CTR1_ARATH
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 03-AUG-2022, entry version 173.
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; 8.
DR STRING; 3702.AT5G03730.1; -.
DR iPTMnet; Q05609; -.
DR PaxDb; Q05609; -.
DR PRIDE; Q05609; -.
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; locus:2144613; AT5G03730.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_006806_3_1_1; -.
DR InParanoid; Q05609; -.
DR OMA; HELCPRW; -.
DR OrthoDB; 285142at2759; -.
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 Genevisible; Q05609; AT.
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 InterPro; IPR028324; CTR1.
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; PTHR44329:SF149; PTHR44329:SF149; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
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 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
