PKS1_ARATH
ID PKS1_ARATH Reviewed; 439 AA.
AC Q9SWI1; O80610;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Protein PHYTOCHROME KINASE SUBSTRATE 1;
GN Name=PKS1; OrderedLocusNames=At2g02950; ORFNames=T17M13.12;
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 [MRNA], FUNCTION, INTERACTION WITH PHYA AND PHYB,
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=10348744; DOI=10.1126/science.284.5419.1539;
RA Fankhauser C., Yeh K.C., Lagarias J.C., Zhang H., Elich T.D., Chory J.;
RT "PKS1, a substrate phosphorylated by phytochrome that modulates light
RT signaling in Arabidopsis.";
RL Science 284:1539-1541(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, INDUCTION, TISSUE SPECIFICITY, INTERACTION WITH PKS2, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14615593; DOI=10.1105/tpc.014563;
RA Lariguet P., Boccalandro H.E., Alonso J.M., Ecker J.R., Chory J.,
RA Casal J.J., Fankhauser C.;
RT "A growth regulatory loop that provides homeostasis to phytochrome a
RT signaling.";
RL Plant Cell 15:2966-2978(2003).
RN [6]
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 [7]
RP INDUCTION.
RX PubMed=16908503; DOI=10.1093/jxb/erl086;
RA Molas M.L., Kiss J.Z., Correll M.J.;
RT "Gene profiling of the red light signalling pathways in roots.";
RL J. Exp. Bot. 57:3217-3229(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION,
RP INTERACTION WITH PHOT1 AND RPT3, 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 [9]
RP FUNCTION, TISSUE SPECIFICITY, AND 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 [10]
RP FUNCTION, INTERACTION WITH PKS1; RPT3; PHOT1 AND PHOT2, SUBCELLULAR
RP LOCATION, 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: May be responsible for light-regulated cytoplasmic
CC sequestration of phytochromes or may be a negative regulator of
CC phytochrome B signaling. Component of the network that modulates the
CC very low-fluence response (VLFR) branch of phyA signaling. Acts
CC positively in PHOT1 signaling. Regulates phytochrome-mediated
CC photomorphogenesis and hypocotyl phototropism. Involved in the control
CC of leaf flattening and leaf positioning. Promotes negative root
CC phototropism and negatively regulates root gravitropism. May act by
CC controlling auxin homeostasis. {ECO:0000269|PubMed:10348744,
CC ECO:0000269|PubMed:14615593, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:18024556, ECO:0000269|PubMed:20071603}.
CC -!- SUBUNIT: Interacts with PKS2, RPT3, PHOT1, PHOT2 and the C-termini of
CC both phytochromes A (phyA) and B (phyB). Binds both spectral forms of
CC phytochrome, Pr and Pfr. {ECO:0000269|PubMed:10348744,
CC ECO:0000269|PubMed:14615593, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:20071603}.
CC -!- INTERACTION:
CC Q9SWI1; O22286: BPM3; NbExp=3; IntAct=EBI-626200, EBI-540923;
CC Q9SWI1; Q17TI5: BRX; NbExp=3; IntAct=EBI-626200, EBI-4426649;
CC Q9SWI1; O48963: PHOT1; NbExp=3; IntAct=EBI-626200, EBI-1553849;
CC Q9SWI1; P14712: PHYA; NbExp=3; IntAct=EBI-626200, EBI-624446;
CC Q9SWI1; P14713: PHYB; NbExp=2; IntAct=EBI-626200, EBI-300727;
CC Q9SWI1; Q9FMF5: RPT3; NbExp=2; IntAct=EBI-626200, EBI-1553842;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10348744,
CC ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20071603}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10348744,
CC ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20071603}.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings in both darkness and
CC light. Moderate in leaves and very low in roots and flowers. Expressed
CC in the elongation zone of the root and hypocotyl.
CC {ECO:0000269|PubMed:10348744, ECO:0000269|PubMed:14615593,
CC ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:18024556}.
CC -!- DEVELOPMENTAL STAGE: Decreases with development.
CC {ECO:0000269|PubMed:10348744}.
CC -!- INDUCTION: Up-regulated by white, red, far-red and blue light.
CC {ECO:0000269|PubMed:14615593, ECO:0000269|PubMed:16908503}.
CC -!- PTM: Phosphorylated on Ser and to a lower extent on Thr by
CC phytochromes. Phosphorylation is stimulated twofold by red light.
CC {ECO:0000269|PubMed:10348744, ECO:0000269|PubMed:16777956}.
CC -!- DISRUPTION PHENOTYPE: Increased hypocotyl growth inhibition and
CC cotyledon unfolding responses in the very low fluence response (VLFR)
CC mode. Reduced phototropic response. Reduced hyponasty when grown under
CC blue light. Loss of negative root phototropism. Auxin accumulation in
CC protoplasts. {ECO:0000269|PubMed:14615593, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:18024556, 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; AF149053; AAD38033.1; -; mRNA.
DR EMBL; AC004138; AAC32913.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05643.1; -; Genomic_DNA.
DR EMBL; AF325064; AAK17132.1; -; mRNA.
DR EMBL; AY052708; AAK96612.1; -; mRNA.
DR EMBL; AY063721; AAL36071.1; -; mRNA.
DR PIR; E84442; E84442.
DR PIR; T52304; T52304.
DR RefSeq; NP_565292.1; NM_126347.3.
DR AlphaFoldDB; Q9SWI1; -.
DR BioGRID; 225; 8.
DR DIP; DIP-34783N; -.
DR IntAct; Q9SWI1; 9.
DR STRING; 3702.AT2G02950.1; -.
DR iPTMnet; Q9SWI1; -.
DR PaxDb; Q9SWI1; -.
DR PRIDE; Q9SWI1; -.
DR ProteomicsDB; 236164; -.
DR EnsemblPlants; AT2G02950.1; AT2G02950.1; AT2G02950.
DR GeneID; 814823; -.
DR Gramene; AT2G02950.1; AT2G02950.1; AT2G02950.
DR KEGG; ath:AT2G02950; -.
DR Araport; AT2G02950; -.
DR TAIR; locus:2056695; AT2G02950.
DR eggNOG; ENOG502QSBI; Eukaryota.
DR HOGENOM; CLU_048817_0_0_1; -.
DR InParanoid; Q9SWI1; -.
DR OMA; MSCKSHK; -.
DR OrthoDB; 841461at2759; -.
DR PhylomeDB; Q9SWI1; -.
DR PRO; PR:Q9SWI1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SWI1; baseline and differential.
DR Genevisible; Q9SWI1; AT.
DR GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009638; P:phototropism; IGI:TAIR.
DR GO; GO:0009958; P:positive gravitropism; IMP: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; IMP:TAIR.
DR GO; GO:0010218; P:response to far red light; IEP:TAIR.
DR GO; GO:0010114; P:response to red light; IEP:TAIR.
DR InterPro; IPR039615; PKS.
DR InterPro; IPR039821; PSK1/PSK2.
DR PANTHER; PTHR33781; PTHR33781; 2.
DR PANTHER; PTHR33781:SF12; PTHR33781:SF12; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Phytochrome signaling pathway;
KW Reference proteome.
FT CHAIN 1..439
FT /note="Protein PHYTOCHROME KINASE SUBSTRATE 1"
FT /id="PRO_0000058450"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M9T4"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M9T4"
FT CONFLICT 196
FT /note="E -> D (in Ref. 1; AAD38033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48085 MW; 7A0A825FF7D3F3FC CRC64;
MVTLTPSSAS TPKTSFDFMK NNNSHSSLYV SSSSYLSSKE DALVTTKKLM EPSKTLNMSI
NPKQEEFGDE KKMVKKAPED PEIGVFGAEK YFNGDMDSDQ GSSVLSLTNP EVERTVVDSK
QSAKKSTGTP SVRSESSWNS QSVLLQNKLV NSCNSSFKEK KNSNGQIQKV TNNKKSFLAN
LGCKCACSDG DSVDVEEKTS VKRSADPNIS VITMRSSADM NTELIKIQKQ EELSQRKSLE
VFGSPVAIEK KSSVVQKKLP LPPWKSRTEE DDTKSEGSDS SSDLFEIEGL TGNPKPFLTR
QGSDPASPTC YAPSEVSVEW SIVTASAADF SVMSECATSP VRRNRPTQIP RIPITAKSAP
QRRKSSSSSG GNGFLMSCKS HKSVMVSGDL DRRSSMNKTQ PSYVPRFPME TTKPKSFETR
RRISNSSISH TQSSLLYSQ
