PRL1_ARATH
ID PRL1_ARATH Reviewed; 486 AA.
AC Q42384;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein pleiotropic regulatory locus 1;
DE Short=Protein PRL1;
DE AltName: Full=MOS4-associated complex protein 2;
DE Short=MAC protein 2;
GN Name=PRL1; Synonyms=MAC2; OrderedLocusNames=At4g15900;
GN ORFNames=dl3990w, FCAALL.40;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH KAP2.
RC STRAIN=cv. Columbia;
RX PubMed=9765207; DOI=10.1101/gad.12.19.3059;
RA Nemeth K., Salchert K., Putnoky P., Bhalerao R., Koncz-Kalman Z.,
RA Stankovic-Stangeland B., Bako L., Mathur J., Oekresz L., Stabel S.,
RA Geigenberger P., Stitt M., Redei G.P., Schell J., Koncz C.;
RT "Pleiotropic control of glucose and hormone responses by PRL1, a nuclear WD
RT protein, in Arabidopsis.";
RL Genes Dev. 12:3059-3073(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [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 REVIEW, AND FUNCTION.
RX PubMed=9800212; DOI=10.1098/rstb.1998.0307;
RA Salchert K., Bhalerao R., Koncz-Kalman Z., Koncz C.;
RT "Control of cell elongation and stress responses by steroid hormones and
RT carbon catabolic repression in plants.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 353:1517-1520(1998).
RN [6]
RP FUNCTION, AND INTERACTION WITH AKIN10; AKIN11 AND PIPC.
RX PubMed=10220464; DOI=10.1073/pnas.96.9.5322;
RA Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L., Muranaka T.,
RA Machida Y., Schell J., Koncz C.;
RT "Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like
RT protein kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999).
RN [7]
RP FUNCTION.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
RT plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, COMPONENT OF THE MAC COMPLEX, AND
RP INTERACTION WITH CDC5.
RX PubMed=17575050; DOI=10.1101/gad.1559607;
RA Palma K., Zhao Q., Cheng Y.T., Bi D., Monaghan J., Cheng W., Zhang Y.,
RA Li X.;
RT "Regulation of plant innate immunity by three proteins in a complex
RT conserved across the plant and animal kingdoms.";
RL Genes Dev. 21:1484-1493(2007).
RN [9]
RP FUNCTION.
RX PubMed=17693536; DOI=10.1105/tpc.106.049965;
RA Li Y., Smith C., Corke F., Zheng L., Merali Z., Ryden P., Derbyshire P.,
RA Waldron K., Bevan M.W.;
RT "Signaling from an altered cell wall to the nucleus mediates sugar-
RT responsive growth and development in Arabidopsis thaliana.";
RL Plant Cell 19:2500-2515(2007).
RN [10]
RP INTERACTION WITH DDB1A, COMPONENT OF THE CUL4-RBX1-DDB1-PRL1 COMPLEX, DWD
RP MOTIFS, AND FUNCTION.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [11]
RP FUNCTION.
RX PubMed=20008452; DOI=10.1093/mp/ssp100;
RA Flores-Perez U., Perez-Gil J., Closa M., Wright L.P., Botella-Pavia P.,
RA Phillips M.A., Ferrer A., Gershenzon J., Rodriguez-Concepcion M.;
RT "PLEIOTROPIC REGULATORY LOCUS 1 (PRL1) integrates the regulation of sugar
RT responses with isoprenoid metabolism in Arabidopsis.";
RL Mol. Plant 3:101-112(2010).
RN [12]
RP FUNCTION.
RX PubMed=19500298; DOI=10.1111/j.1365-313x.2009.03935.x;
RA Baruah A., Simkova K., Hincha D.K., Apel K., Laloi C.;
RT "Modulation of (1)O(2)-mediated retrograde signaling by the PLEIOTROPIC
RT RESPONSE LOCUS 1 (PRL1) protein, a central integrator of stress and energy
RT signaling.";
RL Plant J. 60:22-32(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF THE MAC COMPLEX.
RX PubMed=19629177; DOI=10.1371/journal.ppat.1000526;
RA Monaghan J., Xu F., Gao M., Zhao Q., Palma K., Long C., Chen S., Zhang Y.,
RA Li X.;
RT "Two Prp19-like U-box proteins in the MOS4-associated complex play
RT redundant roles in plant innate immunity.";
RL PLoS Pathog. 5:E1000526-E1000526(2009).
CC -!- FUNCTION: Pleiotropic regulator of glucose, stress and hormone
CC responses. Also regulates cytochrome P450 CYP90A1/CPD. Coordinates the
CC expression of hormone- and stress-related genes and genes related to
CC cell wall modification and growth, leading to altered sugar-dependent
CC growth and developmental responses. Component of the MAC complex that
CC probably regulates defense responses through transcriptional control
CC and thereby is essential for plant innate immunity. By suppressing the
CC expression of several (1)O(2)-responsive genes, PRL1 seems to play a
CC major role in modulating responses of plants to environmental changes
CC by interconnecting (1)O(2)-mediated retrograde signaling with other
CC signaling pathways. Acts as negative regulator of SNF1-related protein
CC kinases AKIN10 and AKIN11 via the inhibition of their interaction with
CC SKP1/ASK1. Component of the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein
CC ligase complex, PRL1 may function as the substrate recognition module
CC within this complex, leading to the AKIN10 degradation.
CC {ECO:0000269|PubMed:10220464, ECO:0000269|PubMed:11387208,
CC ECO:0000269|PubMed:17575050, ECO:0000269|PubMed:17693536,
CC ECO:0000269|PubMed:18223036, ECO:0000269|PubMed:19500298,
CC ECO:0000269|PubMed:20008452, ECO:0000269|PubMed:9765207,
CC ECO:0000269|PubMed:9800212}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the multiprotein assembly MOS4-associated complex
CC (MAC) at least composed of MOS4, CDC5, PRL1 and PRP19 (PubMed:17575050,
CC PubMed:19629177). Interacts with CDC5 (PubMed:17575050). Component of
CC the CUL4-RBX1-DDB1-PRL1 E3 ubiquitin-protein ligase complex. Interacts
CC with DDB1A through its DWD motif (PubMed:18223036). Interacts with
CC AKIN10, AKIN11 and PIPC (PubMed:10220464). Interacts with KAP2
CC (PubMed:9765207). {ECO:0000269|PubMed:10220464,
CC ECO:0000269|PubMed:17575050, ECO:0000269|PubMed:18223036,
CC ECO:0000269|PubMed:19629177, ECO:0000269|PubMed:9765207}.
CC -!- INTERACTION:
CC Q42384; P92948: CDC5; NbExp=2; IntAct=EBI-1382964, EBI-1382948;
CC Q42384; O04294: IMPA3; NbExp=3; IntAct=EBI-1382964, EBI-1644689;
CC Q42384; Q38997-2: KIN10; NbExp=3; IntAct=EBI-1382964, EBI-20798606;
CC Q42384; P92958: KIN11; NbExp=2; IntAct=EBI-1382964, EBI-307202;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9765207}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000269|PubMed:18223036}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to glucose and sucrose. Enhanced
CC sensitivity of plants to stress and to growth hormones including
CC cytokinin, ethylene, abscisic acid, and auxin. Accumulation of sugars
CC and starch in leaves, and root elongation. Cell elongation defects.
CC Enhanced susceptibility to virulent and avirulent pathogens.
CC {ECO:0000269|PubMed:17575050}.
CC -!- SIMILARITY: Belongs to the WD repeat PRL1/PRL2 family. {ECO:0000305}.
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DR EMBL; X82824; CAA58031.1; -; Genomic_DNA.
DR EMBL; X82825; CAA58032.1; -; mRNA.
DR EMBL; Z97339; CAB10369.1; -; Genomic_DNA.
DR EMBL; AL161542; CAB78632.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83664.1; -; Genomic_DNA.
DR PIR; S49820; S49820.
DR RefSeq; NP_193325.1; NM_117682.3.
DR AlphaFoldDB; Q42384; -.
DR SMR; Q42384; -.
DR BioGRID; 12566; 20.
DR IntAct; Q42384; 11.
DR STRING; 3702.AT4G15900.1; -.
DR iPTMnet; Q42384; -.
DR PaxDb; Q42384; -.
DR PRIDE; Q42384; -.
DR ProteomicsDB; 234847; -.
DR EnsemblPlants; AT4G15900.1; AT4G15900.1; AT4G15900.
DR GeneID; 827272; -.
DR Gramene; AT4G15900.1; AT4G15900.1; AT4G15900.
DR KEGG; ath:AT4G15900; -.
DR Araport; AT4G15900; -.
DR TAIR; locus:2005539; AT4G15900.
DR eggNOG; KOG0285; Eukaryota.
DR HOGENOM; CLU_000288_72_2_1; -.
DR InParanoid; Q42384; -.
DR OMA; HPLEWKP; -.
DR OrthoDB; 1157847at2759; -.
DR PhylomeDB; Q42384; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q42384; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42384; baseline and differential.
DR Genevisible; Q42384; AT.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IPI:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0048825; P:cotyledon development; IMP: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:0010154; P:fruit development; IMP:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IMP:TAIR.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IMP:TAIR.
DR GO; GO:0009749; P:response to glucose; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR045241; Prp46/PLRG1-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19923; PTHR19923; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Immunity; Innate immunity; Nucleus; Plant defense; Reference proteome;
KW Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..486
FT /note="Protein pleiotropic regulatory locus 1"
FT /id="PRO_0000051157"
FT REPEAT 174..204
FT /note="WD 1"
FT REPEAT 216..246
FT /note="WD 2"
FT REPEAT 258..288
FT /note="WD 3"
FT REPEAT 300..330
FT /note="WD 4"
FT REPEAT 342..371
FT /note="WD 5"
FT REPEAT 384..413
FT /note="WD 6"
FT REPEAT 433..463
FT /note="WD 7"
FT REGION 62..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..290
FT /note="DWD box 1"
FT MOTIF 317..332
FT /note="DWD box 2"
FT COMPBIAS 71..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 54009 MW; 604D3E6FCDA8A998 CRC64;
MPAPTTEIEP IEAQSLKKLS LKSLKRSLEL FSPVHGQFPP PDPEAKQIRL SHKMKVAFGG
VEPVVSQPPR QPDRINEQPG PSNALSLAAP EGSKSTQKGA TESAIVVGPT LLRPILPKGL
NYTGSSGKST TIIPANVSSY QRNLSTAALM ERIPSRWPRP EWHAPWKNYR VIQGHLGWVR
SVAFDPSNEW FCTGSADRTI KIWDVATGVL KLTLTGHIEQ VRGLAVSNRH TYMFSAGDDK
QVKCWDLEQN KVIRSYHGHL SGVYCLALHP TLDVLLTGGR DSVCRVWDIR TKMQIFALSG
HDNTVCSVFT RPTDPQVVTG SHDTTIKFWD LRYGKTMSTL THHKKSVRAM TLHPKENAFA
SASADNTKKF SLPKGEFCHN MLSQQKTIIN AMAVNEDGVM VTGGDNGSIW FWDWKSGHSF
QQSETIVQPG SLESEAGIYA ACYDNTGSRL VTCEADKTIK MWKEDENATP ETHPINFKPP
KEIRRF
