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Protein

Phototropin-1

Gene

PHOT1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein kinase that acts as a blue light photoreceptor in a signal-transduction pathway for photo-induced movements. Phosphorylates BLUS1, a kinase involved in stomatal opening. 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.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

FMNCuratedNote: Binds 2 FMN per subunit.Curated

Absorptioni

Abs(max)=450 nm1 Publication

Exhibits a smaller absorbance peak at 350 nm. The broad fluorescence emission spectrum peaks at 490 nm.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei251 – 2511FMN1 Publication
Binding sitei266 – 2661FMN1 Publication
Binding sitei276 – 2761FMN1 Publication
Binding sitei297 – 2971FMN1 Publication
Binding sitei529 – 5291FMNBy similarity
Binding sitei544 – 5441FMNBy similarity
Binding sitei554 – 5541FMNBy similarity
Binding sitei575 – 5751FMNBy similarity
Binding sitei692 – 6921ATPPROSITE-ProRule annotationCurated
Active sitei788 – 7881Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi233 – 2386FMN1 Publication
Nucleotide bindingi511 – 5166FMNBy similarity
Nucleotide bindingi669 – 6779ATPPROSITE-ProRule annotationCurated

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • blue light photoreceptor activity Source: TAIR
  • FMN binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • kinase activity Source: TAIR
  • phosphorelay sensor kinase activity Source: InterPro
  • protein kinase activity Source: TAIR
  • protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • chloroplast accumulation movement Source: TAIR
  • chloroplast avoidance movement Source: TAIR
  • circadian rhythm Source: TAIR
  • intracellular signal transduction Source: GO_Central
  • negative regulation of anion channel activity by blue light Source: TAIR
  • phototropism Source: TAIR
  • protein autophosphorylation Source: TAIR
  • protein-chromophore linkage Source: UniProtKB-KW
  • regulation of proton transport Source: TAIR
  • regulation of stomatal movement Source: TAIR
  • response to blue light Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Photoreceptor protein, Receptor, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Sensory transduction

Keywords - Ligandi

ATP-binding, Chromophore, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT3G45780-MONOMER.
ARA:GQT-2469-MONOMER.
BRENDAi2.7.11.1. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Phototropin-1 (EC:2.7.11.1)
Alternative name(s):
Non-phototropic hypocotyl protein 1
Root phototropism protein 1
Gene namesi
Name:PHOT1
Synonyms:JK224, NPH1, RPT1
Ordered Locus Names:At3g45780
ORF Names:T6D9_110
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G45780.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: TAIR
  • cytoplasm Source: TAIR
  • cytoplasmic side of plasma membrane Source: TAIR
  • nucleus Source: GO_Central
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Enhanced drought tolerance, when associated with PHOT2 disruption.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi234 – 2341C → A: No effect on the kinase activity regulation. 1 Publication
Mutagenesisi512 – 5121C → A: Loss of light-sensing and light-dependent autophosphorylation. 2 Publications
Mutagenesisi774 – 7741Missing in nph1-1; loss of phototropism. 1 Publication
Mutagenesisi936 – 9361R → K in nph1-2; partial phototropism. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 996996Phototropin-1PRO_0000086522Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei58 – 581Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine1 Publication
Modified residuei234 – 2341S-4a-FMN cysteine
Disulfide bondi261 – 261Interchain
Modified residuei350 – 3501PhosphoserineCombined sources1 Publication
Modified residuei376 – 3761PhosphoserineCombined sources
Modified residuei410 – 4101Phosphoserine1 Publication
Modified residuei450 – 4501PhosphoserineCombined sources
Modified residuei512 – 5121S-4a-FMN cysteine

Post-translational modificationi

Autophosphorylated in response to blue light irradiation.Curated4 Publications
2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark.

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiO48963.
PRIDEiO48963.

PTM databases

iPTMnetiO48963.

Expressioni

Gene expression databases

GenevisibleiO48963. AT.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. 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).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-1553849,EBI-1553849
GRF6P483496EBI-1553849,EBI-1633785
RPT3Q9FMF52EBI-1553849,EBI-1553842

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi9041. 12 interactions.
DIPiDIP-38655N.
IntActiO48963. 11 interactions.
MINTiMINT-6823333.
STRINGi3702.AT3G45780.1.

Structurei

Secondary structure

1
996
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi186 – 1916Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi211 – 2144Combined sources
Helixi218 – 2225Combined sources
Turni226 – 2316Combined sources
Helixi234 – 2374Combined sources
Helixi244 – 25613Combined sources
Beta strandi260 – 2678Combined sources
Beta strandi273 – 28412Combined sources
Beta strandi290 – 30011Combined sources
Helixi453 – 47119Combined sources
Beta strandi475 – 4806Combined sources
Beta strandi489 – 4924Combined sources
Helixi494 – 5007Combined sources
Helixi504 – 5074Combined sources
Helixi512 – 5154Combined sources
Helixi522 – 53312Combined sources
Beta strandi538 – 5458Combined sources
Beta strandi551 – 56212Combined sources
Beta strandi568 – 5758Combined sources
Helixi588 – 5925Combined sources
Helixi595 – 61319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z6CX-ray2.10A/B180-308[»]
4HHDX-ray2.75A/B452-615[»]
ProteinModelPortaliO48963.
SMRiO48963. Positions 184-332, 458-989.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO48963.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini184 – 25774PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini258 – 31255PAC 1PROSITE-ProRule annotationAdd
BLAST
Domaini462 – 53574PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini536 – 59055PAC 2PROSITE-ProRule annotationAdd
BLAST
Domaini663 – 952290Protein kinasePROSITE-ProRule annotationCuratedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni806 – 86257Activation loopBy similarityAdd
BLAST

Domaini

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.By similarity

Sequence similaritiesi

Contains 2 PAC (PAS-associated C-terminal) domains.PROSITE-ProRule annotation
Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IH6N. Eukaryota.
COG2202. LUCA.
HOGENOMiHOG000265679.
InParanoidiO48963.
KOiK08282.
OMAiMSENVVP.
OrthoDBiEOG093600ZE.
PhylomeDBiO48963.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13426. PAS_9. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00086. PAC. 2 hits.
SM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 2 hits.
SSF56112. SSF56112. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 2 hits.
PROSITEiPS50113. PAC. 2 hits.
PS50112. PAS. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O48963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPTEKPSTK PSSRTLPRDT RGSLEVFNPS TQLTRPDNPV FRPEPPAWQN
60 70 80 90 100
LSDPRGTSPQ PRPQQEPAPS NPVRSDQEIA VTTSWMALKD PSPETISKKT
110 120 130 140 150
ITAEKPQKSA VAAEQRAAEW GLVLKTDTKT GKPQGVGVRN SGGTENDPNG
160 170 180 190 200
KKTTSQRNSQ NSCRSSGEMS DGDVPGGRSG IPRVSEDLKD ALSTFQQTFV
210 220 230 240 250
VSDATKPDYP IMYASAGFFN MTGYTSKEVV GRNCRFLQGS GTDADELAKI
260 270 280 290 300
RETLAAGNNY CGRILNYKKD GTSFWNLLTI APIKDESGKV LKFIGMQVEV
310 320 330 340 350
SKHTEGAKEK ALRPNGLPES LIRYDARQKD MATNSVTELV EAVKRPRALS
360 370 380 390 400
ESTNLHPFMT KSESDELPKK PARRMSENVV PSGRRNSGGG RRNSMQRINE
410 420 430 440 450
IPEKKSRKSS LSFMGIKKKS ESLDESIDDG FIEYGEEDDE ISDRDERPES
460 470 480 490 500
VDDKVRQKEM RKGIDLATTL ERIEKNFVIT DPRLPDNPII FASDSFLELT
510 520 530 540 550
EYSREEILGR NCRFLQGPET DLTTVKKIRN AIDNQTEVTV QLINYTKSGK
560 570 580 590 600
KFWNIFHLQP MRDQKGEVQY FIGVQLDGSK HVEPVRNVIE ETAVKEGEDL
610 620 630 640 650
VKKTAVNIDE AVRELPDANM TPEDLWANHS KVVHCKPHRK DSPPWIAIQK
660 670 680 690 700
VLESGEPIGL KHFKPVKPLG SGDTGSVHLV ELVGTDQLFA MKAMDKAVML
710 720 730 740 750
NRNKVHRARA EREILDLLDH PFLPALYASF QTKTHICLIT DYYPGGELFM
760 770 780 790 800
LLDRQPRKVL KEDAVRFYAA QVVVALEYLH CQGIIYRDLK PENVLIQGNG
810 820 830 840 850
DISLSDFDLS CLTSCKPQLL IPSIDEKKKK KQQKSQQTPI FMAEPMRASN
860 870 880 890 900
SFVGTEEYIA PEIISGAGHT SAVDWWALGI LMYEMLYGYT PFRGKTRQKT
910 920 930 940 950
FTNVLQKDLK FPASIPASLQ VKQLIFRLLQ RDPKKRLGCF EGANEVKQHS
960 970 980 990
FFKGINWALI RCTNPPELET PIFSGEAENG EKVVDPELED LQTNVF
Length:996
Mass (Da):111,689
Last modified:June 1, 1998 - v1
Checksum:iC9B68812F1B3A04E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030864 mRNA. Translation: AAC01753.1.
AL157735 Genomic DNA. Translation: CAB75791.1.
CP002686 Genomic DNA. Translation: AEE78072.1.
CP002686 Genomic DNA. Translation: AEE78073.1.
AF360218 mRNA. Translation: AAK25928.1.
AY040062 mRNA. Translation: AAK64120.1.
PIRiT47518.
RefSeqiNP_001030814.1. NM_001035737.1.
NP_190164.1. NM_114447.3.
UniGeneiAt.3720.
At.67829.

Genome annotation databases

EnsemblPlantsiAT3G45780.1; AT3G45780.1; AT3G45780.
AT3G45780.2; AT3G45780.2; AT3G45780.
GeneIDi823721.
GrameneiAT3G45780.1; AT3G45780.1; AT3G45780.
AT3G45780.2; AT3G45780.2; AT3G45780.
KEGGiath:AT3G45780.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030864 mRNA. Translation: AAC01753.1.
AL157735 Genomic DNA. Translation: CAB75791.1.
CP002686 Genomic DNA. Translation: AEE78072.1.
CP002686 Genomic DNA. Translation: AEE78073.1.
AF360218 mRNA. Translation: AAK25928.1.
AY040062 mRNA. Translation: AAK64120.1.
PIRiT47518.
RefSeqiNP_001030814.1. NM_001035737.1.
NP_190164.1. NM_114447.3.
UniGeneiAt.3720.
At.67829.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z6CX-ray2.10A/B180-308[»]
4HHDX-ray2.75A/B452-615[»]
ProteinModelPortaliO48963.
SMRiO48963. Positions 184-332, 458-989.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9041. 12 interactions.
DIPiDIP-38655N.
IntActiO48963. 11 interactions.
MINTiMINT-6823333.
STRINGi3702.AT3G45780.1.

PTM databases

iPTMnetiO48963.

Proteomic databases

PaxDbiO48963.
PRIDEiO48963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G45780.1; AT3G45780.1; AT3G45780.
AT3G45780.2; AT3G45780.2; AT3G45780.
GeneIDi823721.
GrameneiAT3G45780.1; AT3G45780.1; AT3G45780.
AT3G45780.2; AT3G45780.2; AT3G45780.
KEGGiath:AT3G45780.

Organism-specific databases

TAIRiAT3G45780.

Phylogenomic databases

eggNOGiENOG410IH6N. Eukaryota.
COG2202. LUCA.
HOGENOMiHOG000265679.
InParanoidiO48963.
KOiK08282.
OMAiMSENVVP.
OrthoDBiEOG093600ZE.
PhylomeDBiO48963.

Enzyme and pathway databases

BioCyciARA:AT3G45780-MONOMER.
ARA:GQT-2469-MONOMER.
BRENDAi2.7.11.1. 399.

Miscellaneous databases

EvolutionaryTraceiO48963.
PROiO48963.

Gene expression databases

GenevisibleiO48963. AT.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13426. PAS_9. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00086. PAC. 2 hits.
SM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 2 hits.
SSF56112. SSF56112. 2 hits.
TIGRFAMsiTIGR00229. sensory_box. 2 hits.
PROSITEiPS50113. PAC. 2 hits.
PS50112. PAS. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPHOT1_ARATH
AccessioniPrimary (citable) accession number: O48963
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: June 1, 1998
Last modified: September 7, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.