PHOT2_ARATH
ID PHOT2_ARATH Reviewed; 915 AA.
AC P93025; O81204; Q8RWE6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Phototropin-2;
DE EC=2.7.11.1;
DE AltName: Full=Defective in chloroplast avoidance protein 1;
DE AltName: Full=Non-phototropic hypocotyl 1-like protein 1;
DE Short=AtKin7;
DE Short=NPH1-like protein 1;
GN Name=PHOT2; Synonyms=CAV1, KIN7, NPL1; OrderedLocusNames=At5g58140;
GN ORFNames=K21L19.6;
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] (ISOFORM 1).
RA Jarillo J.A., Ahmad M., Cashmore A.R.;
RT "NPH2: a second member of the NPH serine/threonine kinase family of
RT Arabidopsis.";
RL (er) Plant Gene Register PGR98-100(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 560-915 (ISOFORM 1).
RA Winge P., Thangstad O.P.;
RT "Arabidopsis thaliana putative serine/threonine protein kinase.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, FMN-BINDING, AND PHOSPHORYLATION.
RX PubMed=11371609; DOI=10.1073/pnas.101137598;
RA Sakai T., Kagawa T., Kasahara M., Swartz T.E., Christie J.M., Briggs W.R.,
RA Wada M., Okada K.;
RT "Arabidopsis nph1 and npl1: blue light receptors that mediate both
RT phototropism and chloroplast relocation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6969-6974(2001).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF THR-727.
RX PubMed=11251116; DOI=10.1126/science.291.5511.2138;
RA Kagawa T., Sakai T., Suetsugu N., Oikawa K., Ishiguro S., Kato T.,
RA Tabata S., Okada K., Wada M.;
RT "Arabidopsis NPL1: a phototropin homolog controlling the chloroplast high-
RT light avoidance response.";
RL Science 291:2138-2141(2001).
RN [8]
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF CYS-170 AND CYS-426.
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 [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 [10]
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 [11]
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 [12]
RP FUNCTION.
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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-22 AND SER-364, 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 [15]
RP INTERACTION WITH PKS1; PKS2; RPT3 AND PHOT1.
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 [16]
RP FUNCTION.
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 [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-246 IN COMPLEX WITH FMN,
RP SUBUNIT, AND MUTAGENESIS OF THR-217 AND MET-232.
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. Mediates calcium spiking
CC of extra- and intracellular origins in response to blue light. Involved
CC in hypocotyl phototropism. Contributes to the chloroplast accumulation
CC in low blue light and mediates their translocation (avoidance response)
CC at high fluence. Regulates stomata opening and photomorphogenesis
CC response of leaf tissue. Not involved in hypocotyl elongation
CC inhibition, anthocyanin accumulation or cotyledon opening.
CC {ECO:0000269|PubMed:11251116, ECO:0000269|PubMed:11371609,
CC ECO:0000269|PubMed:12821778, ECO:0000269|PubMed:14982991,
CC ECO:0000269|PubMed:15031408, 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. Interacts with PKS1, PKS2, RPT3 and PHOT1.
CC {ECO:0000269|PubMed:18585389, ECO:0000269|PubMed:20071603}.
CC -!- INTERACTION:
CC P93025; P43254: COP1; NbExp=2; IntAct=EBI-2270423, EBI-301649;
CC P93025; P93025: PHOT2; NbExp=2; IntAct=EBI-2270423, EBI-2270423;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12821778};
CC Peripheral membrane protein {ECO:0000269|PubMed:12821778}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P93025-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93025-2; Sequence=VSP_016306, VSP_016307;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers, and to a
CC lower extent in roots. {ECO:0000269|PubMed:11251116}.
CC -!- INDUCTION: Light fluence rate-dependent induction, independent of light
CC quality. {ECO:0000269|PubMed:11251116}.
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:11371609}.
CC -!- PTM: 2 molecules of FMN bind covalently to cysteines after exposure to
CC blue light and are reversed in the dark. {ECO:0000250}.
CC -!- MISCELLANEOUS: Undergoes a photocycle characterized by fluorescence and
CC absorption changes induced by blue light. Half-time of photoproduct
CC formation is 11 seconds and 15 seconds for dark regeneration.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF053941; AAC27293.2; -; mRNA.
DR EMBL; AB019228; BAB09904.1; -; Genomic_DNA.
DR EMBL; AB024029; BAB09904.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97002.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97004.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68619.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68620.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68621.1; -; Genomic_DNA.
DR EMBL; AY093141; AAM13140.1; -; mRNA.
DR EMBL; BT008901; AAP68340.1; -; mRNA.
DR EMBL; U79744; AAB39188.1; -; mRNA.
DR PIR; T51600; T51600.
DR RefSeq; NP_001318824.1; NM_001345288.1. [P93025-1]
DR RefSeq; NP_001330355.1; NM_001345289.1. [P93025-1]
DR RefSeq; NP_001330356.1; NM_001345290.1. [P93025-1]
DR RefSeq; NP_851210.1; NM_180879.2. [P93025-1]
DR RefSeq; NP_851211.1; NM_180880.2. [P93025-1]
DR PDB; 2Z6D; X-ray; 2.00 A; A/B=117-246.
DR PDB; 4EEP; X-ray; 1.70 A; A=385-496.
DR PDB; 4EER; X-ray; 1.75 A; A=385-496.
DR PDB; 4EES; X-ray; 1.80 A; A=385-496.
DR PDB; 4EET; X-ray; 1.20 A; B/D=385-496.
DR PDB; 4EEU; X-ray; 1.41 A; A=385-496.
DR PDB; 4NXB; X-ray; 2.56 A; A/B=388-496.
DR PDB; 4NXE; X-ray; 2.10 A; A/B=388-496.
DR PDB; 4NXF; X-ray; 1.77 A; A/B=388-496.
DR PDB; 4NXG; X-ray; 2.09 A; A/B=388-496.
DR PDB; 6GPU; X-ray; 1.17 A; A=387-492.
DR PDB; 6GPV; X-ray; 2.00 A; A=387-492.
DR PDB; 6QQH; X-ray; 1.38 A; A=387-507.
DR PDB; 6QQI; X-ray; 1.70 A; A=387-507.
DR PDB; 6QQJ; X-ray; 2.08 A; A=387-507.
DR PDB; 6QQK; X-ray; 2.40 A; A=387-507.
DR PDB; 6QSA; X-ray; 1.70 A; A=387-507.
DR PDB; 6S45; X-ray; 2.20 A; A=387-492.
DR PDB; 6S46; X-ray; 2.75 A; A=387-492.
DR PDB; 7ABY; X-ray; 1.45 A; A=387-496.
DR PDBsum; 2Z6D; -.
DR PDBsum; 4EEP; -.
DR PDBsum; 4EER; -.
DR PDBsum; 4EES; -.
DR PDBsum; 4EET; -.
DR PDBsum; 4EEU; -.
DR PDBsum; 4NXB; -.
DR PDBsum; 4NXE; -.
DR PDBsum; 4NXF; -.
DR PDBsum; 4NXG; -.
DR PDBsum; 6GPU; -.
DR PDBsum; 6GPV; -.
DR PDBsum; 6QQH; -.
DR PDBsum; 6QQI; -.
DR PDBsum; 6QQJ; -.
DR PDBsum; 6QQK; -.
DR PDBsum; 6QSA; -.
DR PDBsum; 6S45; -.
DR PDBsum; 6S46; -.
DR PDBsum; 7ABY; -.
DR AlphaFoldDB; P93025; -.
DR SMR; P93025; -.
DR BioGRID; 21170; 11.
DR DIP; DIP-53468N; -.
DR IntAct; P93025; 4.
DR MINT; P93025; -.
DR STRING; 3702.AT5G58140.2; -.
DR iPTMnet; P93025; -.
DR PaxDb; P93025; -.
DR PRIDE; P93025; -.
DR ProteomicsDB; 235062; -. [P93025-1]
DR EnsemblPlants; AT5G58140.1; AT5G58140.1; AT5G58140. [P93025-1]
DR EnsemblPlants; AT5G58140.2; AT5G58140.2; AT5G58140. [P93025-1]
DR EnsemblPlants; AT5G58140.5; AT5G58140.5; AT5G58140. [P93025-1]
DR EnsemblPlants; AT5G58140.6; AT5G58140.6; AT5G58140. [P93025-1]
DR EnsemblPlants; AT5G58140.7; AT5G58140.7; AT5G58140. [P93025-1]
DR GeneID; 835926; -.
DR Gramene; AT5G58140.1; AT5G58140.1; AT5G58140. [P93025-1]
DR Gramene; AT5G58140.2; AT5G58140.2; AT5G58140. [P93025-1]
DR Gramene; AT5G58140.5; AT5G58140.5; AT5G58140. [P93025-1]
DR Gramene; AT5G58140.6; AT5G58140.6; AT5G58140. [P93025-1]
DR Gramene; AT5G58140.7; AT5G58140.7; AT5G58140. [P93025-1]
DR KEGG; ath:AT5G58140; -.
DR Araport; AT5G58140; -.
DR TAIR; locus:2155821; AT5G58140.
DR eggNOG; ENOG502QPPH; Eukaryota.
DR HOGENOM; CLU_006321_0_1_1; -.
DR InParanoid; P93025; -.
DR PhylomeDB; P93025; -.
DR EvolutionaryTrace; P93025; -.
DR PRO; PR:P93025; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P93025; baseline and differential.
DR Genevisible; P93025; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016020; C:membrane; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009882; F:blue light photoreceptor activity; IMP: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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0009902; P:chloroplast relocation; TAS: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; TAS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009637; P:response to blue light; IGI:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP: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; Alternative splicing; ATP-binding; Cell membrane;
KW Chromophore; 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..915
FT /note="Phototropin-2"
FT /id="PRO_0000086523"
FT DOMAIN 120..193
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 194..248
FT /note="PAC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 376..449
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 450..504
FT /note="PAC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 577..864
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..774
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 22..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 702
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 169..174
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 187
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 202
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 212
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:18585389"
FT BINDING 425..430
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 583..591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48963"
FT MOD_RES 170
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 426
FT /note="S-4a-FMN cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 535..549
FT /note="RPEDLWAAHSKPVYP -> VRCTSSLLLNKDGKV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_016306"
FT VAR_SEQ 550..915
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_016307"
FT MUTAGEN 170
FT /note="C->A: No effect on light-dependent
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:12383086"
FT MUTAGEN 217
FT /note="T->Q: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:18585389"
FT MUTAGEN 232
FT /note="M->V: Loss of dimerization."
FT /evidence="ECO:0000269|PubMed:18585389"
FT MUTAGEN 426
FT /note="C->A: Severe loss of light-sensing and light-
FT dependent autophosphorylation."
FT /evidence="ECO:0000269|PubMed:12383086"
FT MUTAGEN 727
FT /note="T->I: In cav1-2; loss of chloroplast avoidance
FT response in response to high fluence blue light."
FT /evidence="ECO:0000269|PubMed:11251116"
FT CONFLICT 722
FT /note="D -> Y (in Ref. 5; AAB39188)"
FT /evidence="ECO:0000305"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:2Z6D"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2Z6D"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2Z6D"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:2Z6D"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2Z6D"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2Z6D"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:2Z6D"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:2Z6D"
FT STRAND 209..220
FT /evidence="ECO:0007829|PDB:2Z6D"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:2Z6D"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:6GPU"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:6GPU"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:6GPU"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6GPU"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:6GPU"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:6GPU"
FT HELIX 436..448
FT /evidence="ECO:0007829|PDB:6GPU"
FT STRAND 452..459
FT /evidence="ECO:0007829|PDB:6GPU"
FT STRAND 465..476
FT /evidence="ECO:0007829|PDB:6GPU"
FT STRAND 482..492
FT /evidence="ECO:0007829|PDB:6GPU"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:6QQH"
SQ SEQUENCE 915 AA; 102472 MW; CA163E2596289737 CRC64;
MERPRAPPSP LNDAESLSER RSLEIFNPSS GKETHGSTSS SSKPPLDGNN KGSSSKWMEF
QDSAKITERT AEWGLSAVKP DSGDDGISFK LSSEVERSKN MSRRSSEEST SSESGAFPRV
SQELKTALST LQQTFVVSDA TQPHCPIVYA SSGFFTMTGY SSKEIVGRNC RFLQGPDTDK
NEVAKIRDCV KNGKSYCGRL LNYKKDGTPF WNLLTVTPIK DDQGNTIKFI GMQVEVSKYT
EGVNDKALRP NGLSKSLIRY DARQKEKALD SITEVVQTIR HRKSQVQESV SNDTMVKPDS
STTPTPGRQT RQSDEASKSF RTPGRVSTPT GSKLKSSNNR HEDLLRMEPE ELMLSTEVIG
QRDSWDLSDR ERDIRQGIDL ATTLERIEKN FVISDPRLPD NPIIFASDSF LELTEYSREE
ILGRNCRFLQ GPETDQATVQ KIRDAIRDQR EITVQLINYT KSGKKFWNLF HLQPMRDQKG
ELQYFIGVQL DGSDHVEPLQ NRLSERTEMQ SSKLVKATAT NVDEAVRELP DANTRPEDLW
AAHSKPVYPL PHNKESTSWK AIKKIQASGE TVGLHHFKPI KPLGSGDTGS VHLVELKGTG
ELYAMKAMEK TMMLNRNKAH RACIEREIIS LLDHPFLPTL YASFQTSTHV CLITDFCPGG
ELFALLDRQP MKILTEDSAR FYAAEVVIGL EYLHCLGIVY RDLKPENILL KKDGHIVLAD
FDLSFMTTCT PQLIIPAAPS KRRRSKSQPL PTFVAEPSTQ SNSFVGTEEY IAPEIITGAG
HTSAIDWWAL GILLYEMLYG RTPFRGKNRQ KTFANILHKD LTFPSSIPVS LVGRQLINTL
LNRDPSSRLG SKGGANEIKQ HAFFRGINWP LIRGMSPPPL DAPLSIIEKD PNAKDIKWED
DGVLVNSTDL DIDLF
