PKS4_ARATH
ID PKS4_ARATH Reviewed; 406 AA.
AC Q9FYE2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein PHYTOCHROME KINASE SUBSTRATE 4;
GN Name=PKS4; OrderedLocusNames=At5g04190; ORFNames=F21E1.110;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16170454; DOI=10.1007/s00239-004-0294-2;
RA Lariguet P., Dunand C.;
RT "Plant photoreceptors: phylogenetic overview.";
RL J. Mol. Evol. 61:559-569(2005).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16777956; DOI=10.1073/pnas.0603799103;
RA Lariguet P., Schepens I., Hodgson D., Pedmale U.V., Trevisan M., Kami C.,
RA de Carbonnel M., Alonso J.M., Ecker J.R., Liscum E., Fankhauser C.;
RT "PHYTOCHROME KINASE SUBSTRATE 1 is a phototropin 1 binding protein required
RT for phototropism.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10134-10139(2006).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18024556; DOI=10.1104/pp.107.106468;
RA Boccalandro H.E., De Simone S.N., Bergmann-Honsberger A., Schepens I.,
RA Fankhauser C., Casal J.J.;
RT "PHYTOCHROME KINASE SUBSTRATE1 regulates root phototropism and
RT gravitropism.";
RL Plant Physiol. 146:108-115(2008).
RN [7]
RP FUNCTION, INTERACTION WITH PHYA AND PHYB, INDUCTION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18390804; DOI=10.1104/pp.108.118166;
RA Schepens I., Boccalandro H.E., Kami C., Casal J.J., Fankhauser C.;
RT "PHYTOCHROME KINASE SUBSTRATE4 modulates phytochrome-mediated control of
RT hypocotyl growth orientation.";
RL Plant Physiol. 147:661-671(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20071603; DOI=10.1104/pp.109.150441;
RA de Carbonnel M., Davis P., Roelfsema M.R., Inoue S., Schepens I.,
RA Lariguet P., Geisler M., Shimazaki K., Hangarter R., Fankhauser C.;
RT "The Arabidopsis PHYTOCHROME KINASE SUBSTRATE2 protein is a phototropin
RT signaling element that regulates leaf flattening and leaf positioning.";
RL Plant Physiol. 152:1391-1405(2010).
CC -!- FUNCTION: Modulates phytochrome-mediated control of hypocotyl growth
CC orientation. Involved in PHYA and PHYB signaling. Acts as an inhibitor
CC of asymmetric growth. Not involved in the control of leaf flattening.
CC {ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:18390804,
CC ECO:0000269|PubMed:20071603}.
CC -!- SUBUNIT: Interacts in vitro with PHYA and PHYB.
CC {ECO:0000269|PubMed:18390804}.
CC -!- INTERACTION:
CC Q9FYE2; Q1ECQ5: At4g02485; NbExp=3; IntAct=EBI-25513821, EBI-25519982;
CC Q9FYE2; Q17TI5: BRX; NbExp=3; IntAct=EBI-25513821, EBI-4426649;
CC -!- TISSUE SPECIFICITY: Expressed in the hypocotyl elongation zone. Not
CC found in the root elongation zone. {ECO:0000269|PubMed:18390804}.
CC -!- INDUCTION: Down-regulated by light. {ECO:0000269|PubMed:18390804}.
CC -!- DISRUPTION PHENOTYPE: Reduced phototropic response. Altered light-
CC induced deviation from vertical growth and decreased phytochrome-
CC mediated inhibition of hypocotyl elongation and cotyledon opening. No
CC visible phenotype at the level of leaf flattening and leaf positioning.
CC No effect on negative root phototropism. {ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:18024556, ECO:0000269|PubMed:18390804,
CC ECO:0000269|PubMed:20071603}.
CC -!- MISCELLANEOUS: PKS1, PKS2 and/or PKS4 are essential for phototropism
CC but not for inhibition of gravitropism under long-term blue light
CC irradiation.
CC -!- SIMILARITY: Belongs to the PKS family. {ECO:0000305}.
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DR EMBL; AL391716; CAC05501.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90709.1; -; Genomic_DNA.
DR EMBL; BT015323; AAT99802.1; -; mRNA.
DR EMBL; BT021129; AAX22264.1; -; mRNA.
DR RefSeq; NP_196039.1; NM_120501.3.
DR AlphaFoldDB; Q9FYE2; -.
DR BioGRID; 15577; 4.
DR IntAct; Q9FYE2; 2.
DR STRING; 3702.AT5G04190.1; -.
DR iPTMnet; Q9FYE2; -.
DR PaxDb; Q9FYE2; -.
DR PRIDE; Q9FYE2; -.
DR ProteomicsDB; 226180; -.
DR EnsemblPlants; AT5G04190.1; AT5G04190.1; AT5G04190.
DR GeneID; 830297; -.
DR Gramene; AT5G04190.1; AT5G04190.1; AT5G04190.
DR KEGG; ath:AT5G04190; -.
DR Araport; AT5G04190; -.
DR TAIR; locus:2146638; AT5G04190.
DR eggNOG; ENOG502QWEH; Eukaryota.
DR HOGENOM; CLU_722304_0_0_1; -.
DR InParanoid; Q9FYE2; -.
DR OMA; CNPRSIS; -.
DR OrthoDB; 903048at2759; -.
DR PhylomeDB; Q9FYE2; -.
DR PRO; PR:Q9FYE2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FYE2; baseline and differential.
DR Genevisible; Q9FYE2; AT.
DR GO; GO:0009638; P:phototropism; IGI:TAIR.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR039615; PKS.
DR InterPro; IPR039820; PSK4.
DR PANTHER; PTHR33781; PTHR33781; 1.
DR PANTHER; PTHR33781:SF1; PTHR33781:SF1; 1.
PE 1: Evidence at protein level;
KW Phytochrome signaling pathway; Reference proteome.
FT CHAIN 1..406
FT /note="Protein PHYTOCHROME KINASE SUBSTRATE 4"
FT /id="PRO_0000393343"
FT REGION 106..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 44458 MW; 392006A37FD3039E CRC64;
MAQTTVTVVA TKRDALDPYI KILQNRSNDI DVSFSSYLKP DNNEQQQKEN EDTELSIFEA
RSYFSENGSN DSRCQTRNLS GPRFSSVASA KVSSFTVGQT ASSEASWNSQ TGLLSNKNRQ
GSDRDGRRSS KKGPRWFFRR RACPCSSSKS VQVQESKPRI AVPKTGSDRI VSNRIVHSHQ
TISSPEPIRL TIPSNTVTRS IDYTANKEAR APVSNFSFPT LNETSQLSEN PKNPVLNHIK
PVRIEPALLP IKPVLNPTSP KGVIIDEEAT SDASSDLFEI ESFSTQTAAR PWAPPVRDSM
EETVSEYGYE PSEASVTWSV MTAEPASAVA ANFSRIALSS SSTAFSGYDK KRTGLLNCHC
EKAVMVNGDK RLVQPVKSVG VQNDVAGKVL CNNGSSKLSV TSRPRQ