ID   CTR1_ARATH              Reviewed;         821 AA.
AC   Q05609;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Serine/threonine-protein kinase CTR1 {ECO:0000303|PubMed:8431946};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=Protein CONSTITUTIVE TRIPLE RESPONSE1 {ECO:0000303|PubMed:8431946};
GN   Name=CTR1 {ECO:0000303|PubMed:8431946};
GN   OrderedLocusNames=At5g03730 {ECO:0000312|Araport:AT5G03730};
GN   ORFNames=F17C15_150 {ECO:0000312|EMBL:CAB82938.1};
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 [MRNA], DISRUPTION PHENOTYPE, FUNCTION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF GLU-596 AND ASP-694.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=8431946; DOI=10.1016/0092-8674(93)90119-b;
RA   Kieber J.J., Rothenberg M., Roman G., Feldmann K.A., Ecker J.R.;
RT   "CTR1, a negative regulator of the ethylene response pathway in
RT   Arabidopsis, encodes a member of the raf family of protein kinases.";
RL   Cell 72:427-441(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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   FUNCTION, AND INTERACTION WITH EIN2.
RX   PubMed=23132950; DOI=10.1073/pnas.1214848109;
RA   Ju C., Yoon G.M., Shemansky J.M., Lin D.Y., Ying Z.I., Chang J.,
RA   Garrett W.M., Kessenbrock M., Groth G., Tucker M.L., Cooper B.,
RA   Kieber J.J., Chang C.;
RT   "CTR1 phosphorylates the central regulator EIN2 to control ethylene hormone
RT   signaling from the ER membrane to the nucleus in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:19486-19491(2012).
RN   [5]
RP   FUNCTION, AND ACTIVITY REGULATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=25822663; DOI=10.1371/journal.pgen.1005143;
RA   Xie L.-J., Chen Q.-F., Chen M.-X., Yu L.-J., Huang L., Chen L., Wang F.-Z.,
RA   Xia F.-N., Zhu T.-R., Wu J.-X., Yin J., Liao B., Shi J., Zhang J.-H.,
RA   Aharoni A., Yao N., Shu W., Xiao S.;
RT   "Unsaturation of very-long-chain ceramides protects plant from hypoxia-
RT   induced damages by modulating ethylene signaling in Arabidopsis.";
RL   PLoS Genet. 11:e1005143-e1005143(2015).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 540-821.
RA   Mayerhofer H., Panneerselvam S., Mueller-Dieckmann J.;
RT   "Crystal structure of the Constitutive Triple Response 1 kinase domain from
RT   Arabidopsis thaliana.";
RL   Submitted (OCT-2010) to the PDB data bank.
CC   -!- FUNCTION: Acts as a negative regulator in the ethylene response pathway
CC       (PubMed:8431946). Phosphorylates the cytosolic C-terminal domain of
CC       EIN2, preventing the signaling in the absence of ethylene
CC       (PubMed:23132950). Interacts with C24:1-ceramide upon hypoxic
CC       conditions (e.g. submergences) to in turn regulate EIN2 endoplasmic
CC       reticulum (ER)-to-nucleus translocation and EIN3 stabilization
CC       (PubMed:25822663). {ECO:0000269|PubMed:23132950,
CC       ECO:0000269|PubMed:25822663, ECO:0000269|PubMed:8431946}.
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   -!- 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;
CC   -!- ACTIVITY REGULATION: Kinase activity is inhibited by C24:1-ceramide
CC       during hypoxia (e.g. submergences). {ECO:0000269|PubMed:25822663}.
CC   -!- SUBUNIT: Interacts with EIN2 (via C-terminus).
CC       {ECO:0000269|PubMed:23132950}.
CC   -!- INTERACTION:
CC       Q05609; Q38846: ERS1; NbExp=2; IntAct=EBI-1606697, EBI-1606754;
CC       Q05609; P49333: ETR1; NbExp=6; IntAct=EBI-1606697, EBI-1606682;
CC       Q05609; Q0WPQ2: ETR2; NbExp=2; IntAct=EBI-1606697, EBI-1787533;
CC   -!- TISSUE SPECIFICITY: Expressed in both seedlings and adult plants.
CC       {ECO:0000269|PubMed:8431946}.
CC   -!- DISRUPTION PHENOTYPE: Mutants display ethylene-treated phenotypes,
CC       resulting in plants with small, unexpanded leaves and whose seed
CC       cotyledon growth is impaired. {ECO:0000269|PubMed:8431946}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily. {ECO:0000305}.
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DR   EMBL; L08789; AAA32779.1; -; mRNA.
DR   EMBL; L08790; AAA32780.1; -; Genomic_DNA.
DR   EMBL; AL162506; CAB82938.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90647.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90648.1; -; Genomic_DNA.
DR   PIR; T48400; T48400.
DR   RefSeq; NP_195993.1; NM_120454.4.
DR   RefSeq; NP_850760.1; NM_180429.4.
DR   PDB; 3P86; X-ray; 2.50 A; A/B=540-821.
DR   PDB; 3PPZ; X-ray; 2.99 A; A/B=540-821.
DR   PDBsum; 3P86; -.
DR   PDBsum; 3PPZ; -.
DR   AlphaFoldDB; Q05609; -.
DR   SMR; Q05609; -.
DR   BioGRID; 17024; 8.
DR   IntAct; Q05609; 9.
DR   STRING; 3702.Q05609; -.
DR   iPTMnet; Q05609; -.
DR   PaxDb; 3702-AT5G03730-1; -.
DR   ProteomicsDB; 220456; -.
DR   EnsemblPlants; AT5G03730.1; AT5G03730.1; AT5G03730.
DR   EnsemblPlants; AT5G03730.2; AT5G03730.2; AT5G03730.
DR   GeneID; 831748; -.
DR   Gramene; AT5G03730.1; AT5G03730.1; AT5G03730.
DR   Gramene; AT5G03730.2; AT5G03730.2; AT5G03730.
DR   KEGG; ath:AT5G03730; -.
DR   Araport; AT5G03730; -.
DR   TAIR; AT5G03730; CTR1.
DR   eggNOG; KOG0192; Eukaryota.
DR   HOGENOM; CLU_006806_3_1_1; -.
DR   InParanoid; Q05609; -.
DR   OMA; SGDYYMP; -.
DR   OrthoDB; 1216705at2759; -.
DR   PhylomeDB; Q05609; -.
DR   BRENDA; 2.7.11.1; 399.
DR   PRO; PR:Q05609; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q05609; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
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:TAIR.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:TAIR.
DR   GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009686; P:gibberellin biosynthetic process; IMP:TAIR.
DR   GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; TAS:TAIR.
DR   GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR   GO; GO:2000069; P:regulation of post-embryonic root development; IMP:TAIR.
DR   GO; GO:2000035; P:regulation of stem cell division; IMP:TAIR.
DR   GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR   GO; GO:0009750; P:response to fructose; IMP:TAIR.
DR   GO; GO:0001666; P:response to hypoxia; IMP:TAIR.
DR   GO; GO:0009744; P:response to sucrose; IMP:TAIR.
DR   GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   PANTHER; PTHR23257:SF813; SERINE_THREONINE-PROTEIN KINASE EDR1; 1.
DR   Pfam; PF14381; EDR1; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q05609; AT.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Ethylene signaling pathway; Kinase;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..821
FT                   /note="Serine/threonine-protein kinase CTR1"
FT                   /id="PRO_0000085907"
FT   DOMAIN          551..809
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        676
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         557..565
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         578
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         596
FT                   /note="E->K: In ctr1-4; exhibits ethylene-treated
FT                   phenotype."
FT                   /evidence="ECO:0000269|PubMed:8431946"
FT   MUTAGEN         694
FT                   /note="D->E: In ctr1-1; exhibits ethylene-treated
FT                   phenotype."
FT                   /evidence="ECO:0000269|PubMed:8431946"
FT   HELIX           548..550
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          551..559
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          561..570
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          573..580
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           587..602
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          611..615
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          617..619
FT                   /evidence="ECO:0007829|PDB:3PPZ"
FT   STRAND          622..626
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           633..638
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           642..645
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           648..666
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          668..670
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           679..681
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          682..684
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          690..692
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   STRAND          703..705
FT                   /evidence="ECO:0007829|PDB:3PPZ"
FT   TURN            715..717
FT                   /evidence="ECO:0007829|PDB:3PPZ"
FT   HELIX           720..723
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           732..746
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   TURN            750..753
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           756..765
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           778..787
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           792..794
FT                   /evidence="ECO:0007829|PDB:3P86"
FT   HELIX           798..809
FT                   /evidence="ECO:0007829|PDB:3P86"
SQ   SEQUENCE   821 AA;  90306 MW;  2922D3DCD0CC15BC CRC64;
     MEMPGRRSNY TLLSQFSDDQ VSVSVTGAPP PHYDSLSSEN RSNHNSGNTG KAKAERGGFD
     WDPSGGGGGD HRLNNQPNRV GNNMYASSLG LQRQSSGSSF GESSLSGDYY MPTLSAAANE
     IESVGFPQDD GFRLGFGGGG GDLRIQMAAD SAGGSSSGKS WAQQTEESYQ LQLALALRLS
     SEATCADDPN FLDPVPDESA LRTSPSSAET VSHRFWVNGC LSYYDKVPDG FYMMNGLDPY
     IWTLCIDLHE SGRIPSIESL RAVDSGVDSS LEAIIVDRRS DPAFKELHNR VHDISCSCIT
     TKEVVDQLAK LICNRMGGPV IMGEDELVPM WKECIDGLKE IFKVVVPIGS LSVGLCRHRA
     LLFKVLADII DLPCRIAKGC KYCNRDDAAS CLVRFGLDRE YLVDLVGKPG HLWEPDSLLN
     GPSSISISSP LRFPRPKPVE PAVDFRLLAK QYFSDSQSLN LVFDPASDDM GFSMFHRQYD
     NPGGENDALA ENGGGSLPPS ANMPPQNMMR ASNQIEAAPM NAPPISQPVP NRANRELGLD
     GDDMDIPWCD LNIKEKIGAG SFGTVHRAEW HGSDVAVKIL MEQDFHAERV NEFLREVAIM
     KRLRHPNIVL FMGAVTQPPN LSIVTEYLSR GSLYRLLHKS GAREQLDERR RLSMAYDVAK
     GMNYLHNRNP PIVHRDLKSP NLLVDKKYTV KVCDFGLSRL KASTFLSSKS AAGTPEWMAP
     EVLRDEPSNE KSDVYSFGVI LWELATLQQP WGNLNPAQVV AAVGFKCKRL EIPRNLNPQV
     AAIIEGCWTN EPWKRPSFAT IMDLLRPLIK SAVPPPNRSD L
//