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Protein

F-box protein CPR30

Gene

CPR30

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

Functioni

Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates negatively both salicylic acid (SA)-dependent and SA-independent defense signaling.By similarity1 Publication

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.

GO - Molecular functioni

GO - Biological processi

  • negative regulation of defense response Source: TAIR
  • negative regulation of protein catabolic process Source: TAIR
  • plant-type hypersensitive response Source: UniProtKB-KW
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Hypersensitive response, Plant defense, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
F-box protein CPR30
Alternative name(s):
Protein CONSTITUTIVE EXPRESSER OF PR GENES 30
Gene namesi
Name:CPR30
Ordered Locus Names:At4g12560
ORF Names:T1P17.150
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G12560.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cytoplasm Source: TAIR
  • nucleus Source: TAIR
  • SCF ubiquitin ligase complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Temperature dependent; normal at high temperature (above 28 degrees Celsius), but in colder temperature, dwarf morphology, constitutive resistance to the bacterial pathogen Pseudomonas syringae, and induction of defense-response gene expression such as PR-30.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 413413F-box protein CPR30PRO_0000283502Add
BLAST

Proteomic databases

PaxDbiQ9SU30.

Expressioni

Tissue specificityi

Expressed in seedling, root, stem, leaves, inflorescence and silique, especially in veins and trichomes.1 Publication

Interactioni

Subunit structurei

Part of a SCF (ASK-cullin-F-box) protein ligase complex (By similarity). Interacts with SKP1A/ASK1, SPK1B/ASK2, ASK9, ASK10, ASK11, ASK13, ASK14, ASK16, ASK17, ASK18 and ASK19.By similarity1 Publication

Protein-protein interaction databases

BioGridi12167. 16 interactions.
DIPiDIP-59704N.
STRINGi3702.AT4G12560.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SU30.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 4848F-boxPROSITE-ProRule annotationAdd
BLAST

Domaini

The F-box is necessary for the interaction with ASK proteins.By similarity

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410J96M. Eukaryota.
ENOG4111BET. LUCA.
HOGENOMiHOG000090389.
InParanoidiQ9SU30.
OMAiMILLRGA.
PhylomeDBiQ9SU30.

Family and domain databases

InterProiIPR006527. F-box-assoc_dom_typ1.
IPR017451. F-box-assoc_interact_dom.
IPR001810. F-box_dom.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF07734. FBA_1. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
TIGRFAMsiTIGR01640. F_box_assoc_1. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9SU30-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIPMDIVN DIFLRLPAKT LVRCRALSKP CYHLINDPDF IESHLHRVLQ
60 70 80 90 100
TGDHLMILLR GALRLYSVDL DSLDSVSDVE HPMKRGGPTE VFGSSNGLIG
110 120 130 140 150
LSNSPTDLAV FNPSTRQIHR LPPSSIDLPD GSSTRGYVFY GLGYDSVSDD
160 170 180 190 200
YKVVRMVQFK IDSEDELGCS FPYEVKVFSL KKNSWKRIES VASSIQLLFY
210 220 230 240 250
FYYHLLYRRG YGVLAGNSLH WVLPRRPGLI AFNLIVRFDL ALEEFEIVRF
260 270 280 290 300
PEAVANGNVD IQMDIGVLDG CLCLMCNYDQ SYVDVWMMKE YNVRDSWTKV
310 320 330 340 350
FTVQKPKSVK SFSYMRPLVY SKDKKKVLLE LNNTKLVWFD LESKKMSTLR
360 370 380 390 400
IKDCPSSYSA ELVVSSLVLG CKGDLNNIKY RKEQQAKEAR EAKIMQNTKR
410
RDDFLSKGFK LVL
Length:413
Mass (Da):47,259
Last modified:April 3, 2007 - v2
Checksum:iFFE6E60966C780E4
GO

Sequence cautioni

The sequence CAB41726.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB78299.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti402 – 4021D → G in BAF01202 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL049730 Genomic DNA. Translation: CAB41726.1. Sequence problems.
AL161534 Genomic DNA. Translation: CAB78299.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83147.1.
CP002687 Genomic DNA. Translation: AEE83148.1.
AK229339 mRNA. Translation: BAF01202.1.
PIRiT07648.
RefSeqiNP_001078377.1. NM_001084908.1.
NP_192993.2. NM_117326.3.
UniGeneiAt.33465.

Genome annotation databases

EnsemblPlantsiAT4G12560.1; AT4G12560.1; AT4G12560.
AT4G12560.2; AT4G12560.2; AT4G12560.
GeneIDi826869.
GrameneiAT4G12560.1; AT4G12560.1; AT4G12560.
AT4G12560.2; AT4G12560.2; AT4G12560.
KEGGiath:AT4G12560.

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
AL049730 Genomic DNA. Translation: CAB41726.1. Sequence problems.
AL161534 Genomic DNA. Translation: CAB78299.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE83147.1.
CP002687 Genomic DNA. Translation: AEE83148.1.
AK229339 mRNA. Translation: BAF01202.1.
PIRiT07648.
RefSeqiNP_001078377.1. NM_001084908.1.
NP_192993.2. NM_117326.3.
UniGeneiAt.33465.

3D structure databases

ProteinModelPortaliQ9SU30.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12167. 16 interactions.
DIPiDIP-59704N.
STRINGi3702.AT4G12560.1.

Proteomic databases

PaxDbiQ9SU30.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G12560.1; AT4G12560.1; AT4G12560.
AT4G12560.2; AT4G12560.2; AT4G12560.
GeneIDi826869.
GrameneiAT4G12560.1; AT4G12560.1; AT4G12560.
AT4G12560.2; AT4G12560.2; AT4G12560.
KEGGiath:AT4G12560.

Organism-specific databases

TAIRiAT4G12560.

Phylogenomic databases

eggNOGiENOG410J96M. Eukaryota.
ENOG4111BET. LUCA.
HOGENOMiHOG000090389.
InParanoidiQ9SU30.
OMAiMILLRGA.
PhylomeDBiQ9SU30.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ9SU30.

Family and domain databases

InterProiIPR006527. F-box-assoc_dom_typ1.
IPR017451. F-box-assoc_interact_dom.
IPR001810. F-box_dom.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF07734. FBA_1. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.
TIGRFAMsiTIGR01640. F_box_assoc_1. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "An F-box gene, CPR30, functions as a negative regulator of the defense response in Arabidopsis."
    Gou M., Su N., Zheng J., Huai J., Wu G., Zhao J., He J., Tang D., Yang S., Wang G.
    Plant J. 60:757-770(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SKP1A/ASK1; SPK1B/ASK2; ASK9; ASK10; ASK11; ASK13; ASK14; ASK16; ASK17; ASK18 AND ASK19.

Entry informationi

Entry nameiCPR30_ARATH
AccessioniPrimary (citable) accession number: Q9SU30
Secondary accession number(s): Q0WNU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: June 8, 2016
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.