Reviewed, UniProtKB/Swiss-Prot Q42384 (PRL1_ARATH)

Names and origin

Protein names

Recommended name:
    Protein pleiotropic regulatory locus 1
      Short name=Protein PRL1
Alternative name(s):
    MOS4-associated complex protein 2
      Short name=MAC protein 2

Gene names

Name:	PRL1
Synonyms:	MAC2
Ordered Locus Names:	At4g15900
ORF Names:	dl3990w, FCAALL.40

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Pleiotropic regulator of glucose, stress and hormone responses. Also regulates cytochrome P450 CYP90A1/CPD. Coordinates the expression of hormone- and stress-related genes and genes related to cell wall modification and growth, leading to altered sugar-dependent growth and developmental responses. Component of the MAC complex that probably regulates defense responses through transcriptional control and thereby is essential for plant innate immunity. By suppressing the expression of several (1)O(2)-responsive genes, PRL1 seems to play a major role in modulating responses of plants to environmental changes by interconnecting (1)O(2)-mediated retrograde signaling with other signaling pathways. Acts as negative regulator of SNF1-related protein kinases AKIN10 and AKIN11 via the inhibition of their interaction with SKP1/ASK1. Component of the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein ligase complex, PRL1 may function as the substrate recognition module within this complex, leading to the AKIN10 degradation.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the multiprotein assembly MOS4-associated complex (MAC) at least composed of MOS4, CDC5, PRL1 and PRP19. Interacts with CDC5. Component of the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein ligase complex. Interacts with DDB1A through its DWD motif. Interacts with AKIN10 and AKIN11. Interacts with KAP2.
Subcellular location	Nucleus.
Domain	The DWD box is required for interaction with DDB1A.
Disruption phenotype	Hypersensitivity to glucose and sucrose. Enhanced sensitivity of plants to stress and to growth hormones including cytokinin, ethylene, abscisic acid, and auxin. Accumulation of sugars and starch in leaves, and root elongation. Cell elongation defects. Enhanced susceptibility to virulent and avirulent pathogens.
Sequence similarities	Belongs to the WD repeat PRL1/PRL2 family. Contains 7 WD repeats.

Ontologies

Keywords
Biological process	Immune response Innate immunity Plant defense Ubl conjugation pathway
Cellular component	Nucleus
Domain	Repeat WD repeat
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cotyledon development Ref.9 Inferred from mutant phenotype. Source: TAIR defense response signaling pathway, resistance gene-dependent Ref.7 Inferred from mutant phenotype. Source: TAIR defense response signaling pathway, resistance gene-independent Ref.7 Inferred from mutant phenotype. Source: TAIR defense response to bacterium Ref.7 Inferred from mutant phenotype. Source: TAIR defense response to fungus Ref.7 Inferred from mutant phenotype. Source: TAIR hormone-mediated signaling pathway Ref.9 Inferred from mutant phenotype. Source: TAIR leaf development Ref.9 Inferred from mutant phenotype. Source: TAIR negative regulation of transcription Ref.5 Inferred from mutant phenotype. Source: TAIR proteolysis Ref.9 Inferred from mutant phenotype. Source: TAIR response to glucose stimulus Ref.1 Inferred from mutant phenotype. Source: TAIR root development Ref.9 Inferred from mutant phenotype. Source: TAIR sugar mediated signaling pathway Ref.9 Inferred from mutant phenotype. Source: TAIR
Cellular component	CUL4 RING ubiquitin ligase complex Ref.9 Inferred from physical interaction. Source: TAIR nucleus Ref.1 Inferred from direct assay. Source: TAIR
Molecular function	basal transcription repressor activity Ref.1 Inferred from mutant phenotype. Source: TAIR protein binding Ref.1 Ref.5 Ref.7 Ref.9 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q8LGH4	1	EBI-1382964,EBI-1632927
AtCDC5	P92948	1	EBI-1382964,EBI-1382948
KAP2	O04294	3	EBI-1382964,EBI-1644689
KIN10	Q38997	1	EBI-1382964,EBI-2107143
KIN11	P92958	1	EBI-1382964,EBI-307202
PRKCB	P05771	1	EBI-1382964,EBI-706216	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 486	486	Protein pleiotropic regulatory locus 1		PRO_0000051157
Regions
	Repeat	174 – 204	31	WD 1
	Repeat	216 – 246	31	WD 2
	Repeat	258 – 288	31	WD 3
	Repeat	300 – 330	31	WD 4
	Repeat	342 – 371	30	WD 5
	Repeat	384 – 413	30	WD 6
	Repeat	433 – 463	31	WD 7
	Motif	275 – 290	16	DWD box 1
	Motif	317 – 332	16	DWD box 2

Sequences

	Sequence		Length	Mass (Da)
	Q42384-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 604D3E6FCDA8A998	FASTA	486	54,009
	10 20 30 40 50 60 MPAPTTEIEP IEAQSLKKLS LKSLKRSLEL FSPVHGQFPP PDPEAKQIRL SHKMKVAFGG 70 80 90 100 110 120 VEPVVSQPPR QPDRINEQPG PSNALSLAAP EGSKSTQKGA TESAIVVGPT LLRPILPKGL 130 140 150 160 170 180 NYTGSSGKST TIIPANVSSY QRNLSTAALM ERIPSRWPRP EWHAPWKNYR VIQGHLGWVR 190 200 210 220 230 240 SVAFDPSNEW FCTGSADRTI KIWDVATGVL KLTLTGHIEQ VRGLAVSNRH TYMFSAGDDK 250 260 270 280 290 300 QVKCWDLEQN KVIRSYHGHL SGVYCLALHP TLDVLLTGGR DSVCRVWDIR TKMQIFALSG 310 320 330 340 350 360 HDNTVCSVFT RPTDPQVVTG SHDTTIKFWD LRYGKTMSTL THHKKSVRAM TLHPKENAFA 370 380 390 400 410 420 SASADNTKKF SLPKGEFCHN MLSQQKTIIN AMAVNEDGVM VTGGDNGSIW FWDWKSGHSF 430 440 450 460 470 480 QQSETIVQPG SLESEAGIYA ACYDNTGSRL VTCEADKTIK MWKEDENATP ETHPINFKPP KEIRRF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD protein, in Arabidopsis." Nemeth K., Salchert K., Putnoky P., Bhalerao R., Koncz-Kalman Z., Stankovic-Stangeland B., Bako L., Mathur J., Oekresz L., Stabel S., Geigenberger P., Stitt M., Redei G.P., Schell J., Koncz C. Genes Dev. 12:3059-3073(1998) [PubMed: 9765207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KAP2. Strain: cv. Columbia.
[2]	"Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana." Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E. , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N. Nature 391:485-488(1998) [PubMed: 9461215] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Control of cell elongation and stress responses by steroid hormones and carbon catabolic repression in plants." Salchert K., Bhalerao R., Koncz-Kalman Z., Koncz C. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 353:1517-1520(1998) [PubMed: 9800212] [Abstract] Cited for: REVIEW, FUNCTION.
[5]	"Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases." Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L., Muranaka T., Machida Y., Schell J., Koncz C. Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999) [PubMed: 10220464] [Abstract] Cited for: FUNCTION, INTERACTION WITH AKIN10 AND AKIN11.
[6]	"SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase." Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A., Salchert K., del Pozo C., Schell J., Koncz C. EMBO J. 20:2742-2756(2001) [PubMed: 11387208] [Abstract] Cited for: FUNCTION.
[7]	"Regulation of plant innate immunity by three proteins in a complex conserved across the plant and animal kingdoms." Palma K., Zhao Q., Cheng Y.T., Bi D., Monaghan J., Cheng W., Zhang Y., Li X. Genes Dev. 21:1484-1493(2007) [PubMed: 17575050] [Abstract] Cited for: DISRUPTION PHENOTYPE, FUNCTION, COMPONENT OF THE MAC COMPLEX, INTERACTION WITH CDC5.
[8]	"Signaling from an altered cell wall to the nucleus mediates sugar-responsive growth and development in Arabidopsis thaliana." Li Y., Smith C., Corke F., Zheng L., Merali Z., Ryden P., Derbyshire P., Waldron K., Bevan M.W. Plant Cell 19:2500-2515(2007) [PubMed: 17693536] [Abstract] Cited for: FUNCTION.
[9]	"Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases." Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H., He Y.J., Xiong Y., Deng X.W. Plant Cell 20:152-167(2008) [PubMed: 18223036] [Abstract] Cited for: INTERACTION WITH DDB1A, COMPONENT OF THE CUL4-RBX1-DDB1-PRL1 COMPLEX, DWD MOTIFS, FUNCTION.
[10]	"PLEIOTROPIC REGULATORY LOCUS 1 (PRL1) integrates the regulation of sugar responses with isoprenoid metabolism in Arabidopsis." Flores-Perez U., Perez-Gil J., Closa M., Wright L.P., Botella-Pavia P., Phillips M.A., Ferrer A., Gershenzon J., Rodriguez-Concepcion M. Mol. Plant 0:0-0(2009) [PubMed: 20008452] [Abstract] Cited for: FUNCTION.
[11]	"Modulation of (1)O(2)-mediated retrograde signaling by the PLEIOTROPIC RESPONSE LOCUS 1 (PRL1) protein, a central integrator of stress and energy signaling." Baruah A., Simkova K., Hincha D.K., Apel K., Laloi C. Plant J. 60:22-32(2009) [PubMed: 19500298] [Abstract] Cited for: FUNCTION.
[12]	"Two Prp19-like U-box proteins in the MOS4-associated complex play redundant roles in plant innate immunity." Monaghan J., Xu F., Gao M., Zhao Q., Palma K., Long C., Chen S., Zhang Y., Li X. PLoS Pathog. 5:E1000526-E1000526(2009) [PubMed: 19629177] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, COMPONENT OF THE MAC COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X82824 Genomic DNA. Translation: CAA58031.1. X82825 mRNA. Translation: CAA58032.1. Z97339 Genomic DNA. Translation: CAB10369.1. AL161542 Genomic DNA. Translation: CAB78632.1.
IPI	IPI00524936.
PIR	S49820.
RefSeq	NP_193325.1.
UniGene	At.103
3D structure databases
SMR	Q42384. Positions 170-463.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q42384. 10 interactions.
STRING	Q42384.
Proteomic databases
PRIDE	Q42384.
Genome annotation databases
GeneID	827272.
GenomeReviews	Gene locus AT4G15900 in contig CT486007_GR.
KEGG	ath:AT4G15900.
NMPDR	fig|3702.1.peg.19342.
Organism-specific databases
GeneFarm	2847. 267.
TAIR	At4g15900.
Phylogenomic databases
HOGENOM	HBG630928.
InParanoid	Q42384.
OMA	KFPDGNF.
PhylomeDB	Q42384.
Gene expression databases
Genevestigator	Q42384.
GermOnline	AT4G15900. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR020472. G-protein_beta_WD-40_rep_reg. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019782. WD40_repeat_2. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00400. WD40. 7 hits. [Graphical view]
PRINTS	PR00320. GPROTEINBRPT.
SMART	SM00320. WD40. 7 hits. [Graphical view]
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 5 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRL1_ARATH

Accession

Primary (citable) accession number: Q42384

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)