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Protein

Phototropin-2

Gene

PHOT2

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. Mediates calcium spiking of extra- and intracellular origins in response to blue light. Involved in hypocotyl phototropism. Contributes to the chloroplast accumulation in low blue light and mediates their translocation (avoidance response) at high fluence. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening.6 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)DescriptionActionsGraphical viewLength
Binding sitei187FMN1 Publication1
Binding sitei202FMN1 Publication1
Binding sitei212FMN1 Publication1
Binding sitei233FMN1 Publication1
Binding sitei443FMNBy similarity1
Binding sitei458FMNBy similarity1
Binding sitei468FMNBy similarity1
Binding sitei489FMNBy similarity1
Binding sitei606ATPPROSITE-ProRule annotation1
Active sitei702Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 174FMN1 Publication6
Nucleotide bindingi425 – 430FMNBy similarity6
Nucleotide bindingi583 – 591ATPPROSITE-ProRule annotation9

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 serine/threonine kinase activity Source: TAIR

GO - Biological processi

  • chloroplast relocation 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
  • response to blue light Source: TAIR
  • response to cytokinin Source: TAIR
  • stomatal movement 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

Names & Taxonomyi

Protein namesi
Recommended name:
Phototropin-2 (EC:2.7.11.1)
Alternative name(s):
Defective in chloroplast avoidance protein 1
Non-phototropic hypocotyl 1-like protein 1
Short name:
AtKin7
Short name:
NPH1-like protein 1
Gene namesi
Name:PHOT2
Synonyms:CAV1, KIN7, NPL1
Ordered Locus Names:At5g58140
ORF Names:K21L19.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G58140.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • membrane Source: TAIR
  • nucleus Source: GO_Central
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi170C → A: No effect on light-dependent autophosphorylation. 1 Publication1
Mutagenesisi217T → Q: Loss of dimerization. 1 Publication1
Mutagenesisi232M → V: Loss of dimerization. 1 Publication1
Mutagenesisi426C → A: Severe loss of light-sensing and light-dependent autophosphorylation. 1 Publication1
Mutagenesisi727T → I in cav1-2; loss of chloroplast avoidance response in response to high fluence blue light. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865231 – 915Phototropin-2Add BLAST915

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineCombined sources1
Modified residuei22PhosphoserineCombined sources1
Modified residuei121PhosphoserineBy similarity1
Modified residuei170S-4a-FMN cysteineBy similarity1
Modified residuei364PhosphoserineCombined sources1
Modified residuei426S-4a-FMN cysteineBy similarity1

Post-translational modificationi

Autophosphorylated in response to blue light irradiation.1 Publication
2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP93025.
PRIDEiP93025.

PTM databases

iPTMnetiP93025.

Expressioni

Tissue specificityi

Expressed in leaves, stems and flowers, and to a lower extent in roots.1 Publication

Inductioni

Light fluence rate-dependent induction, independent of light quality.1 Publication

Gene expression databases

ExpressionAtlasiP93025. baseline and differential.
GenevisibleiP93025. AT.

Interactioni

Subunit structurei

Homodimer. Interacts with PKS1, PKS2, RPT3 and PHOT1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2270423,EBI-2270423

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi21170. 11 interactors.
DIPiDIP-53468N.
IntActiP93025. 3 interactors.
MINTiMINT-6823418.
STRINGi3702.AT5G58140.1.

Structurei

Secondary structure

1915
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi124 – 130Combined sources7
Beta strandi134 – 139Combined sources6
Beta strandi147 – 150Combined sources4
Helixi152 – 158Combined sources7
Helixi162 – 165Combined sources4
Helixi170 – 173Combined sources4
Helixi180 – 191Combined sources12
Beta strandi196 – 203Combined sources8
Beta strandi209 – 220Combined sources12
Beta strandi226 – 235Combined sources10
Beta strandi390 – 394Combined sources5
Beta strandi403 – 406Combined sources4
Helixi408 – 414Combined sources7
Helixi418 – 421Combined sources4
Helixi426 – 429Combined sources4
Helixi436 – 447Combined sources12
Beta strandi452 – 459Combined sources8
Beta strandi465 – 476Combined sources12
Beta strandi482 – 491Combined sources10
Turni492 – 495Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z6DX-ray2.00A/B117-246[»]
4EEPX-ray1.70A385-496[»]
4EERX-ray1.75A385-496[»]
4EESX-ray1.80A385-496[»]
4EETX-ray1.20B/D385-496[»]
4EEUX-ray1.41A385-496[»]
4NXBX-ray2.56A/B388-496[»]
4NXEX-ray2.10A/B388-496[»]
4NXFX-ray1.77A/B388-496[»]
4NXGX-ray2.09A/B388-496[»]
ProteinModelPortaliP93025.
SMRiP93025.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP93025.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini120 – 193PAS 1PROSITE-ProRule annotationAdd BLAST74
Domaini194 – 248PAC 1PROSITE-ProRule annotationAdd BLAST55
Domaini376 – 449PAS 2PROSITE-ProRule annotationAdd BLAST74
Domaini450 – 504PAC 2PROSITE-ProRule annotationAdd BLAST55
Domaini577 – 864Protein kinasePROSITE-ProRule annotationAdd BLAST288

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni720 – 774Activation loopBy similarityAdd BLAST55

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi16 – 114Ser-richAdd BLAST99

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.
InParanoidiP93025.
KOiK20715.
OMAiPRIPDNP.
OrthoDBiEOG093600ZE.
PhylomeDBiP93025.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P93025-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERPRAPPSP LNDAESLSER RSLEIFNPSS GKETHGSTSS SSKPPLDGNN
60 70 80 90 100
KGSSSKWMEF QDSAKITERT AEWGLSAVKP DSGDDGISFK LSSEVERSKN
110 120 130 140 150
MSRRSSEEST SSESGAFPRV SQELKTALST LQQTFVVSDA TQPHCPIVYA
160 170 180 190 200
SSGFFTMTGY SSKEIVGRNC RFLQGPDTDK NEVAKIRDCV KNGKSYCGRL
210 220 230 240 250
LNYKKDGTPF WNLLTVTPIK DDQGNTIKFI GMQVEVSKYT EGVNDKALRP
260 270 280 290 300
NGLSKSLIRY DARQKEKALD SITEVVQTIR HRKSQVQESV SNDTMVKPDS
310 320 330 340 350
STTPTPGRQT RQSDEASKSF RTPGRVSTPT GSKLKSSNNR HEDLLRMEPE
360 370 380 390 400
ELMLSTEVIG QRDSWDLSDR ERDIRQGIDL ATTLERIEKN FVISDPRLPD
410 420 430 440 450
NPIIFASDSF LELTEYSREE ILGRNCRFLQ GPETDQATVQ KIRDAIRDQR
460 470 480 490 500
EITVQLINYT KSGKKFWNLF HLQPMRDQKG ELQYFIGVQL DGSDHVEPLQ
510 520 530 540 550
NRLSERTEMQ SSKLVKATAT NVDEAVRELP DANTRPEDLW AAHSKPVYPL
560 570 580 590 600
PHNKESTSWK AIKKIQASGE TVGLHHFKPI KPLGSGDTGS VHLVELKGTG
610 620 630 640 650
ELYAMKAMEK TMMLNRNKAH RACIEREIIS LLDHPFLPTL YASFQTSTHV
660 670 680 690 700
CLITDFCPGG ELFALLDRQP MKILTEDSAR FYAAEVVIGL EYLHCLGIVY
710 720 730 740 750
RDLKPENILL KKDGHIVLAD FDLSFMTTCT PQLIIPAAPS KRRRSKSQPL
760 770 780 790 800
PTFVAEPSTQ SNSFVGTEEY IAPEIITGAG HTSAIDWWAL GILLYEMLYG
810 820 830 840 850
RTPFRGKNRQ KTFANILHKD LTFPSSIPVS LVGRQLINTL LNRDPSSRLG
860 870 880 890 900
SKGGANEIKQ HAFFRGINWP LIRGMSPPPL DAPLSIIEKD PNAKDIKWED
910
DGVLVNSTDL DIDLF
Length:915
Mass (Da):102,472
Last modified:November 22, 2005 - v2
Checksum:iCA163E2596289737
GO
Isoform 2 (identifier: P93025-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     535-549: RPEDLWAAHSKPVYP → VRCTSSLLLNKDGKV
     550-915: Missing.

Note: May be due to a competing acceptor splice site. No experimental confirmation available.
Show »
Length:549
Mass (Da):61,600
Checksum:i3777BA44BAE08C96
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti722D → Y in AAB39188 (Ref. 5) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_016306535 – 549RPEDL…KPVYP → VRCTSSLLLNKDGKV in isoform 2. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_016307550 – 915Missing in isoform 2. 1 PublicationAdd BLAST366

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053941 mRNA. Translation: AAC27293.2.
AB019228, AB024029 Genomic DNA. Translation: BAB09904.1.
CP002688 Genomic DNA. Translation: AED97002.1.
CP002688 Genomic DNA. Translation: AED97004.1.
AY093141 mRNA. Translation: AAM13140.1.
BT008901 mRNA. Translation: AAP68340.1.
U79744 mRNA. Translation: AAB39188.1.
PIRiT51600.
RefSeqiNP_851210.1. NM_180879.2. [P93025-1]
NP_851211.1. NM_180880.2. [P93025-1]
UniGeneiAt.22044.
At.72500.

Genome annotation databases

EnsemblPlantsiAT5G58140.1; AT5G58140.1; AT5G58140. [P93025-1]
AT5G58140.2; AT5G58140.2; AT5G58140. [P93025-1]
GeneIDi835926.
GrameneiAT5G58140.1; AT5G58140.1; AT5G58140.
AT5G58140.2; AT5G58140.2; AT5G58140.
KEGGiath:AT5G58140.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053941 mRNA. Translation: AAC27293.2.
AB019228, AB024029 Genomic DNA. Translation: BAB09904.1.
CP002688 Genomic DNA. Translation: AED97002.1.
CP002688 Genomic DNA. Translation: AED97004.1.
AY093141 mRNA. Translation: AAM13140.1.
BT008901 mRNA. Translation: AAP68340.1.
U79744 mRNA. Translation: AAB39188.1.
PIRiT51600.
RefSeqiNP_851210.1. NM_180879.2. [P93025-1]
NP_851211.1. NM_180880.2. [P93025-1]
UniGeneiAt.22044.
At.72500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z6DX-ray2.00A/B117-246[»]
4EEPX-ray1.70A385-496[»]
4EERX-ray1.75A385-496[»]
4EESX-ray1.80A385-496[»]
4EETX-ray1.20B/D385-496[»]
4EEUX-ray1.41A385-496[»]
4NXBX-ray2.56A/B388-496[»]
4NXEX-ray2.10A/B388-496[»]
4NXFX-ray1.77A/B388-496[»]
4NXGX-ray2.09A/B388-496[»]
ProteinModelPortaliP93025.
SMRiP93025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21170. 11 interactors.
DIPiDIP-53468N.
IntActiP93025. 3 interactors.
MINTiMINT-6823418.
STRINGi3702.AT5G58140.1.

PTM databases

iPTMnetiP93025.

Proteomic databases

PaxDbiP93025.
PRIDEiP93025.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G58140.1; AT5G58140.1; AT5G58140. [P93025-1]
AT5G58140.2; AT5G58140.2; AT5G58140. [P93025-1]
GeneIDi835926.
GrameneiAT5G58140.1; AT5G58140.1; AT5G58140.
AT5G58140.2; AT5G58140.2; AT5G58140.
KEGGiath:AT5G58140.

Organism-specific databases

TAIRiAT5G58140.

Phylogenomic databases

eggNOGiENOG410IH6N. Eukaryota.
COG2202. LUCA.
HOGENOMiHOG000265679.
InParanoidiP93025.
KOiK20715.
OMAiPRIPDNP.
OrthoDBiEOG093600ZE.
PhylomeDBiP93025.

Miscellaneous databases

EvolutionaryTraceiP93025.
PROiP93025.

Gene expression databases

ExpressionAtlasiP93025. baseline and differential.
GenevisibleiP93025. 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 nameiPHOT2_ARATH
AccessioniPrimary (citable) accession number: P93025
Secondary accession number(s): O81204, Q8RWE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: November 30, 2016
This is version 148 of the entry and version 2 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 11 seconds and 15 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.