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Protein

Coronatine-insensitive protein 1

Gene

COI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for jasmonate-regulated plant fertility and defense processes, and for coronatine and/or other elicitors perceptions/responses. Seems to not be required for meiosis. Required for the regulation of some genes induced by wounding, but not for all. Component of SCF(COI1) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (probably including the ribulose bisphosphate carboxylase small chain 1B RBCS-1B and the histone deacetylase HDA6). These SCF complexes play crucial roles in regulating response to jasmonate, and their interactions with the COP9 signalosome (CSN) appear to be important for their activity. Interacts with TIFY10A and inositol pentakisphosphate to form a high-affinity jasmonates coreceptor. Involved in the regulation of plant gene expression during plant-pathogen interactions with Pseudomonas syringae and Alternaria brassicicola.9 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei85JasmonateCombined sources1 Publication1
Binding sitei348JasmonateCombined sources1 Publication1
Binding sitei386JasmonateCombined sources1 Publication1
Binding sitei409JasmonateCombined sources1 Publication1
Binding sitei496JasmonateCombined sources1 Publication1

GO - Biological processi

  • anther dehiscence Source: CACAO
  • defense response Source: TAIR
  • defense response to bacterium Source: TAIR
  • defense response to fungus Source: TAIR
  • jasmonic acid and ethylene-dependent systemic resistance Source: TAIR
  • jasmonic acid mediated signaling pathway Source: TAIR
  • negative regulation of defense response Source: TAIR
  • protein ubiquitination Source: UniProtKB-UniPathway
  • regulation of flower development Source: TAIR
  • response to far red light Source: TAIR
  • response to insect Source: TAIR
  • response to jasmonic acid Source: TAIR
  • response to wounding Source: TAIR
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: TAIR
  • shade avoidance Source: TAIR
  • stomatal movement Source: TAIR
Complete GO annotation...

Keywords - Biological processi

Jasmonic acid signaling pathway, Plant defense, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Coronatine-insensitive protein 1
Alternative name(s):
COI-1
F-box/LRR-repeat protein 2
Short name:
AtCOI1
Short name:
AtFBL2
Gene namesi
Name:COI1
Synonyms:FBL2
Ordered Locus Names:At2g39940
ORF Names:T28M21.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G39940.

Pathology & Biotechi

Disruption phenotypei

Mutants coi1-1 to coi1-14 are male sterile, insensitive to MeJA and coronatine, and exhibit enhanced resistance to Pseudomonas syringae atropurpurea (coronatine producing strain). Mutant coi1-16 has reduced sensitivity to jasmonate, but is male fertile when grown below 22 degrees Celsius and male sterile otherwise.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11L → A: No effects on interactions. 1 Publication1
Mutagenesisi22E → A: Abrogates SFC(COI1) complexes formation, loss of response to jasmonate. 1 Publication1
Mutagenesisi44W → A: Abrogates SFC(COI1) complexes formation and of interactions with RBCS-1B and RPD3B, loss of response to jasmonate. 1 Publication1
Mutagenesisi85R → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi88M → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi89F → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi121R → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi245L → F in coi1-16; abrogates interactions with RBCS-1B and RPD3B (coi1-16). 2 Publications1
Mutagenesisi301L → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi302Y → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi326R → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi348R → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi351R → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi386Y → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi409R → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi444Y → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi469L → A: Loss of interaction with TIFY10A. 1 Publication1
Mutagenesisi496R → A: Loss of interaction with TIFY10A. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001199601 – 592Coronatine-insensitive protein 1Add BLAST592

Proteomic databases

PaxDbiO04197.

Expressioni

Gene expression databases

GenevisibleiO04197. AT.

Interactioni

Subunit structurei

Component of SCF(COI1) E3 ubiquitin ligase complexes at least composed of ASK1 or ASK2, CUL1, RBX1A or RBX1B and COI1. Interacts with ASK1 and ASK2, but separately, Binds also to ASK11 and ASK12. Interacts with RBCS-1B and HDA6. SCF complexes interact with the COP9 signalosome (CSN). Interacts with TIFY10A.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CUL1Q94AH63EBI-401159,EBI-532411
HDA6Q9FML23EBI-401159,EBI-639608
SKP1AQ392557EBI-401159,EBI-532357
SKP1BQ9FHW76EBI-401159,EBI-604076
TIFY10AQ9LMA85EBI-401159,EBI-1388539
TIFY6BQ9LVI46EBI-401159,EBI-1792431
TIFY7Q8W4J85EBI-401159,EBI-1792583

Protein-protein interaction databases

BioGridi3919. 20 interactors.
DIPiDIP-31324N.
IntActiO04197. 13 interactors.
STRINGi3702.AT2G39940.1.

Structurei

Secondary structure

1592
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 19Combined sources3
Helixi21 – 25Combined sources5
Helixi31 – 37Combined sources7
Helixi42 – 51Combined sources10
Beta strandi54 – 58Combined sources5
Helixi60 – 62Combined sources3
Helixi65 – 71Combined sources7
Beta strandi76 – 81Combined sources6
Helixi85 – 89Combined sources5
Helixi94 – 96Combined sources3
Helixi101 – 110Combined sources10
Beta strandi116 – 121Combined sources6
Helixi126 – 136Combined sources11
Helixi137 – 139Combined sources3
Beta strandi142 – 147Combined sources6
Beta strandi149 – 152Combined sources4
Helixi153 – 162Combined sources10
Beta strandi167 – 170Combined sources4
Beta strandi175 – 177Combined sources3
Helixi182 – 190Combined sources9
Beta strandi196 – 198Combined sources3
Helixi209 – 218Combined sources10
Beta strandi224 – 226Combined sources3
Helixi232 – 235Combined sources4
Helixi236 – 241Combined sources6
Beta strandi247 – 250Combined sources4
Beta strandi262 – 264Combined sources3
Beta strandi274 – 277Combined sources4
Turni282 – 284Combined sources3
Helixi285 – 294Combined sources10
Beta strandi297 – 300Combined sources4
Helixi307 – 314Combined sources8
Beta strandi322 – 326Combined sources5
Helixi327 – 329Combined sources3
Helixi330 – 340Combined sources11
Beta strandi346 – 350Combined sources5
Beta strandi355 – 362Combined sources8
Helixi367 – 376Combined sources10
Beta strandi381 – 388Combined sources8
Helixi392 – 401Combined sources10
Beta strandi407 – 412Combined sources6
Helixi425 – 434Combined sources10
Beta strandi440 – 444Combined sources5
Helixi447 – 449Combined sources3
Helixi452 – 460Combined sources9
Beta strandi467 – 470Combined sources4
Helixi477 – 484Combined sources8
Beta strandi492 – 497Combined sources6
Helixi502 – 511Combined sources10
Beta strandi517 – 522Combined sources6
Helixi532 – 535Combined sources4
Beta strandi540 – 545Combined sources6
Beta strandi567 – 572Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OGKX-ray2.80B/D/F/H/J/L/N/P1-592[»]
3OGLX-ray3.18B/D/F/H/J/L/N/P1-592[»]
3OGMX-ray3.34B/D/F/H/J/L/N/P1-592[»]
ProteinModelPortaliO04197.
SMRiO04197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO04197.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 57F-boxAdd BLAST42
Repeati58 – 82LRR 1Add BLAST25
Repeati83 – 102LRR 2Add BLAST20
Repeati103 – 120LRR 3Add BLAST18
Repeati121 – 154LRR 4Add BLAST34
Repeati155 – 182LRR 5Add BLAST28
Repeati183 – 210LRR 6Add BLAST28
Repeati211 – 236LRR 7Add BLAST26
Repeati237 – 264LRR 8Add BLAST28
Repeati265 – 283LRR 8Add BLAST19
Repeati284 – 308LRR 10Add BLAST25
Repeati309 – 332LRR 11Add BLAST24
Repeati333 – 368LRR 12Add BLAST36
Repeati369 – 393LRR 13Add BLAST25
Repeati394 – 426LRR 14Add BLAST33
Repeati427 – 456LRR 15Add BLAST30
Repeati457 – 478LRR 16Add BLAST22
Repeati479 – 500LRR 17Add BLAST22
Repeati501 – 524LRR 18Add BLAST24

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi102 – 517Leu-richAdd BLAST416

Domaini

The F-box domain is essential for the formation of SFC(COI1) complexes.1 Publication
The Leu-rich domain is involved in the interactions with RBCS-1B and RPD3B.1 Publication

Sequence similaritiesi

Contains 1 F-box domain.Curated
Contains 18 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG1947. Eukaryota.
ENOG410XQ54. LUCA.
HOGENOMiHOG000238474.
InParanoidiO04197.
KOiK13463.
OMAiGFCYAVE.
OrthoDBiEOG093604QH.
PhylomeDBiO04197.

Family and domain databases

Gene3Di3.80.10.10. 3 hits.
InterProiIPR032675. L_dom-like.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O04197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDPDIKRCK LSCVATVDDV IEQVMTYITD PKDRDSASLV CRRWFKIDSE
60 70 80 90 100
TREHVTMALC YTATPDRLSR RFPNLRSLKL KGKPRAAMFN LIPENWGGYV
110 120 130 140 150
TPWVTEISNN LRQLKSVHFR RMIVSDLDLD RLAKARADDL ETLKLDKCSG
160 170 180 190 200
FTTDGLLSIV THCRKIKTLL MEESSFSEKD GKWLHELAQH NTSLEVLNFY
210 220 230 240 250
MTEFAKISPK DLETIARNCR SLVSVKVGDF EILELVGFFK AAANLEEFCG
260 270 280 290 300
GSLNEDIGMP EKYMNLVFPR KLCRLGLSYM GPNEMPILFP FAAQIRKLDL
310 320 330 340 350
LYALLETEDH CTLIQKCPNL EVLETRNVIG DRGLEVLAQY CKQLKRLRIE
360 370 380 390 400
RGADEQGMED EEGLVSQRGL IALAQGCQEL EYMAVYVSDI TNESLESIGT
410 420 430 440 450
YLKNLCDFRL VLLDREERIT DLPLDNGVRS LLIGCKKLRR FAFYLRQGGL
460 470 480 490 500
TDLGLSYIGQ YSPNVRWMLL GYVGESDEGL MEFSRGCPNL QKLEMRGCCF
510 520 530 540 550
SERAIAAAVT KLPSLRYLWV QGYRASMTGQ DLMQMARPYW NIELIPSRRV
560 570 580 590
PEVNQQGEIR EMEHPAHILA YYSLAGQRTD CPTTVRVLKE PI
Length:592
Mass (Da):67,665
Last modified:July 1, 1997 - v1
Checksum:i1DDCF04990144C06
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036340 mRNA. Translation: AAC17498.1.
EF470606 Genomic DNA. Translation: ABR45936.1.
EF470607 Genomic DNA. Translation: ABR45937.1.
EF470608 Genomic DNA. Translation: ABR45938.1.
EF470609 Genomic DNA. Translation: ABR45939.1.
EF470610 Genomic DNA. Translation: ABR45940.1.
EF470611 Genomic DNA. Translation: ABR45941.1.
EF470612 Genomic DNA. Translation: ABR45942.1.
EF470613 Genomic DNA. Translation: ABR45943.1.
EF470614 Genomic DNA. Translation: ABR45944.1.
EF470615 Genomic DNA. Translation: ABR45945.1.
EF470616 Genomic DNA. Translation: ABR45946.1.
EF470617 Genomic DNA. Translation: ABR45947.1.
EF470619 Genomic DNA. Translation: ABR45949.1.
EF470620 Genomic DNA. Translation: ABR45950.1.
EF470621 Genomic DNA. Translation: ABR45951.1.
EF470622 Genomic DNA. Translation: ABR45952.1.
EF470623 Genomic DNA. Translation: ABR45953.1.
EF470624 Genomic DNA. Translation: ABR45954.1.
AF002109 Genomic DNA. Translation: AAB95279.1.
CP002685 Genomic DNA. Translation: AEC09753.1.
AY045625 mRNA. Translation: AAK73983.1.
AY133556 mRNA. Translation: AAM91386.1.
PIRiT52139.
RefSeqiNP_565919.1. NM_129552.4.
UniGeneiAt.20831.
At.71018.

Genome annotation databases

EnsemblPlantsiAT2G39940.1; AT2G39940.1; AT2G39940.
GeneIDi818581.
GrameneiAT2G39940.1; AT2G39940.1; AT2G39940.
KEGGiath:AT2G39940.

Cross-referencesi

Web resourcesi

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036340 mRNA. Translation: AAC17498.1.
EF470606 Genomic DNA. Translation: ABR45936.1.
EF470607 Genomic DNA. Translation: ABR45937.1.
EF470608 Genomic DNA. Translation: ABR45938.1.
EF470609 Genomic DNA. Translation: ABR45939.1.
EF470610 Genomic DNA. Translation: ABR45940.1.
EF470611 Genomic DNA. Translation: ABR45941.1.
EF470612 Genomic DNA. Translation: ABR45942.1.
EF470613 Genomic DNA. Translation: ABR45943.1.
EF470614 Genomic DNA. Translation: ABR45944.1.
EF470615 Genomic DNA. Translation: ABR45945.1.
EF470616 Genomic DNA. Translation: ABR45946.1.
EF470617 Genomic DNA. Translation: ABR45947.1.
EF470619 Genomic DNA. Translation: ABR45949.1.
EF470620 Genomic DNA. Translation: ABR45950.1.
EF470621 Genomic DNA. Translation: ABR45951.1.
EF470622 Genomic DNA. Translation: ABR45952.1.
EF470623 Genomic DNA. Translation: ABR45953.1.
EF470624 Genomic DNA. Translation: ABR45954.1.
AF002109 Genomic DNA. Translation: AAB95279.1.
CP002685 Genomic DNA. Translation: AEC09753.1.
AY045625 mRNA. Translation: AAK73983.1.
AY133556 mRNA. Translation: AAM91386.1.
PIRiT52139.
RefSeqiNP_565919.1. NM_129552.4.
UniGeneiAt.20831.
At.71018.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OGKX-ray2.80B/D/F/H/J/L/N/P1-592[»]
3OGLX-ray3.18B/D/F/H/J/L/N/P1-592[»]
3OGMX-ray3.34B/D/F/H/J/L/N/P1-592[»]
ProteinModelPortaliO04197.
SMRiO04197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3919. 20 interactors.
DIPiDIP-31324N.
IntActiO04197. 13 interactors.
STRINGi3702.AT2G39940.1.

Proteomic databases

PaxDbiO04197.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G39940.1; AT2G39940.1; AT2G39940.
GeneIDi818581.
GrameneiAT2G39940.1; AT2G39940.1; AT2G39940.
KEGGiath:AT2G39940.

Organism-specific databases

TAIRiAT2G39940.

Phylogenomic databases

eggNOGiKOG1947. Eukaryota.
ENOG410XQ54. LUCA.
HOGENOMiHOG000238474.
InParanoidiO04197.
KOiK13463.
OMAiGFCYAVE.
OrthoDBiEOG093604QH.
PhylomeDBiO04197.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

EvolutionaryTraceiO04197.
PROiO04197.

Gene expression databases

GenevisibleiO04197. AT.

Family and domain databases

Gene3Di3.80.10.10. 3 hits.
InterProiIPR032675. L_dom-like.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOI1_ARATH
AccessioniPrimary (citable) accession number: O04197
Secondary accession number(s): B2BD84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.