PHOT1_ARATH
ID PHOT1_ARATH Reviewed; 996 AA.
AC O48963;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Phototropin-1;
DE EC=2.7.11.1;
DE AltName: Full=Non-phototropic hypocotyl protein 1;
DE AltName: Full=Root phototropism protein 1;
GN Name=PHOT1; Synonyms=JK224, NPH1, RPT1; OrderedLocusNames=At3g45780;
GN ORFNames=T6D9_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 {ECO:0000312|EMBL:CAB75791.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF VAL-774 AND ARG-936.
RC STRAIN=cv. Columbia; TISSUE=Hypocotyl;
RX PubMed=9405347; DOI=10.1126/science.278.5346.2120;
RA Huala E., Oeller P.W., Liscum E., Han I.-S., Larsen E., Briggs W.R.;
RT "Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain.";
RL Science 278:2120-2123(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3] {ECO:0000312|EMBL:CAB75791.1}
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 PHOSPHORYLATION.
RX PubMed=11537679; DOI=10.1073/pnas.89.10.4718;
RA Reymond P., Short T.W., Briggs W.R., Poff K.L.;
RT "Light-induced phosphorylation of a membrane protein plays an early role in
RT signal transduction for phototropism in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4718-4721(1992).
RN [6] {ECO:0000305}
RP PHOSPHORYLATION.
RX PubMed=9831559; DOI=10.1126/science.282.5394.1698;
RA Christie J.M., Reymond P., Powell G.K., Bernasconi P., Raibekas A.A.,
RA Liscum E., Briggs W.R.;
RT "Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor
RT for phototropism.";
RL Science 282:1698-1701(1998).
RN [7] {ECO:0000305}
RP FMN-BINDING.
RX PubMed=10411952; DOI=10.1073/pnas.96.15.8779;
RA Christie J.M., Salomon M., Nozue K., Wada M., Briggs W.R.;
RT "LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor
RT phototropin (nph1): binding sites for the chromophore flavin
RT mononucleotide.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8779-8783(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RPT3.
RX PubMed=10542152; DOI=10.1126/science.286.5441.961;
RA Motchoulski A., Liscum E.;
RT "Arabidopsis NPH3: a NPH1 photoreceptor-interacting protein essential for
RT phototropism.";
RL Science 286:961-964(1999).
RN [9]
RP FUNCTION.
RX PubMed=10662859; DOI=10.2307/3870924;
RA Sakai T., Wada T., Ishiguro S., Okada K.;
RT "RPT2: a signal transducer of the phototropic response in Arabidopsis.";
RL Plant Cell 12:225-236(2000).
RN [10]
RP FUNCTION.
RX PubMed=11439133; DOI=10.1046/j.1365-313x.2001.01038.x;
RA Folta K.M., Spalding E.P.;
RT "Unexpected roles for cryptochrome 2 and phototropin revealed by high-
RT resolution analysis of blue light-mediated hypocotyl growth inhibition.";
RL Plant J. 26:471-478(2001).
RN [11]
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF CYS-234 AND CYS-512.
RX PubMed=12383086; DOI=10.1046/j.1365-313x.2002.01415.x;
RA Christie J.M., Swartz T.E., Bogomolni R.A., Briggs W.R.;
RT "Phototropin LOV domains exhibit distinct roles in regulating photoreceptor
RT function.";
RL Plant J. 32:205-219(2002).
RN [12]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-512.
RX PubMed=12068117; DOI=10.1104/pp.002410;
RA Kasahara M., Swartz T.E., Olney M.A., Onodera A., Mochizuki N.,
RA Fukuzawa H., Asamizu E., Tabata S., Kanegae H., Takano M., Christie J.M.,
RA Nagatani A., Briggs W.R.;
RT "Photochemical properties of the flavin mononucleotide-binding domains of
RT the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii.";
RL Plant Physiol. 129:762-773(2002).
RN [13]
RP FUNCTION.
RX PubMed=12650626; DOI=10.1023/a:1022393406204;
RA Folta K.M., Kaufman L.S.;
RT "Phototropin 1 is required for high-fluence blue-light-mediated mRNA
RT destabilization.";
RL Plant Mol. Biol. 51:609-618(2003).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12821778; DOI=10.1073/pnas.1336802100;
RA Harada A., Sakai T., Okada K.;
RT "Phot1 and phot2 mediate blue light-induced transient increases in
RT cytosolic Ca2+ differently in Arabidopsis leaves.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8583-8588(2003).
RN [15]
RP GENE FAMILY, AND REVIEW.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RPT2.
RX PubMed=15031408; DOI=10.1105/tpc.019901;
RA Inada S., Ohgishi M., Mayama T., Okada K., Sakai T.;
RT "RPT2 is a signal transducer involved in phototropic response and stomatal
RT opening by association with phototropin 1 in Arabidopsis thaliana.";
RL Plant Cell 16:887-896(2004).
RN [17]
RP FUNCTION.
RX PubMed=14982991; DOI=10.1073/pnas.0305984101;
RA Ohgishi M., Saji K., Okada K., Sakai T.;
RT "Functional analysis of each blue light receptor, cry1, cry2, phot1, and
RT phot2, by using combinatorial multiple mutants in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2223-2228(2004).
RN [18]
RP FUNCTION, INTERACTION WITH PKS1, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
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 [19]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-58; SER-185; SER-350
RP AND SER-410, FMN BINDING, AUTOPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=20031924; DOI=10.1093/mp/ssm017;
RA Sullivan S., Thomson C.E., Lamont D.J., Jones M.A., Christie J.M.;
RT "In vivo phosphorylation site mapping and functional characterization of
RT Arabidopsis phototropin 1.";
RL Mol. Plant 1:178-194(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350; SER-376 AND SER-450, 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 [21]
RP INTERACTION WITH PKS1; PKS2; RPT3 AND PHOT2.
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).
RN [22]
RP INTERACTION WITH RPT3/NPH3 AND CAR6.
RX PubMed=21367967; DOI=10.1104/pp.110.167411;
RA Knauer T., Duemmer M., Landgraf F., Forreiter C.;
RT "A negative effector of blue light-induced and gravitropic bending in
RT Arabidopsis.";
RL Plant Physiol. 156:439-447(2011).
RN [23]
RP FUNCTION, AND INTERACTION WITH BLUS1.
RX PubMed=23811955; DOI=10.1038/ncomms3094;
RA Takemiya A., Sugiyama N., Fujimoto H., Tsutsumi T., Yamauchi S., Hiyama A.,
RA Tada Y., Christie J.M., Shimazaki K.;
RT "Phosphorylation of BLUS1 kinase by phototropins is a primary step in
RT stomatal opening.";
RL Nat. Commun. 4:2094-2094(2013).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 180-308 IN COMPLEX WITH FMN, AND
RP SUBUNIT.
RX PubMed=18585389; DOI=10.1016/j.jmb.2008.06.033;
RA Nakasako M., Zikihara K., Matsuoka D., Katsura H., Tokutomi S.;
RT "Structural basis of the LOV1 dimerization of Arabidopsis phototropins 1
RT and 2.";
RL J. Mol. Biol. 381:718-733(2008).
CC -!- FUNCTION: Protein kinase that acts as a blue light photoreceptor in a
CC signal-transduction pathway for photo-induced movements. Phosphorylates
CC BLUS1, a kinase involved in stomatal opening. Required for blue light
CC mediated mRNA destabilization. Mediates calcium spiking of
CC extracellular origin in response to a low rate of blue light. Also
CC mediates rapid membrane depolarization and growth inhibition in
CC response to blue light. Necessary for root phototropism. Involved in
CC hypocotyl phototropism under a low rate but not under a high rate of
CC blue light. Contributes to the chloroplast accumulation but seems not
CC to be required for chloroplast translocation. Regulates stomata opening
CC and photomorphogenesis response of leaf tissue. Confers sensitivity to
CC drought. Not involved in hypocotyl elongation inhibition, anthocyanin
CC accumulation or cotyledon opening. {ECO:0000269|PubMed:10662859,
CC ECO:0000269|PubMed:11439133, ECO:0000269|PubMed:12650626,
CC ECO:0000269|PubMed:12821778, ECO:0000269|PubMed:14982991,
CC ECO:0000269|PubMed:15031408, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:20031924, ECO:0000269|PubMed:23811955}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 2 FMN per subunit. {ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=450 nm {ECO:0000269|PubMed:12068117};
CC Note=Exhibits a smaller absorbance peak at 350 nm. The broad
CC fluorescence emission spectrum peaks at 490 nm.;
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with PKS1, PKS2, RPT2,
CC RPT3, PHOT2 and BLUS1 (PubMed:10542152, PubMed:15031408,
CC PubMed:16777956, PubMed:18585389, PubMed:20071603, PubMed:23811955).
CC Subunit of a complex made of CAR6, PHOT1 and RPT3/NPH3
CC (PubMed:21367967). {ECO:0000269|PubMed:10542152,
CC ECO:0000269|PubMed:15031408, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:18585389, ECO:0000269|PubMed:20071603,
CC ECO:0000269|PubMed:21367967, ECO:0000269|PubMed:23811955}.
CC -!- INTERACTION:
CC O48963; P48349: GRF6; NbExp=6; IntAct=EBI-1553849, EBI-1633785;
CC O48963; O48963: PHOT1; NbExp=5; IntAct=EBI-1553849, EBI-1553849;
CC O48963; Q9SWI1: PKS1; NbExp=3; IntAct=EBI-1553849, EBI-626200;
CC O48963; Q9FMF5: RPT3; NbExp=3; IntAct=EBI-1553849, EBI-1553842;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Cytoplasm.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation (By similarity). The PAS (PER-ARNT-SIM) domains are
CC required for the binding of FMN chromophores. {ECO:0000250}.
CC -!- PTM: Autophosphorylated in response to blue light irradiation.
CC {ECO:0000269|PubMed:11537679, ECO:0000269|PubMed:16777956,
CC ECO:0000269|PubMed:20031924, ECO:0000269|PubMed:9831559, ECO:0000305}.
CC -!- PTM: 2 molecules of FMN bind covalently to cysteines after exposure to
CC blue light and are reversed in the dark.
CC -!- DISRUPTION PHENOTYPE: Enhanced drought tolerance, when associated with
CC PHOT2 disruption. {ECO:0000269|PubMed:20031924}.
CC -!- MISCELLANEOUS: Undergoes a photocycle characterized by fluorescence and
CC absorption changes induced by blue light. Half-time of photoproduct
CC formation is 14 seconds and 70 seconds for dark regeneration.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF030864; AAC01753.1; -; mRNA.
DR EMBL; AL157735; CAB75791.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78072.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78073.1; -; Genomic_DNA.
DR EMBL; AF360218; AAK25928.1; -; mRNA.
DR EMBL; AY040062; AAK64120.1; -; mRNA.
DR PIR; T47518; T47518.
DR RefSeq; NP_001030814.1; NM_001035737.2.
DR RefSeq; NP_190164.1; NM_114447.4.
DR PDB; 2Z6C; X-ray; 2.10 A; A/B=180-308.
DR PDB; 4HHD; X-ray; 2.75 A; A/B=452-615.
DR PDBsum; 2Z6C; -.
DR PDBsum; 4HHD; -.
DR AlphaFoldDB; O48963; -.
DR SMR; O48963; -.
DR BioGRID; 9041; 12.
DR DIP; DIP-38655N; -.
DR IntAct; O48963; 15.
DR MINT; O48963; -.
DR STRING; 3702.AT3G45780.2; -.
DR iPTMnet; O48963; -.
DR PaxDb; O48963; -.
DR PRIDE; O48963; -.
DR ProteomicsDB; 236731; -.
DR EnsemblPlants; AT3G45780.1; AT3G45780.1; AT3G45780.
DR EnsemblPlants; AT3G45780.2; AT3G45780.2; AT3G45780.
DR GeneID; 823721; -.
DR Gramene; AT3G45780.1; AT3G45780.1; AT3G45780.
DR Gramene; AT3G45780.2; AT3G45780.2; AT3G45780.
DR KEGG; ath:AT3G45780; -.
DR Araport; AT3G45780; -.
DR TAIR; locus:2102674; AT3G45780.
DR eggNOG; ENOG502QPPH; Eukaryota.
DR HOGENOM; CLU_006321_1_1_1; -.
DR InParanoid; O48963; -.
DR OMA; VQPKPHR; -.
DR OrthoDB; 529293at2759; -.
DR PhylomeDB; O48963; -.
DR BRENDA; 2.7.11.1; 399.
DR EvolutionaryTrace; O48963; -.
DR PRO; PR:O48963; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O48963; baseline and differential.
DR Genevisible; O48963; AT.
DR GO; GO:0009986; C:cell surface; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009882; F:blue light photoreceptor activity; IDA:TAIR.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0003729; F:mRNA binding; HDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0009904; P:chloroplast accumulation movement; IMP:TAIR.
DR GO; GO:0009903; P:chloroplast avoidance movement; IMP:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IMP:TAIR.
DR GO; GO:0010362; P:negative regulation of anion channel activity by blue light; IMP:TAIR.
DR GO; GO:0009638; P:phototropism; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0010155; P:regulation of proton transport; IGI:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009637; P:response to blue light; IGI:TAIR.
DR CDD; cd00130; PAS; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Chromophore; Cytoplasm;
KW Disulfide bond; Flavoprotein; FMN; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome;
KW Repeat; Sensory transduction; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..996
FT /note="Phototropin-1"
FT /id="PRO_0000086522"
FT DOMAIN 184..257
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 258..312
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 462..535
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 536..590
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 663..952
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..862
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 788
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 233..238
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 251
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 266
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 276
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 297
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 511..516
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 575
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 669..677
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT BINDING 692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000305"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P93025"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20031924"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20031924"
FT MOD_RES 234
FT /note="S-4a-FMN cysteine"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20031924,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20031924"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 512
FT /note="S-4a-FMN cysteine"
FT DISULFID 261
FT /note="Interchain"
FT MUTAGEN 234
FT /note="C->A: No effect on the kinase activity regulation."
FT /evidence="ECO:0000269|PubMed:12383086"
FT MUTAGEN 512
FT /note="C->A: Loss of light-sensing and light-dependent
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:12068117,
FT ECO:0000269|PubMed:12383086"
FT MUTAGEN 774
FT /note="Missing: In nph1-1; loss of phototropism."
FT /evidence="ECO:0000269|PubMed:9405347"
FT MUTAGEN 936
FT /note="R->K: In nph1-2; partial phototropism."
FT /evidence="ECO:0000269|PubMed:9405347"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:2Z6C"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:2Z6C"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:2Z6C"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:2Z6C"
FT TURN 226..231
FT /evidence="ECO:0007829|PDB:2Z6C"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:2Z6C"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:2Z6C"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:2Z6C"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:2Z6C"
FT STRAND 290..300
FT /evidence="ECO:0007829|PDB:2Z6C"
FT HELIX 453..471
FT /evidence="ECO:0007829|PDB:4HHD"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:4HHD"
FT STRAND 489..492
FT /evidence="ECO:0007829|PDB:4HHD"
FT HELIX 494..500
FT /evidence="ECO:0007829|PDB:4HHD"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:4HHD"
FT HELIX 512..515
FT /evidence="ECO:0007829|PDB:4HHD"
FT HELIX 522..533
FT /evidence="ECO:0007829|PDB:4HHD"
FT STRAND 538..545
FT /evidence="ECO:0007829|PDB:4HHD"
FT STRAND 551..562
FT /evidence="ECO:0007829|PDB:4HHD"
FT STRAND 568..575
FT /evidence="ECO:0007829|PDB:4HHD"
FT HELIX 588..592
FT /evidence="ECO:0007829|PDB:4HHD"
FT HELIX 595..613
FT /evidence="ECO:0007829|PDB:4HHD"
SQ SEQUENCE 996 AA; 111689 MW; C9B68812F1B3A04E CRC64;
MEPTEKPSTK PSSRTLPRDT RGSLEVFNPS TQLTRPDNPV FRPEPPAWQN LSDPRGTSPQ
PRPQQEPAPS NPVRSDQEIA VTTSWMALKD PSPETISKKT ITAEKPQKSA VAAEQRAAEW
GLVLKTDTKT GKPQGVGVRN SGGTENDPNG KKTTSQRNSQ NSCRSSGEMS DGDVPGGRSG
IPRVSEDLKD ALSTFQQTFV VSDATKPDYP IMYASAGFFN MTGYTSKEVV GRNCRFLQGS
GTDADELAKI RETLAAGNNY CGRILNYKKD GTSFWNLLTI APIKDESGKV LKFIGMQVEV
SKHTEGAKEK ALRPNGLPES LIRYDARQKD MATNSVTELV EAVKRPRALS ESTNLHPFMT
KSESDELPKK PARRMSENVV PSGRRNSGGG RRNSMQRINE IPEKKSRKSS LSFMGIKKKS
ESLDESIDDG FIEYGEEDDE ISDRDERPES VDDKVRQKEM RKGIDLATTL ERIEKNFVIT
DPRLPDNPII FASDSFLELT EYSREEILGR NCRFLQGPET DLTTVKKIRN AIDNQTEVTV
QLINYTKSGK KFWNIFHLQP MRDQKGEVQY FIGVQLDGSK HVEPVRNVIE ETAVKEGEDL
VKKTAVNIDE AVRELPDANM TPEDLWANHS KVVHCKPHRK DSPPWIAIQK VLESGEPIGL
KHFKPVKPLG SGDTGSVHLV ELVGTDQLFA MKAMDKAVML NRNKVHRARA EREILDLLDH
PFLPALYASF QTKTHICLIT DYYPGGELFM LLDRQPRKVL KEDAVRFYAA QVVVALEYLH
CQGIIYRDLK PENVLIQGNG DISLSDFDLS CLTSCKPQLL IPSIDEKKKK KQQKSQQTPI
FMAEPMRASN SFVGTEEYIA PEIISGAGHT SAVDWWALGI LMYEMLYGYT PFRGKTRQKT
FTNVLQKDLK FPASIPASLQ VKQLIFRLLQ RDPKKRLGCF EGANEVKQHS FFKGINWALI
RCTNPPELET PIFSGEAENG EKVVDPELED LQTNVF
