CPR1_ARATH
ID CPR1_ARATH Reviewed; 413 AA.
AC Q9SU30; Q0WNU7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=F-box protein CPR1;
DE AltName: Full=Protein CONSTITUTIVE EXPRESSER OF PR GENES 1;
DE AltName: Full=Protein CONSTITUTIVE EXPRESSER OF PR GENES 30 {ECO:0000303|PubMed:19682297};
GN Name=CPR1; Synonyms=CPR30 {ECO:0000303|PubMed:19682297};
GN OrderedLocusNames=At4g12560; ORFNames=T1P17.150;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH SKP1A/ASK1; SPK1B/ASK2; ASK9; ASK10; ASK11; ASK13;
RP ASK14; ASK16; ASK17; ASK18 AND ASK19.
RX PubMed=19682297; DOI=10.1111/j.1365-313x.2009.03995.x;
RA Gou M., Su N., Zheng J., Huai J., Wu G., Zhao J., He J., Tang D., Yang S.,
RA Wang G.;
RT "An F-box gene, CPR30, functions as a negative regulator of the defense
RT response in Arabidopsis.";
RL Plant J. 60:757-770(2009).
RN [5]
RP INTERACTION WITH TRAF1B.
RX PubMed=26867179; DOI=10.1016/j.chom.2016.01.005;
RA Huang S., Chen X., Zhong X., Li M., Ao K., Huang J., Li X.;
RT "Plant TRAF proteins regulate NLR immune receptor turnover.";
RL Cell Host Microbe 19:204-215(2016).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins (By similarity). Regulates
CC negatively both salicylic acid (SA)-dependent and SA-independent
CC defense signaling. {ECO:0000250, ECO:0000269|PubMed:19682297}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (ASK-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with SKP1A/ASK1, SPK1B/ASK2, ASK9, ASK10, ASK11,
CC ASK13, ASK14, ASK16, ASK17, ASK18 and ASK19. Interacts with TRAF1B
CC (PubMed:26867179). {ECO:0000250, ECO:0000269|PubMed:19682297,
CC ECO:0000269|PubMed:26867179}.
CC -!- INTERACTION:
CC Q9SU30; O23530: SNC1; NbExp=2; IntAct=EBI-15941797, EBI-15866586;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19682297}. Nucleus
CC {ECO:0000269|PubMed:19682297}.
CC -!- TISSUE SPECIFICITY: Expressed in seedling, root, stem, leaves,
CC inflorescence and silique, especially in veins and trichomes.
CC {ECO:0000269|PubMed:19682297}.
CC -!- DOMAIN: The F-box is necessary for the interaction with ASK proteins.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Temperature dependent; normal at high temperature
CC (above 28 degrees Celsius), but in colder temperature, dwarf
CC morphology, constitutive resistance to the bacterial pathogen
CC Pseudomonas syringae, and induction of defense-response gene expression
CC such as PR-30. {ECO:0000269|PubMed:19682297}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41726.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049730; CAB41726.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161534; CAB78299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83147.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83148.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66283.1; -; Genomic_DNA.
DR EMBL; AK229339; BAF01202.1; -; mRNA.
DR PIR; T07648; T07648.
DR RefSeq; NP_001078377.1; NM_001084908.2.
DR RefSeq; NP_001328191.1; NM_001340790.1.
DR RefSeq; NP_192993.2; NM_117326.4.
DR AlphaFoldDB; Q9SU30; -.
DR BioGRID; 12167; 16.
DR DIP; DIP-59704N; -.
DR IntAct; Q9SU30; 2.
DR STRING; 3702.AT4G12560.2; -.
DR PaxDb; Q9SU30; -.
DR PRIDE; Q9SU30; -.
DR ProteomicsDB; 224542; -.
DR EnsemblPlants; AT4G12560.1; AT4G12560.1; AT4G12560.
DR EnsemblPlants; AT4G12560.2; AT4G12560.2; AT4G12560.
DR EnsemblPlants; AT4G12560.3; AT4G12560.3; AT4G12560.
DR GeneID; 826869; -.
DR Gramene; AT4G12560.1; AT4G12560.1; AT4G12560.
DR Gramene; AT4G12560.2; AT4G12560.2; AT4G12560.
DR Gramene; AT4G12560.3; AT4G12560.3; AT4G12560.
DR KEGG; ath:AT4G12560; -.
DR Araport; AT4G12560; -.
DR TAIR; locus:2135615; AT4G12560.
DR eggNOG; ENOG502QVMN; Eukaryota.
DR HOGENOM; CLU_027176_1_2_1; -.
DR InParanoid; Q9SU30; -.
DR OMA; LMCNYDQ; -.
DR OrthoDB; 584641at2759; -.
DR PhylomeDB; Q9SU30; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SU30; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SU30; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006527; F-box-assoc_dom_typ1.
DR InterPro; IPR017451; F-box-assoc_interact_dom.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF00646; F-box; 1.
DR Pfam; PF07734; FBA_1; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR TIGRFAMs; TIGR01640; F_box_assoc_1; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hypersensitive response; Nucleus; Plant defense;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..413
FT /note="F-box protein CPR1"
FT /id="PRO_0000283502"
FT DOMAIN 1..48
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT CONFLICT 402
FT /note="D -> G (in Ref. 3; BAF01202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 47259 MW; FFE6E60966C780E4 CRC64;
MATIPMDIVN DIFLRLPAKT LVRCRALSKP CYHLINDPDF IESHLHRVLQ TGDHLMILLR
GALRLYSVDL DSLDSVSDVE HPMKRGGPTE VFGSSNGLIG LSNSPTDLAV FNPSTRQIHR
LPPSSIDLPD GSSTRGYVFY GLGYDSVSDD YKVVRMVQFK IDSEDELGCS FPYEVKVFSL
KKNSWKRIES VASSIQLLFY FYYHLLYRRG YGVLAGNSLH WVLPRRPGLI AFNLIVRFDL
ALEEFEIVRF PEAVANGNVD IQMDIGVLDG CLCLMCNYDQ SYVDVWMMKE YNVRDSWTKV
FTVQKPKSVK SFSYMRPLVY SKDKKKVLLE LNNTKLVWFD LESKKMSTLR IKDCPSSYSA
ELVVSSLVLG CKGDLNNIKY RKEQQAKEAR EAKIMQNTKR RDDFLSKGFK LVL
