CRPK1_ARATH
ID CRPK1_ARATH Reviewed; 390 AA.
AC Q93YN1; Q9FX80;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cold-responsive protein kinase 1 {ECO:0000303|PubMed:28344081};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:28344081};
GN Name=CRPK1 {ECO:0000303|PubMed:28344081};
GN OrderedLocusNames=At1g16670 {ECO:0000312|Araport:AT1G16670};
GN ORFNames=F19K19.4 {ECO:0000312|EMBL:AAG10816.1};
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=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 [4]
RP INDUCTION BY P.BRASSICAE OVIPOSITION; FLG22 AND ELF26.
RX PubMed=17142483; DOI=10.1104/pp.106.090837;
RA Little D., Gouhier-Darimont C., Bruessow F., Reymond P.;
RT "Oviposition by pierid butterflies triggers defense responses in
RT Arabidopsis.";
RL Plant Physiol. 143:784-800(2007).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-2 AND LYS-69, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, SUBUNIT, INTERACTION WITH GRF6, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=28344081; DOI=10.1016/j.molcel.2017.02.016;
RA Liu Z., Jia Y., Ding Y., Shi Y., Li Z., Guo Y., Gong Z., Yang S.;
RT "Plasma membrane CRPK1-mediated phosphorylation of 14-3-3 proteins induces
RT their nuclear import to fine-tune CBF signaling during cold response.";
RL Mol. Cell 66:117-128(2017).
CC -!- FUNCTION: Negative regulator of freezing tolerance that phosphorylates
CC 14-3-3 proteins (e.g. GRF6) thus triggering their translocation from
CC the cytosol to the nucleus in response to cold stress.
CC {ECO:0000269|PubMed:28344081}.
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; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:28344081};
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 EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159,
CC ECO:0000269|PubMed:28344081};
CC -!- ACTIVITY REGULATION: Activated by cold. {ECO:0000269|PubMed:28344081}.
CC -!- SUBUNIT: Interacts with and phosphorylates 14-3-3 proteins. Binds to
CC GRF6 at the plasma membrane. {ECO:0000269|PubMed:28344081}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28344081};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- INDUCTION: Accumulates upon P.brassicae oviposition and in response to
CC bacterial elicitors (e.g. flg22 and elf26).
CC {ECO:0000269|PubMed:17142483}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:28344081}.
CC -!- DISRUPTION PHENOTYPE: Enhanced freezing tolerance due to impaired
CC phosphorylation and subsequent translocation of 14-3-3 proteins in cold
CC conditions. Altered cold induction of cold-responsive C-repeat-binding
CC factor (CBF) target genes. {ECO:0000269|PubMed:28344081}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG10816.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011808; AAG10816.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29481.1; -; Genomic_DNA.
DR EMBL; AY059921; AAL24403.1; -; mRNA.
DR EMBL; BT000152; AAN15471.1; -; mRNA.
DR PIR; H86301; H86301.
DR RefSeq; NP_564003.1; NM_101527.4.
DR AlphaFoldDB; Q93YN1; -.
DR SMR; Q93YN1; -.
DR STRING; 3702.AT1G16670.1; -.
DR iPTMnet; Q93YN1; -.
DR PaxDb; Q93YN1; -.
DR PRIDE; Q93YN1; -.
DR ProteomicsDB; 224551; -.
DR EnsemblPlants; AT1G16670.1; AT1G16670.1; AT1G16670.
DR GeneID; 838236; -.
DR Gramene; AT1G16670.1; AT1G16670.1; AT1G16670.
DR KEGG; ath:AT1G16670; -.
DR Araport; AT1G16670; -.
DR TAIR; locus:2017923; AT1G16670.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_4_1; -.
DR InParanoid; Q93YN1; -.
DR OMA; NWHARAR; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q93YN1; -.
DR PRO; PR:Q93YN1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93YN1; baseline and differential.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0050826; P:response to freezing; IMP:UniProtKB.
DR GO; GO:0009625; P:response to insect; IEP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Stress response; Transferase.
FT CHAIN 1..390
FT /note="Cold-responsive protein kinase 1"
FT /id="PRO_0000440310"
FT DOMAIN 41..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 345..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 47..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 114
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 208
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 216
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MUTAGEN 2
FT /note="G->A: Normal subcellular localization at the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:28344081"
FT MUTAGEN 69
FT /note="K->E: Loss of kinase activity. Impaired
FT autophosphorylation. Enhanced freezing tolerance due to
FT impaired phosphorylation and subsequent translocation of
FT 14-3-3 proteins in cold conditions."
FT /evidence="ECO:0000269|PubMed:28344081"
SQ SEQUENCE 390 AA; 43289 MW; 645ED5E069D8C8D8 CRC64;
MGCSWLSCHR REATEVDGEI AAIDNVKIYK YREIRQATDD FSAENKIGEG GFGSVYKGCL
KDGKLAAIKV LSAESRQGVK EFLTEINVIS EIQHENLVKL YGCCVEGNHR ILVYNFLENN
SLDKTLLAGG YTRSGIQFDW SSRANICVGV AKGLAFLHEE VRPHIIHRDI KASNILLDKY
LSPKISDFGL ARLMPPNMTH VSTRVAGTIG YLAPEYAVRG QLTRKADIYS FGVLLMEIVS
GRSNKNTRLP TEYQYLLERA WELYERNELV DLVDSGLNGV FDAEEACRYL KIGLLCTQDS
PKLRPSMSTV VRLLTGEKDI DYKKISRPGL ISDFMDLKVR GPVATKTEQV NRQNYTNPSS
SSNGSSRDHS NAYSSGASSA NAGNTFSSTI
