PKS2_ARATH
ID PKS2_ARATH Reviewed; 442 AA.
AC Q9M9T4; Q8L8R2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Protein PHYTOCHROME KINASE SUBSTRATE 2;
GN Name=PKS2; OrderedLocusNames=At1g14280; ORFNames=F14L17.4;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 INDUCTION, TISSUE SPECIFICITY, AND 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 FUNCTION, INTERACTION WITH PKS1, 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-245, AND
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH PKS1;
RP RPT3; PHOT1 AND PHOT2, 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: Acts predominantly in the phot1 pathway. Involved in the leaf
CC positioning and also in the phot2 pathway controlling the leaf
CC flattening. Component of the network that modulates the very low-
CC fluence response (VLFR) branch of phyA signaling. Regulates
CC phytochrome-mediated photomorphogenesis and hypocotyl phototropism. May
CC act by controlling auxin homeostasis. {ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:20071603}.
CC -!- SUBUNIT: Interacts with PKS1, RPT3, PHOT1 and PHOT2.
CC {ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:20071603}.
CC -!- INTERACTION:
CC Q9M9T4; Q17TI5: BRX; NbExp=3; IntAct=EBI-25512733, EBI-4426649;
CC Q9M9T4; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-25512733, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20071603};
CC Peripheral membrane protein {ECO:0000269|PubMed:20071603}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, with the strongest expression
CC on edges of the laminas. Not found in roots.
CC {ECO:0000269|PubMed:14615593, ECO:0000269|PubMed:20071603}.
CC -!- INDUCTION: Up-regulated by white light. {ECO:0000269|PubMed:14615593}.
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. No effect on negative root phototropism. Auxin accumulation
CC in protoplasts. {ECO:0000269|PubMed:14615593,
CC ECO:0000269|PubMed:16777956, ECO:0000269|PubMed:18024556,
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; AC012188; AAF43927.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29138.1; -; Genomic_DNA.
DR EMBL; AY088864; AAM67170.1; -; mRNA.
DR EMBL; AF334730; AAG50108.1; -; mRNA.
DR EMBL; AY054676; AAK96867.1; -; mRNA.
DR EMBL; AY081531; AAM10093.1; -; mRNA.
DR PIR; H86276; H86276.
DR RefSeq; NP_172880.1; NM_101294.3.
DR AlphaFoldDB; Q9M9T4; -.
DR BioGRID; 23229; 4.
DR IntAct; Q9M9T4; 2.
DR STRING; 3702.AT1G14280.1; -.
DR iPTMnet; Q9M9T4; -.
DR PaxDb; Q9M9T4; -.
DR PRIDE; Q9M9T4; -.
DR ProteomicsDB; 234767; -.
DR EnsemblPlants; AT1G14280.1; AT1G14280.1; AT1G14280.
DR GeneID; 837989; -.
DR Gramene; AT1G14280.1; AT1G14280.1; AT1G14280.
DR KEGG; ath:AT1G14280; -.
DR Araport; AT1G14280; -.
DR TAIR; locus:2012502; AT1G14280.
DR eggNOG; ENOG502QSBI; Eukaryota.
DR HOGENOM; CLU_048817_0_0_1; -.
DR InParanoid; Q9M9T4; -.
DR OMA; RCVCSNW; -.
DR OrthoDB; 841461at2759; -.
DR PhylomeDB; Q9M9T4; -.
DR PRO; PR:Q9M9T4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9T4; baseline and differential.
DR Genevisible; Q9M9T4; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009638; P:phototropism; IGI:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR InterPro; IPR039615; PKS.
DR InterPro; IPR039821; PSK1/PSK2.
DR PANTHER; PTHR33781; PTHR33781; 1.
DR PANTHER; PTHR33781:SF14; PTHR33781:SF14; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Phytochrome signaling pathway;
KW Reference proteome.
FT CHAIN 1..442
FT /note="Protein PHYTOCHROME KINASE SUBSTRATE 2"
FT /id="PRO_0000393341"
FT REGION 110..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 153
FT /note="K -> N (in Ref. 3; AAM67170)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="N -> K (in Ref. 3; AAM67170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49131 MW; 7BFAAF3A3EA37889 CRC64;
MVTLTSSSST PNVSFDFMMN NNNNSNNLYG PFSSSSTSFS YLTSKEDALT QKNLMSGITN
DVLGINKKAS EDLEISVFGA EKYFNGDMDS DHSPRLVSPL PDPEVPIERI FVGPKQSSKN
SSETPSLRSE SSWNSQSLLL QSKYVEKKKN IKKNSSCNSY FQEKDMSSNH KVSNKKSFLA
TLGCRCVCSN WSSVDVVDDK RRSSGLKKIK TQLSFSGDLS SEMKIHQQQQ EAMLEQRKSL
EIFGSPLIEK RIIQKKFPWE YSSSAKKEEH GFSVKYEEEE DGSVSDVSTD LFEIESLTGK
ANPFLARQGS SDPDSPDGYA PSEVSIQWSV VTASVADFSV MSECATSPVK KNRSFQIPRI
PIMAKSNREI APQRRKSSSS GLLMGCKSHK SVRVSGDSYT SMNRTPSYVP RFPVEANPTS
TETRRRISSS SVSHTQSPFL YT
