COI1_ARATH
ID COI1_ARATH Reviewed; 592 AA.
AC O04197; B2BD84;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Coronatine-insensitive protein 1;
DE AltName: Full=COI-1;
DE AltName: Full=F-box/LRR-repeat protein 2;
DE Short=AtCOI1;
DE Short=AtFBL2;
GN Name=COI1; Synonyms=FBL2; OrderedLocusNames=At2g39940; ORFNames=T28M21.10;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9582125; DOI=10.1126/science.280.5366.1091;
RA Xie D., Feys B.F., James S., Nieto-Rostro M., Turner J.G.;
RT "COI1: an Arabidopsis gene required for jasmonate-regulated defense and
RT fertility.";
RL Science 280:1091-1094(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Aa-0, cv. Ak-1, cv. Bay-0, cv. C24, cv. Columbia, cv. Cvi-0,
RC cv. Di-0, cv. Ei-2, cv. Gu-0, cv. HOG, cv. Landsberg erecta, cv. Lz-0,
RC cv. Nd-1, cv. Sha, cv. Sorbo, cv. Tsu-0, cv. Wassilewskija, and cv. Wei-0;
RA Caldwell K.S., Michelmore R.W.;
RT "Genes encoding defense signaling proteins in plants show weaker signatures
RT of selection than those encoding recognition proteins.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=12244256; DOI=10.2307/3869877;
RA Feys B.J.F., Benedetti C.S., Penfold C.N., Turner J.G.;
RT "Arabidopsis mutants selected for resistance to the phytotoxin coronatine
RT are male sterile, insensitive to methyl jasmonate, and resistant to a
RT bacterial pathogen.";
RL Plant Cell 6:751-759(1994).
RN [7]
RP FUNCTION.
RX PubMed=10810145; DOI=10.2307/3870996;
RA Reymond P., Weber H., Damond M., Farmer E.E.;
RT "Differential gene expression in response to mechanical wounding and insect
RT feeding in Arabidopsis.";
RL Plant Cell 12:707-720(2000).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11077244; DOI=10.1016/s1360-1385(00)01769-6;
RA Xiao W., Jang J.-C.;
RT "F-box proteins in Arabidopsis.";
RL Trends Plant Sci. 5:454-457(2000).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF LEU-245.
RX PubMed=12172836; DOI=10.1007/s00425-002-0787-4;
RA Ellis C., Turner J.G.;
RT "A conditionally fertile coi1 allele indicates cross-talk between plant
RT hormone signalling pathways in Arabidopsis thaliana seeds and young
RT seedlings.";
RL Planta 215:549-556(2002).
RN [10]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-22.
RX PubMed=12172031; DOI=10.1105/tpc.003368;
RA Xu L., Liu F., Lechner E., Genschik P., Crosby W.L., Ma H., Peng W.,
RA Huang D., Xie D.;
RT "The SCF(COI1) ubiquitin-ligase complexes are required for jasmonate
RT response in Arabidopsis.";
RL Plant Cell 14:1919-1935(2002).
RN [11]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-11; TRP-44 AND LEU-245.
RX PubMed=12445118; DOI=10.1046/j.1365-313x.2002.01432.x;
RA Devoto A., Nieto-Rostro M., Xie D., Ellis C., Harmston R., Patrick E.,
RA Davis J., Sherratt L., Coleman M., Turner J.G.;
RT "COI1 links jasmonate signalling and fertility to the SCF ubiquitin-ligase
RT complex in Arabidopsis.";
RL Plant J. 32:457-466(2002).
RN [12]
RP DOMAIN LEUCINE-RICH REPEATS.
RX PubMed=12008900; DOI=10.1023/a:1014440531842;
RA Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
RT "Cloning by pathway activation in yeast: identification of an Arabidopsis
RT thaliana F-box protein that can turn on glucose repression.";
RL Plant Mol. Biol. 49:69-79(2002).
RN [13]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12724535; DOI=10.1105/tpc.010207;
RA Feng S., Ma L., Wang X., Xie D., Dinesh-Kumar S.P., Wei N., Deng X.W.;
RT "The COP9 signalosome interacts physically with SCF COI1 and modulates
RT jasmonate responses.";
RL Plant Cell 15:1083-1094(2003).
RN [14]
RP FUNCTION.
RX PubMed=12805591; DOI=10.1104/pp.103.022186;
RA van Wees S.C.M., Chang H.-S., Zhu T., Glazebrook J.;
RT "Characterization of the early response of Arabidopsis to Alternaria
RT brassicicola infection using expression profiling.";
RL Plant Physiol. 132:606-617(2003).
RN [15]
RP INTERACTION WITH SKP1A/ASK1; SKP1B/ASK2; ASK11 AND ASK12.
RX PubMed=14749489; DOI=10.1093/pcp/pch009;
RA Takahashi N., Kuroda H., Kuromori T., Hirayama T., Seki M., Shinozaki K.,
RA Shimada H., Matsui M.;
RT "Expression and interaction analysis of Arabidopsis Skp1-related genes.";
RL Plant Cell Physiol. 45:83-91(2004).
RN [16]
RP FUNCTION.
RX PubMed=14756769; DOI=10.1111/j.1365-313x.2003.01986.x;
RA He P., Chintamanani S., Chen Z., Zhu L., Kunkel B.N., Alfano J.R., Tang X.,
RA Zhou J.-M.;
RT "Activation of a COI1-dependent pathway in Arabidopsis by Pseudomonas
RT syringae type III effectors and coronatine.";
RL Plant J. 37:589-602(2004).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS)1-592 IN COMPLEX WITH
RP JASMONOYL-ISOLEUCINE AND CORONATINE, INTERACTION WITH SKP1A AND TIFY10A,
RP AND MUTAGENESIS OF ARG-85; MET-88; PHE-89; ARG-121; LEU-301; TYR-302;
RP ARG-326; ARG-348; ARG-351; TYR-386; ARG-409; TYR-444; LEU-469 AND ARG-496.
RX PubMed=20927106; DOI=10.1038/nature09430;
RA Sheard L.B., Tan X., Mao H., Withers J., Ben-Nissan G., Hinds T.R.,
RA Kobayashi Y., Hsu F.F., Sharon M., Browse J., He S.Y., Rizo J., Howe G.A.,
RA Zheng N.;
RT "Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-
RT receptor.";
RL Nature 468:400-405(2010).
CC -!- FUNCTION: Required for jasmonate-regulated plant fertility and defense
CC processes, and for coronatine and/or other elicitors
CC perceptions/responses. Seems to not be required for meiosis. Required
CC for the regulation of some genes induced by wounding, but not for all.
CC Component of SCF(COI1) E3 ubiquitin ligase complexes, which may mediate
CC the ubiquitination and subsequent proteasomal degradation of target
CC proteins (probably including the ribulose bisphosphate carboxylase
CC small chain 1B RBCS-1B and the histone deacetylase HDA6). These SCF
CC complexes play crucial roles in regulating response to jasmonate, and
CC their interactions with the COP9 signalosome (CSN) appear to be
CC important for their activity. Interacts with TIFY10A and inositol
CC pentakisphosphate to form a high-affinity jasmonates coreceptor.
CC Involved in the regulation of plant gene expression during plant-
CC pathogen interactions with Pseudomonas syringae and Alternaria
CC brassicicola. {ECO:0000269|PubMed:10810145,
CC ECO:0000269|PubMed:12172031, ECO:0000269|PubMed:12172836,
CC ECO:0000269|PubMed:12244256, ECO:0000269|PubMed:12445118,
CC ECO:0000269|PubMed:12724535, ECO:0000269|PubMed:12805591,
CC ECO:0000269|PubMed:14756769, ECO:0000269|PubMed:9582125}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of SCF(COI1) E3 ubiquitin ligase complexes at least
CC composed of ASK1 or ASK2, CUL1, RBX1A or RBX1B and COI1. Interacts with
CC ASK1 and ASK2, but separately, Binds also to ASK11 and ASK12. Interacts
CC with RBCS-1B and HDA6. SCF complexes interact with the COP9 signalosome
CC (CSN). Interacts with TIFY10A. {ECO:0000269|PubMed:12172031,
CC ECO:0000269|PubMed:12445118, ECO:0000269|PubMed:12724535,
CC ECO:0000269|PubMed:14749489, ECO:0000269|PubMed:20927106}.
CC -!- INTERACTION:
CC O04197; Q94AH6: CUL1; NbExp=3; IntAct=EBI-401159, EBI-532411;
CC O04197; Q9FML2: HDA6; NbExp=3; IntAct=EBI-401159, EBI-639608;
CC O04197; Q39255: SKP1A; NbExp=11; IntAct=EBI-401159, EBI-532357;
CC O04197; Q9FHW7: SKP1B; NbExp=6; IntAct=EBI-401159, EBI-604076;
CC O04197; Q9LMA8: TIFY10A; NbExp=10; IntAct=EBI-401159, EBI-1388539;
CC O04197; Q9LVI4: TIFY6B; NbExp=6; IntAct=EBI-401159, EBI-1792431;
CC O04197; Q8W4J8: TIFY7; NbExp=7; IntAct=EBI-401159, EBI-1792583;
CC -!- DOMAIN: The F-box domain is essential for the formation of SFC(COI1)
CC complexes. {ECO:0000269|PubMed:12008900}.
CC -!- DOMAIN: The Leu-rich domain is involved in the interactions with RBCS-
CC 1B and RPD3B. {ECO:0000269|PubMed:12008900}.
CC -!- DISRUPTION PHENOTYPE: Mutants coi1-1 to coi1-14 are male sterile,
CC insensitive to MeJA and coronatine, and exhibit enhanced resistance to
CC Pseudomonas syringae atropurpurea (coronatine producing strain). Mutant
CC coi1-16 has reduced sensitivity to jasmonate, but is male fertile when
CC grown below 22 degrees Celsius and male sterile otherwise.
CC {ECO:0000269|PubMed:9582125}.
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DR EMBL; AF036340; AAC17498.1; -; mRNA.
DR EMBL; EF470606; ABR45936.1; -; Genomic_DNA.
DR EMBL; EF470607; ABR45937.1; -; Genomic_DNA.
DR EMBL; EF470608; ABR45938.1; -; Genomic_DNA.
DR EMBL; EF470609; ABR45939.1; -; Genomic_DNA.
DR EMBL; EF470610; ABR45940.1; -; Genomic_DNA.
DR EMBL; EF470611; ABR45941.1; -; Genomic_DNA.
DR EMBL; EF470612; ABR45942.1; -; Genomic_DNA.
DR EMBL; EF470613; ABR45943.1; -; Genomic_DNA.
DR EMBL; EF470614; ABR45944.1; -; Genomic_DNA.
DR EMBL; EF470615; ABR45945.1; -; Genomic_DNA.
DR EMBL; EF470616; ABR45946.1; -; Genomic_DNA.
DR EMBL; EF470617; ABR45947.1; -; Genomic_DNA.
DR EMBL; EF470619; ABR45949.1; -; Genomic_DNA.
DR EMBL; EF470620; ABR45950.1; -; Genomic_DNA.
DR EMBL; EF470621; ABR45951.1; -; Genomic_DNA.
DR EMBL; EF470622; ABR45952.1; -; Genomic_DNA.
DR EMBL; EF470623; ABR45953.1; -; Genomic_DNA.
DR EMBL; EF470624; ABR45954.1; -; Genomic_DNA.
DR EMBL; AF002109; AAB95279.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09753.1; -; Genomic_DNA.
DR EMBL; AY045625; AAK73983.1; -; mRNA.
DR EMBL; AY133556; AAM91386.1; -; mRNA.
DR PIR; T52139; T52139.
DR RefSeq; NP_565919.1; NM_129552.4.
DR PDB; 3OGK; X-ray; 2.80 A; B/D/F/H/J/L/N/P=1-592.
DR PDB; 3OGL; X-ray; 3.18 A; B/D/F/H/J/L/N/P=1-592.
DR PDB; 3OGM; X-ray; 3.34 A; B/D/F/H/J/L/N/P=1-592.
DR PDBsum; 3OGK; -.
DR PDBsum; 3OGL; -.
DR PDBsum; 3OGM; -.
DR AlphaFoldDB; O04197; -.
DR SMR; O04197; -.
DR BioGRID; 3919; 21.
DR ComplexPortal; CPX-1339; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
DR ComplexPortal; CPX-1429; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
DR ComplexPortal; CPX-1430; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
DR ComplexPortal; CPX-1431; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
DR ComplexPortal; CPX-1432; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
DR ComplexPortal; CPX-1433; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK6.
DR ComplexPortal; CPX-1434; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
DR ComplexPortal; CPX-1435; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK8.
DR ComplexPortal; CPX-1436; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK9.
DR ComplexPortal; CPX-1437; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK10.
DR ComplexPortal; CPX-1438; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
DR ComplexPortal; CPX-1439; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
DR ComplexPortal; CPX-1440; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
DR ComplexPortal; CPX-1441; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14.
DR ComplexPortal; CPX-1442; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15.
DR ComplexPortal; CPX-1443; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK16.
DR ComplexPortal; CPX-1444; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK17.
DR ComplexPortal; CPX-1445; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
DR ComplexPortal; CPX-1446; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK19.
DR ComplexPortal; CPX-1447; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
DR ComplexPortal; CPX-1448; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK21.
DR ComplexPortal; CPX-1449; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1450; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1451; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR ComplexPortal; CPX-1452; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1453; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1454; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
DR ComplexPortal; CPX-1455; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR ComplexPortal; CPX-1456; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
DR ComplexPortal; CPX-1457; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
DR ComplexPortal; CPX-1458; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
DR ComplexPortal; CPX-1459; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1460; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1461; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR ComplexPortal; CPX-1462; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
DR ComplexPortal; CPX-1463; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
DR ComplexPortal; CPX-1464; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
DR ComplexPortal; CPX-1465; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
DR ComplexPortal; CPX-1466; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1467; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
DR ComplexPortal; CPX-1468; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1469; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
DR ComplexPortal; CPX-1471; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
DR ComplexPortal; CPX-1472; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
DR ComplexPortal; CPX-1473; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
DR ComplexPortal; CPX-1474; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
DR ComplexPortal; CPX-1475; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
DR ComplexPortal; CPX-1476; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK6.
DR ComplexPortal; CPX-1477; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
DR ComplexPortal; CPX-1478; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK8.
DR ComplexPortal; CPX-1479; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK9.
DR ComplexPortal; CPX-1480; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK10.
DR ComplexPortal; CPX-1481; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
DR ComplexPortal; CPX-1482; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
DR ComplexPortal; CPX-1483; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
DR ComplexPortal; CPX-1484; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK14.
DR ComplexPortal; CPX-1485; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK15.
DR ComplexPortal; CPX-1486; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK16.
DR ComplexPortal; CPX-1487; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK17.
DR ComplexPortal; CPX-1488; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
DR ComplexPortal; CPX-1489; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK19.
DR ComplexPortal; CPX-1490; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
DR ComplexPortal; CPX-1491; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK21.
DR ComplexPortal; CPX-1492; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
DR ComplexPortal; CPX-1493; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
DR ComplexPortal; CPX-1494; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
DR ComplexPortal; CPX-1495; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
DR ComplexPortal; CPX-1496; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
DR ComplexPortal; CPX-1497; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK6.
DR ComplexPortal; CPX-1498; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
DR ComplexPortal; CPX-1499; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK8.
DR ComplexPortal; CPX-1502; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK9.
DR ComplexPortal; CPX-1503; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK10.
DR ComplexPortal; CPX-1504; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
DR ComplexPortal; CPX-1505; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
DR ComplexPortal; CPX-1506; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
DR ComplexPortal; CPX-1507; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK14.
DR ComplexPortal; CPX-1508; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK15.
DR ComplexPortal; CPX-1509; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK16.
DR ComplexPortal; CPX-1510; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK17.
DR ComplexPortal; CPX-1511; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
DR ComplexPortal; CPX-1512; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK19.
DR ComplexPortal; CPX-1513; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
DR ComplexPortal; CPX-1514; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK21.
DR DIP; DIP-31324N; -.
DR IntAct; O04197; 14.
DR STRING; 3702.AT2G39940.1; -.
DR PaxDb; O04197; -.
DR PRIDE; O04197; -.
DR ProteomicsDB; 241009; -.
DR EnsemblPlants; AT2G39940.1; AT2G39940.1; AT2G39940.
DR GeneID; 818581; -.
DR Gramene; AT2G39940.1; AT2G39940.1; AT2G39940.
DR KEGG; ath:AT2G39940; -.
DR Araport; AT2G39940; -.
DR TAIR; locus:2061136; AT2G39940.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_2_0_1; -.
DR InParanoid; O04197; -.
DR OMA; CYTATPD; -.
DR OrthoDB; 444688at2759; -.
DR PhylomeDB; O04197; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; O04197; -.
DR PRO; PR:O04197; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04197; baseline and differential.
DR Genevisible; O04197; AT.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0009901; P:anther dehiscence; IMP:CACAO.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; TAS:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0010218; P:response to far red light; IMP:TAIR.
DR GO; GO:0009625; P:response to insect; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:TAIR.
DR GO; GO:0009641; P:shade avoidance; IMP:TAIR.
DR GO; GO:0048443; P:stamen development; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR041567; COI1_F-box.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR041101; Transp_inhibit.
DR Pfam; PF18511; F-box_5; 1.
DR Pfam; PF18791; Transp_inhibit; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Jasmonic acid signaling pathway; Leucine-rich repeat;
KW Plant defense; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..592
FT /note="Coronatine-insensitive protein 1"
FT /id="PRO_0000119960"
FT DOMAIN 16..57
FT /note="F-box"
FT REPEAT 58..82
FT /note="LRR 1"
FT REPEAT 83..102
FT /note="LRR 2"
FT REPEAT 103..120
FT /note="LRR 3"
FT REPEAT 121..154
FT /note="LRR 4"
FT REPEAT 155..182
FT /note="LRR 5"
FT REPEAT 183..210
FT /note="LRR 6"
FT REPEAT 211..236
FT /note="LRR 7"
FT REPEAT 237..264
FT /note="LRR 8"
FT REPEAT 265..283
FT /note="LRR 8"
FT REPEAT 284..308
FT /note="LRR 10"
FT REPEAT 309..332
FT /note="LRR 11"
FT REPEAT 333..368
FT /note="LRR 12"
FT REPEAT 369..393
FT /note="LRR 13"
FT REPEAT 394..426
FT /note="LRR 14"
FT REPEAT 427..456
FT /note="LRR 15"
FT REPEAT 457..478
FT /note="LRR 16"
FT REPEAT 479..500
FT /note="LRR 17"
FT REPEAT 501..524
FT /note="LRR 18"
FT BINDING 85
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:20927106,
FT ECO:0007744|PDB:3OGK, ECO:0007744|PDB:3OGL,
FT ECO:0007744|PDB:3OGM"
FT BINDING 348
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:20927106,
FT ECO:0007744|PDB:3OGK, ECO:0007744|PDB:3OGL,
FT ECO:0007744|PDB:3OGM"
FT BINDING 386
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:20927106,
FT ECO:0007744|PDB:3OGK, ECO:0007744|PDB:3OGM"
FT BINDING 409
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:20927106,
FT ECO:0007744|PDB:3OGK, ECO:0007744|PDB:3OGL,
FT ECO:0007744|PDB:3OGM"
FT BINDING 496
FT /ligand="jasmonate"
FT /ligand_id="ChEBI:CHEBI:58431"
FT /evidence="ECO:0000269|PubMed:20927106,
FT ECO:0007744|PDB:3OGL, ECO:0007744|PDB:3OGM"
FT MUTAGEN 11
FT /note="L->A: No effects on interactions."
FT /evidence="ECO:0000269|PubMed:12445118"
FT MUTAGEN 22
FT /note="E->A: Abrogates SFC(COI1) complexes formation, loss
FT of response to jasmonate."
FT /evidence="ECO:0000269|PubMed:12172031"
FT MUTAGEN 44
FT /note="W->A: Abrogates SFC(COI1) complexes formation and of
FT interactions with RBCS-1B and RPD3B, loss of response to
FT jasmonate."
FT /evidence="ECO:0000269|PubMed:12445118"
FT MUTAGEN 85
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 88
FT /note="M->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 89
FT /note="F->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 121
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 245
FT /note="L->F: In coi1-16; abrogates interactions with RBCS-
FT 1B and RPD3B (coi1-16)."
FT /evidence="ECO:0000269|PubMed:12172836,
FT ECO:0000269|PubMed:12445118"
FT MUTAGEN 301
FT /note="L->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 302
FT /note="Y->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 326
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 348
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 351
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 386
FT /note="Y->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 409
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 444
FT /note="Y->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 469
FT /note="L->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT MUTAGEN 496
FT /note="R->A: Loss of interaction with TIFY10A."
FT /evidence="ECO:0000269|PubMed:20927106"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3OGL"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3OGK"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3OGL"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 392..401
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 477..484
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 502..511
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:3OGK"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 540..545
FT /evidence="ECO:0007829|PDB:3OGK"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:3OGK"
SQ SEQUENCE 592 AA; 67665 MW; 1DDCF04990144C06 CRC64;
MEDPDIKRCK LSCVATVDDV IEQVMTYITD PKDRDSASLV CRRWFKIDSE TREHVTMALC
YTATPDRLSR RFPNLRSLKL KGKPRAAMFN LIPENWGGYV TPWVTEISNN LRQLKSVHFR
RMIVSDLDLD RLAKARADDL ETLKLDKCSG FTTDGLLSIV THCRKIKTLL MEESSFSEKD
GKWLHELAQH NTSLEVLNFY MTEFAKISPK DLETIARNCR SLVSVKVGDF EILELVGFFK
AAANLEEFCG GSLNEDIGMP EKYMNLVFPR KLCRLGLSYM GPNEMPILFP FAAQIRKLDL
LYALLETEDH CTLIQKCPNL EVLETRNVIG DRGLEVLAQY CKQLKRLRIE RGADEQGMED
EEGLVSQRGL IALAQGCQEL EYMAVYVSDI TNESLESIGT YLKNLCDFRL VLLDREERIT
DLPLDNGVRS LLIGCKKLRR FAFYLRQGGL TDLGLSYIGQ YSPNVRWMLL GYVGESDEGL
MEFSRGCPNL QKLEMRGCCF SERAIAAAVT KLPSLRYLWV QGYRASMTGQ DLMQMARPYW
NIELIPSRRV PEVNQQGEIR EMEHPAHILA YYSLAGQRTD CPTTVRVLKE PI
