PubMed:28499073};
GN Name=ZRK12 {ECO:0000303|PubMed:28499073};
GN OrderedLocusNames=At1g67470 {ECO:0000312|Araport:AT1G67470};
GN ORFNames=F12B7.2 {ECO:0000312|EMBL:AAG52308.1},
GN T1F15.6 {ECO:0000312|EMBL:AAC18787.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY ELEVATED TEMPERATURE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=28499073; DOI=10.1111/nph.14585;
RA Wang Z., Cui D., Liu J., Zhao J., Liu C., Xin W., Li Y., Liu N., Ren D.,
RA Tang D., Hu Y.;
RT "Arabidopsis ZED1-related kinases mediate the temperature-sensitive
RT intersection of immune response and growth homeostasis.";
RL New Phytol. 215:711-724(2017).
CC -!- FUNCTION: Together with RPP13L4/ZAR1, involved in the regulation of the
CC ambient temperature-sensitive intersection of growth and immune
CC response in the absence of pathogens. {ECO:0000269|PubMed:28499073}.
CC -!- INDUCTION: Induced by elevated temperature (e.g. at 25 degrees
CC Celsius). {ECO:0000269|PubMed:28499073}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DISRUPTION PHENOTYPE: Slightly shortened inflorescence stem when grown
CC at 25 degrees Celsius (PubMed:28499073). The double mutant zed1-6
CC zrk12-1 exhibits short inflorescence stem and autoimmunity symptoms
CC when grown at 25 degrees Celsius (PubMed:28499073).
CC {ECO:0000269|PubMed:28499073}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC004393; AAC18787.1; -; Genomic_DNA.
DR EMBL; AC011020; AAG52308.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34650.1; -; Genomic_DNA.
DR EMBL; AK118940; BAC43521.1; -; mRNA.
DR PIR; T02158; T02158.
DR RefSeq; NP_564898.1; NM_105414.4.
DR AlphaFoldDB; O64798; -.
DR SMR; O64798; -.
DR BioGRID; 28289; 1.
DR IntAct; O64798; 1.
DR STRING; 3702.AT1G67470.1; -.
DR iPTMnet; O64798; -.
DR PaxDb; O64798; -.
DR PRIDE; O64798; -.
DR ProteomicsDB; 243059; -.
DR EnsemblPlants; AT1G67470.1; AT1G67470.1; AT1G67470.
DR GeneID; 843068; -.
DR Gramene; AT1G67470.1; AT1G67470.1; AT1G67470.
DR KEGG; ath:AT1G67470; -.
DR Araport; AT1G67470; -.
DR TAIR; locus:2008818; AT1G67470.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; O64798; -.
DR OMA; DSHQDIS; -.
DR OrthoDB; 778960at2759; -.
DR PhylomeDB; O64798; -.
DR PRO; PR:O64798; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O64798; baseline and differential.
DR Genevisible; O64798; AT.
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; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR045274; WAK-like.
DR PANTHER; PTHR27005; PTHR27005; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome.
FT CHAIN 1..389
FT /note="Inactive serine/threonine-protein kinase ZRK12"
FT /id="PRO_0000403341"
FT DOMAIN 41..342
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 222
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CONFLICT 142
FT /note="E -> G (in Ref. 3; BAC43521)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="I -> T (in Ref. 3; BAC43521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 45195 MW; B7DE62B92546BEE1 CRC64;
MGWWRKKKKP KSEIASERGA KLLKDLIECC DGKSNPIKFF SADEIRKATN NFGVSNLVSE
LSHDFDYKWY SGKNENHDMI LVRKAFSQSV YYKDTFFRDI AVSSMVSGHK NFLKLIGYCL
EFEEPVMVYH GVKKHYHLES SEQPWKRRMK IAEDIATALA YLHTAFPRPF VYRCLSLTNI
LLDEDGVAKL MDFSFCVSIP EGETFVQVDY IAGTVDYLKP NYLKHGVVSE ETDVFAVGHS
MQMLLMGEKI FDRIMRRPFP TSKFMEEPKM DEIADPEMGE ISEEELCQMK AFLLLSLRCT
GHVGEVPTMV EVAKELKSIQ RCLHNDTFSP SVETQFDSHQ DISSSVILSN QTKDTRALLR
CIACHVFDEM FQWVMMNWFR FFRRNRRIC
