O48963 · PHOT1_ARATH
- ProteinPhototropin-1
- GenePHOT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids996 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein kinase that acts as a blue light (BL) photoreceptor in a signal-transduction pathway for photo-induced movements (PubMed:14739272, PubMed:15821287, PubMed:29101334, PubMed:31904040).
Triggers the phosphorylation of AHA1 and AHA2 C-terminal penultimate Thr in guard cells to activate them and induce stomatal opening in response to blue light (BL) (PubMed:15821287, PubMed:31904040).
Phosphorylates also BLUS1, a kinase involved in stomatal opening (PubMed:23811955).
Mediates the phosphorylation of CBC1 in stomata, but not of CBC2, in response to blue light (PubMed:29101334).
Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening
Triggers the phosphorylation of AHA1 and AHA2 C-terminal penultimate Thr in guard cells to activate them and induce stomatal opening in response to blue light (BL) (PubMed:15821287, PubMed:31904040).
Phosphorylates also BLUS1, a kinase involved in stomatal opening (PubMed:23811955).
Mediates the phosphorylation of CBC1 in stomata, but not of CBC2, in response to blue light (PubMed:29101334).
Required for blue light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to a low rate of blue light. Also mediates rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under a low rate but not under a high rate of blue light. Contributes to the chloroplast accumulation but seems not to be required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Confers sensitivity to drought. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening
Miscellaneous
Undergoes a photocycle characterized by fluorescence and absorption changes induced by blue light. Half-time of photoproduct formation is 14 seconds and 70 seconds for dark regeneration.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Note: Binds 2 FMN per subunit.
Activity regulation
Autophosphorylation is inhibited by staurosporine, but not by tyrphostin 9, sphingosine, GW5074 and BML-265.
Absorption
Exhibits a smaller absorbance peak at 350 nm. The broad fluorescence emission spectrum peaks at 490 nm.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 233 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 235 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 238 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 251 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 266 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 276 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 297 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 302 | FMN 1 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 511 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 513 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 516 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 529 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 544 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 554 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 556 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 575 | FMN 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 669-677 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGSGDTGSV | ||||||
Binding site | 692 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 788 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic side of plasma membrane | |
Cellular Component | plant-type vacuole | |
Molecular Function | ATP binding | |
Molecular Function | blue light photoreceptor activity | |
Molecular Function | FMN binding | |
Molecular Function | identical protein binding | |
Molecular Function | kinase activity | |
Molecular Function | mRNA binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | cellular response to blue light | |
Biological Process | chloroplast accumulation movement | |
Biological Process | chloroplast avoidance movement | |
Biological Process | circadian rhythm | |
Biological Process | negative regulation of anion channel activity by blue light | |
Biological Process | phototropism | |
Biological Process | protein autophosphorylation | |
Biological Process | regulation of proton transport | |
Biological Process | regulation of stomatal movement | |
Biological Process | response to blue light |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhototropin-1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionO48963
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Enhanced drought tolerance, when associated with PHOT2 disruption (PubMed:20031924).
Plants lacking both PHOT1 and PHOT2 have curled downward leaves missing color changes in response to weak or strong blue light (BL) (PubMed:14739272, PubMed:31904040).
Impaired proton H+ pumping associated with altered increased ATP hydrolysis and absence of binding between 14-3-3 protein and H+-ATPase (e.g. AHA1 and AHA2) in response to BL in guard cells of plants missing PHOT1 and PHOT2 (PubMed:15821287).
Plants lacking both PHOT1 and PHOT2 have curled downward leaves missing color changes in response to weak or strong blue light (BL) (PubMed:14739272, PubMed:31904040).
Impaired proton H+ pumping associated with altered increased ATP hydrolysis and absence of binding between 14-3-3 protein and H+-ATPase (e.g. AHA1 and AHA2) in response to BL in guard cells of plants missing PHOT1 and PHOT2 (PubMed:15821287).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 234 | No effect on the kinase activity regulation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 512 | Loss of light-sensing and light-dependent autophosphorylation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 774 | In nph1-1; loss of phototropism. | ||||
Sequence: Missing | ||||||
Mutagenesis | 806 | Lost kinase activity, unable to phosphorylate CBC1. | ||||
Sequence: D → N | ||||||
Mutagenesis | 936 | In nph1-2; partial phototropism. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 85 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000086522 | 1-996 | Phototropin-1 | |||
Sequence: MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRVSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAGNNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKALRPNGLPESLIRYDARQKDMATNSVTELVEAVKRPRALSESTNLHPFMTKSESDELPKKPARRMSENVVPSGRRNSGGGRRNSMQRINEIPEKKSRKSSLSFMGIKKKSESLDESIDDGFIEYGEEDDEISDRDERPESVDDKVRQKEMRKGIDLATTLERIEKNFVITDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDLTTVKKIRNAIDNQTEVTVQLINYTKSGKKFWNIFHLQPMRDQKGEVQYFIGVQLDGSKHVEPVRNVIEETAVKEGEDLVKKTAVNIDEAVRELPDANMTPEDLWANHSKVVHCKPHRKDSPPWIAIQKVLESGEPIGLKHFKPVKPLGSGDTGSVHLVELVGTDQLFAMKAMDKAVMLNRNKVHRARAEREILDLLDHPFLPALYASFQTKTHICLITDYYPGGELFMLLDRQPRKVLKEDAVRFYAAQVVVALEYLHCQGIIYRDLKPENVLIQGNGDISLSDFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPEIISGAGHTSAVDWWALGILMYEMLYGYTPFRGKTRQKTFTNVLQKDLKFPASIPASLQVKQLIFRLLQRDPKKRLGCFEGANEVKQHSFFKGINWALIRCTNPPELETPIFSGEAENGEKVVDPELEDLQTNVF | ||||||
Modified residue | 23 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 58 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 185 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 234 | S-4a-FMN cysteine | ||||
Sequence: C | ||||||
Disulfide bond | 261 | Interchain | ||||
Sequence: C | ||||||
Modified residue | 350 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 376 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 410 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 450 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 512 | S-4a-FMN cysteine | ||||
Sequence: C |
Post-translational modification
Autophosphorylated at Ser-185, Ser-350 and Ser-410 in response to blue light irradiation.
2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Present in guard cells (at protein level).
Gene expression databases
Interaction
Subunit
Homodimer; disulfide-linked (PubMed:18585389, PubMed:24316821).
Interacts with PKS1, PKS2, RPT2, RPT3, PHOT2 and BLUS1 (PubMed:10542152, PubMed:15031408, PubMed:16777956, PubMed:18585389, PubMed:20071603, PubMed:23811955).
Subunit of a complex made of CAR6, PHOT1 and RPT3/NPH3 (PubMed:21367967).
Associates with CBC1 and CBC2 (PubMed:31904040).
Binds to BHP (PubMed:28358053).
Interacts with PKS1, PKS2, RPT2, RPT3, PHOT2 and BLUS1 (PubMed:10542152, PubMed:15031408, PubMed:16777956, PubMed:18585389, PubMed:20071603, PubMed:23811955).
Subunit of a complex made of CAR6, PHOT1 and RPT3/NPH3 (PubMed:21367967).
Associates with CBC1 and CBC2 (PubMed:31904040).
Binds to BHP (PubMed:28358053).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O48963 | GRF6 P48349 | 6 | EBI-1553849, EBI-1633785 | |
BINARY | O48963 | PHOT1 O48963 | 5 | EBI-1553849, EBI-1553849 | |
BINARY | O48963 | PKS1 Q9SWI1 | 3 | EBI-1553849, EBI-626200 | |
BINARY | O48963 | RPT3 Q9FMF5 | 3 | EBI-1553849, EBI-1553842 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-37 | Polar residues | ||||
Sequence: MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPD | ||||||
Region | 1-184 | Disordered | ||||
Sequence: MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPDNPVFRPEPPAWQNLSDPRGTSPQPRPQQEPAPSNPVRSDQEIAVTTSWMALKDPSPETISKKTITAEKPQKSAVAAEQRAAEWGLVLKTDTKTGKPQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGEMSDGDVPGGRSGIPRV | ||||||
Compositional bias | 133-168 | Polar residues | ||||
Sequence: PQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGE | ||||||
Domain | 184-257 | PAS 1 | ||||
Sequence: VSEDLKDALSTFQQTFVVSDATKPDYPIMYASAGFFNMTGYTSKEVVGRNCRFLQGSGTDADELAKIRETLAAG | ||||||
Domain | 258-312 | PAC 1 | ||||
Sequence: NNYCGRILNYKKDGTSFWNLLTIAPIKDESGKVLKFIGMQVEVSKHTEGAKEKAL | ||||||
Region | 351-413 | Disordered | ||||
Sequence: ESTNLHPFMTKSESDELPKKPARRMSENVVPSGRRNSGGGRRNSMQRINEIPEKKSRKSSLSF | ||||||
Compositional bias | 380-394 | Polar residues | ||||
Sequence: VPSGRRNSGGGRRNS | ||||||
Region | 434-453 | Disordered | ||||
Sequence: YGEEDDEISDRDERPESVDD | ||||||
Domain | 462-535 | PAS 2 | ||||
Sequence: KGIDLATTLERIEKNFVITDPRLPDNPIIFASDSFLELTEYSREEILGRNCRFLQGPETDLTTVKKIRNAIDNQ | ||||||
Domain | 536-590 | PAC 2 | ||||
Sequence: TEVTVQLINYTKSGKKFWNIFHLQPMRDQKGEVQYFIGVQLDGSKHVEPVRNVIE | ||||||
Domain | 663-952 | Protein kinase | ||||
Sequence: FKPVKPLGSGDTGSVHLVELVGTDQLFAMKAMDKAVMLNRNKVHRARAEREILDLLDHPFLPALYASFQTKTHICLITDYYPGGELFMLLDRQPRKVLKEDAVRFYAAQVVVALEYLHCQGIIYRDLKPENVLIQGNGDISLSDFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPEIISGAGHTSAVDWWALGILMYEMLYGYTPFRGKTRQKTFTNVLQKDLKFPASIPASLQVKQLIFRLLQRDPKKRLGCFEGANEVKQHSFF | ||||||
Region | 806-862 | Activation loop | ||||
Sequence: DFDLSCLTSCKPQLLIPSIDEKKKKKQQKSQQTPIFMAEPMRASNSFVGTEEYIAPE |
Domain
The activation loop within the kinase domain is the target of phosphorylation (By similarity).
The PAS (PER-ARNT-SIM) domains are required for the binding of FMN chromophores (Probable)
The PAS (PER-ARNT-SIM) domains are required for the binding of FMN chromophores (Probable)
Sequence similarities
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length996
- Mass (Da)111,689
- Last updated1998-06-01 v1
- ChecksumC9B68812F1B3A04E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-37 | Polar residues | ||||
Sequence: MEPTEKPSTKPSSRTLPRDTRGSLEVFNPSTQLTRPD | ||||||
Compositional bias | 133-168 | Polar residues | ||||
Sequence: PQGVGVRNSGGTENDPNGKKTTSQRNSQNSCRSSGE | ||||||
Compositional bias | 380-394 | Polar residues | ||||
Sequence: VPSGRRNSGGGRRNS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF030864 EMBL· GenBank· DDBJ | AAC01753.1 EMBL· GenBank· DDBJ | mRNA | ||
AL157735 EMBL· GenBank· DDBJ | CAB75791.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE78072.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE78073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF360218 EMBL· GenBank· DDBJ | AAK25928.1 EMBL· GenBank· DDBJ | mRNA | ||
AY040062 EMBL· GenBank· DDBJ | AAK64120.1 EMBL· GenBank· DDBJ | mRNA |