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Q05609 (CTR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase CTR1

EC=2.7.11.1
Gene names
Name:CTR1
Ordered Locus Names:At5g03730
ORF Names:F17C15_150
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a negative regulator in the ethylene response pathway. Ref.1

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Tissue specificity

Expressed in both seedlings and adult plants. Ref.1

Disruption phenotype

Mutants display ethylene-treated phenotypes, resulting in plants with small, unexpanded leaves and whose seed cotyledon growth is impaired. Ref.1

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. RAF subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processEthylene signaling pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to iron ion

Inferred from expression pattern PubMed 20627899. Source: TAIR

ethylene-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

gibberellin biosynthetic process

Inferred from mutant phenotype PubMed 17389366. Source: TAIR

negative regulation of ethylene-activated signaling pathway

Traceable author statement PubMed 12535337PubMed 12821658Ref.1PubMed 9560288. Source: TAIR

protein autophosphorylation

Inferred from direct assay PubMed 21477822. Source: TAIR

regulation of post-embryonic root development

Inferred from mutant phenotype PubMed 17656722. Source: TAIR

regulation of stem cell division

Inferred from mutant phenotype PubMed 17656722. Source: TAIR

regulation of timing of transition from vegetative to reproductive phase

Inferred from mutant phenotype PubMed 17389366. Source: TAIR

response to ethylene

Inferred from mutant phenotype Ref.1. Source: TAIR

response to fructose

Inferred from mutant phenotype PubMed 21253566. Source: TAIR

response to sucrose

Inferred from mutant phenotype PubMed 11162499. Source: TAIR

sugar mediated signaling pathway

Traceable author statement PubMed 12663220. Source: TAIR

   Cellular_componentendoplasmic reticulum membrane

Inferred from direct assay PubMed 12821658. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 12177468PubMed 12837948PubMed 8417317PubMed 9560288. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay PubMed 12535337PubMed 21477822. Source: TAIR

protein serine/threonine/tyrosine kinase activity

Inferred from sequence or structural similarity PubMed 16429265. Source: TAIR

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 821821Serine/threonine-protein kinase CTR1
PRO_0000085907

Regions

Domain551 – 809259Protein kinase
Nucleotide binding557 – 5659ATP By similarity
Compositional bias65 – 695Poly-Gly
Compositional bias135 – 1417Poly-Gly

Sites

Active site6761Proton acceptor By similarity
Binding site5781ATP By similarity

Experimental info

Mutagenesis5961E → K in ctr1-4; exhibits ethylene-treated phenotype.
Mutagenesis6941D → E in ctr1-1; exhibits ethylene-treated phenotype.

Secondary structure

............................................... 821
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05609 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 2922D3DCD0CC15BC

FASTA82190,306
        10         20         30         40         50         60 
MEMPGRRSNY TLLSQFSDDQ VSVSVTGAPP PHYDSLSSEN RSNHNSGNTG KAKAERGGFD 

        70         80         90        100        110        120 
WDPSGGGGGD HRLNNQPNRV GNNMYASSLG LQRQSSGSSF GESSLSGDYY MPTLSAAANE 

       130        140        150        160        170        180 
IESVGFPQDD GFRLGFGGGG GDLRIQMAAD SAGGSSSGKS WAQQTEESYQ LQLALALRLS 

       190        200        210        220        230        240 
SEATCADDPN FLDPVPDESA LRTSPSSAET VSHRFWVNGC LSYYDKVPDG FYMMNGLDPY 

       250        260        270        280        290        300 
IWTLCIDLHE SGRIPSIESL RAVDSGVDSS LEAIIVDRRS DPAFKELHNR VHDISCSCIT 

       310        320        330        340        350        360 
TKEVVDQLAK LICNRMGGPV IMGEDELVPM WKECIDGLKE IFKVVVPIGS LSVGLCRHRA 

       370        380        390        400        410        420 
LLFKVLADII DLPCRIAKGC KYCNRDDAAS CLVRFGLDRE YLVDLVGKPG HLWEPDSLLN 

       430        440        450        460        470        480 
GPSSISISSP LRFPRPKPVE PAVDFRLLAK QYFSDSQSLN LVFDPASDDM GFSMFHRQYD 

       490        500        510        520        530        540 
NPGGENDALA ENGGGSLPPS ANMPPQNMMR ASNQIEAAPM NAPPISQPVP NRANRELGLD 

       550        560        570        580        590        600 
GDDMDIPWCD LNIKEKIGAG SFGTVHRAEW HGSDVAVKIL MEQDFHAERV NEFLREVAIM 

       610        620        630        640        650        660 
KRLRHPNIVL FMGAVTQPPN LSIVTEYLSR GSLYRLLHKS GAREQLDERR RLSMAYDVAK 

       670        680        690        700        710        720 
GMNYLHNRNP PIVHRDLKSP NLLVDKKYTV KVCDFGLSRL KASTFLSSKS AAGTPEWMAP 

       730        740        750        760        770        780 
EVLRDEPSNE KSDVYSFGVI LWELATLQQP WGNLNPAQVV AAVGFKCKRL EIPRNLNPQV 

       790        800        810        820 
AAIIEGCWTN EPWKRPSFAT IMDLLRPLIK SAVPPPNRSD L 

« Hide

References

« Hide 'large scale' references
[1]"CTR1, a negative regulator of the ethylene response pathway in Arabidopsis, encodes a member of the raf family of protein kinases."
Kieber J.J., Rothenberg M., Roman G., Feldmann K.A., Ecker J.R.
Cell 72:427-441(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
Tissue: Seedling.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08789 mRNA. Translation: AAA32779.1.
L08790 Genomic DNA. Translation: AAA32780.1.
AL162506 Genomic DNA. Translation: CAB82938.1.
CP002688 Genomic DNA. Translation: AED90647.1.
CP002688 Genomic DNA. Translation: AED90648.1.
PIRT48400.
RefSeqNP_195993.1. NM_120454.3.
NP_850760.1. NM_180429.3.
UniGeneAt.300.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P86X-ray2.50A/B540-821[»]
3PPZX-ray2.99A/B540-821[»]
ProteinModelPortalQ05609.
SMRQ05609. Positions 540-810.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid17024. 6 interactions.
IntActQ05609. 4 interactions.
STRING3702.AT5G03730.1-P.

Proteomic databases

PaxDbQ05609.
PRIDEQ05609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G03730.1; AT5G03730.1; AT5G03730.
AT5G03730.2; AT5G03730.2; AT5G03730.
GeneID831748.
KEGGath:AT5G03730.

Organism-specific databases

GeneFarm884.
TAIRAT5G03730.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000239752.
InParanoidQ05609.
KOK14510.
OMAPSFATIM.
PhylomeDBQ05609.

Enzyme and pathway databases

BioCycARA:AT5G03730-MONOMER.
ARA:GQT-223-MONOMER.
BRENDA2.7.11.1. 399.

Gene expression databases

ArrayExpressQ05609.
GenevestigatorQ05609.

Family and domain databases

InterProIPR028324. CTR1.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERPTHR23257:SF384. PTHR23257:SF384. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCTR1_ARATH
AccessionPrimary (citable) accession number: Q05609
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names