Reviewed, UniProtKB/Swiss-Prot O48963 (PHOT1_ARATH)

Names and origin

Protein names

Recommended name:
    Phototropin-1
    EC=2.7.11.1
Alternative name(s):
    Non-phototropic hypocotyl protein 1
    Root phototropism protein 1

Gene names

Name:	PHOT1
Synonyms:	JK224, NPH1, RPT1
Ordered Locus Names:	At3g45780
ORF Names:	T6D9_110

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	996 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Protein kinase that acts as a blue-light photoreceptor in a signal-transduction pathway for photo-induced movements. Required for blue-light mediated mRNA destabilization. Mediates calcium spiking of extracellular origin in response to low rate of blue light. Mediates also rapid membrane depolarization and growth inhibition in response to blue light. Necessary for root phototropism. Involved in hypocotyl phototropism under low rate but not under high rate blue light. Contributes to the chloroplast accumulation but seems to be not required for chloroplast translocation. Regulates stomata opening and photomorphogenesis response of leaf tissue. Not involved in hypocotyl elongation inhibition, anthocyanin accumulation or cotyledon opening. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts with RPT2 and RPT3. Ref.13 Ref.7
Subcellular location	Cell membrane; Peripheral membrane protein. Cytoplasm. Ref.12 Ref.13 Ref.7
Domain	The PAS repeats are required for binding of the FMN chromophores.
Post-translational modification	Autophosphorylated in response to blue light irradiation. Ref.4 Ref.5 2 molecules of FMN bind covalently to cysteines after exposure to blue light and are reversed in the dark.
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.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 2 PAC (PAS-associated C-terminal) domains. Contains 2 PAS (PER-ARNT-SIM) domains. Contains 1 protein kinase domain.
biophysicochemical properties	Absorption: Exhibits a smaller absorbance peak at 390 nm. The broad fluorescence emission spectrum peaks at 490 nm. Abs(max)=450 nm

Ontologies

Keywords
Biological process	Sensory transduction
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	ATP-binding Chromophore FMN Flavoprotein Nucleotide-binding
Molecular function	Kinase Photoreceptor protein Receptor Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chloroplast accumulation movement Inferred from mutant phenotype. Source: TAIR chloroplast avoidance movement Inferred from mutant phenotype. Source: TAIR negative regulation of anion channel activity by blue light Inferred from mutant phenotype. Source: TAIR phototropism Ref.1 Inferred from mutant phenotype. Source: TAIR protein amino acid autophosphorylation Inferred from direct assay. Source: TAIR protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW regulation of proton transport Inferred from genetic interaction. Source: TAIR regulation of stomatal movement Inferred from mutant phenotype. Source: TAIR regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro two-component signal transduction system (phosphorelay) Inferred from electronic annotation. Source: InterPro
Cellular component	internal side of plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FMN binding Traceable author statement. Source: TAIR blue light photoreceptor activity Ref.5 Inferred from direct assay. Source: TAIR protein binding Ref.7 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Ref.5 Inferred from direct assay. Source: TAIR two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At5g64330	Q0WSP1	1	EBI-1553849,EBI-1553842
PKS1	Q9SWI1	1	EBI-1553849,EBI-626200

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 996	996	Phototropin-1		PRO_0000086522
Regions
	Domain	184 – 257	74	PAS 1
	Domain	258 – 312	55	PAC 1
	Domain	462 – 535	74	PAS 2
	Domain	536 – 590	55	PAC 2
	Domain	663 – 952	290	Protein kinase
	Nucleotide binding	669 – 677	9	ATP By similarity
Sites
	Active site	788	1	Proton acceptor By similarity
	Binding site	692	1	ATP By similarity
Amino acid modifications
	Modified residue	234	1	S-4a-FMN cysteine
	Modified residue	512	1	S-4a-FMN cysteine
Experimental info
	Mutagenesis	512	1	C → A: Impaired photocycle. Ref.10
	Mutagenesis	774	1	Missing in nph1-1; loss of phototropism. Ref.1
	Mutagenesis	936	1	R → K in nph1-2; partial phototropism. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O48963-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: C9B68812F1B3A04E	FASTA	996	111,689
	10 20 30 40 50 60 MEPTEKPSTK PSSRTLPRDT RGSLEVFNPS TQLTRPDNPV FRPEPPAWQN LSDPRGTSPQ 70 80 90 100 110 120 PRPQQEPAPS NPVRSDQEIA VTTSWMALKD PSPETISKKT ITAEKPQKSA VAAEQRAAEW 130 140 150 160 170 180 GLVLKTDTKT GKPQGVGVRN SGGTENDPNG KKTTSQRNSQ NSCRSSGEMS DGDVPGGRSG 190 200 210 220 230 240 IPRVSEDLKD ALSTFQQTFV VSDATKPDYP IMYASAGFFN MTGYTSKEVV GRNCRFLQGS 250 260 270 280 290 300 GTDADELAKI RETLAAGNNY CGRILNYKKD GTSFWNLLTI APIKDESGKV LKFIGMQVEV 310 320 330 340 350 360 SKHTEGAKEK ALRPNGLPES LIRYDARQKD MATNSVTELV EAVKRPRALS ESTNLHPFMT 370 380 390 400 410 420 KSESDELPKK PARRMSENVV PSGRRNSGGG RRNSMQRINE IPEKKSRKSS LSFMGIKKKS 430 440 450 460 470 480 ESLDESIDDG FIEYGEEDDE ISDRDERPES VDDKVRQKEM RKGIDLATTL ERIEKNFVIT 490 500 510 520 530 540 DPRLPDNPII FASDSFLELT EYSREEILGR NCRFLQGPET DLTTVKKIRN AIDNQTEVTV 550 560 570 580 590 600 QLINYTKSGK KFWNIFHLQP MRDQKGEVQY FIGVQLDGSK HVEPVRNVIE ETAVKEGEDL 610 620 630 640 650 660 VKKTAVNIDE AVRELPDANM TPEDLWANHS KVVHCKPHRK DSPPWIAIQK VLESGEPIGL 670 680 690 700 710 720 KHFKPVKPLG SGDTGSVHLV ELVGTDQLFA MKAMDKAVML NRNKVHRARA EREILDLLDH 730 740 750 760 770 780 PFLPALYASF QTKTHICLIT DYYPGGELFM LLDRQPRKVL KEDAVRFYAA QVVVALEYLH 790 800 810 820 830 840 CQGIIYRDLK PENVLIQGNG DISLSDFDLS CLTSCKPQLL IPSIDEKKKK KQQKSQQTPI 850 860 870 880 890 900 FMAEPMRASN SFVGTEEYIA PEIISGAGHT SAVDWWALGI LMYEMLYGYT PFRGKTRQKT 910 920 930 940 950 960 FTNVLQKDLK FPASIPASLQ VKQLIFRLLQ RDPKKRLGCF EGANEVKQHS FFKGINWALI 970 980 990 RCTNPPELET PIFSGEAENG EKVVDPELED LQTNVF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain." Huala E., Oeller P.W., Liscum E., Han I.-S., Larsen E., Briggs W.R. Science 278:2120-2123(1997) [PubMed: 9405347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF VAL-774 AND ARG-936. Strain: cv. Columbia. Tissue: Hypocotyl.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Light-induced phosphorylation of a membrane protein plays an early role in signal transduction for phototropism in Arabidopsis thaliana." Reymond P., Short T.W., Briggs W.R., Poff K.L. Proc. Natl. Acad. Sci. U.S.A. 89:4718-4721(1992) [PubMed: 11537679] [Abstract] Cited for: PHOSPHORYLATION.
[5]	"Arabidopsis NPH1: a flavoprotein with the properties of a photoreceptor for phototropism." Christie J.M., Reymond P., Powell G.K., Bernasconi P., Raibekas A.A., Liscum E., Briggs W.R. Science 282:1698-1701(1998) [PubMed: 9831559] [Abstract] Cited for: PHOSPHORYLATION.
[6]	"LOV (light, oxygen, or voltage) domains of the blue-light photoreceptor phototropin (nph1): binding sites for the chromophore flavin mononucleotide." Christie J.M., Salomon M., Nozue K., Wada M., Briggs W.R. Proc. Natl. Acad. Sci. U.S.A. 96:8779-8783(1999) [PubMed: 10411952] [Abstract] Cited for: FMN-BINDING.
[7]	"Arabidopsis NPH3: a NPH1 photoreceptor-interacting protein essential for phototropism." Motchoulski A., Liscum E. Science 286:961-964(1999) [PubMed: 10542152] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RPT3.
[8]	"RPT2: a signal transducer of the phototropic response in Arabidopsis." Sakai T., Wada T., Ishiguro S., Okada K. Plant Cell 12:225-236(2000) [PubMed: 10662859] [Abstract] Cited for: FUNCTION.
[9]	"Unexpected roles for cryptochrome 2 and phototropin revealed by high-resolution analysis of blue light-mediated hypocotyl growth inhibition." Folta K.M., Spalding E.P. Plant J. 26:471-478(2001) [PubMed: 11439133] [Abstract] Cited for: FUNCTION.
[10]	"Photochemical properties of the flavin mononucleotide-binding domains of the phototropins from Arabidopsis, rice, and Chlamydomonas reinhardtii." Kasahara M., Swartz T.E., Olney M.A., Onodera A., Mochizuki N., Fukuzawa H., Asamizu E., Tabata S., Kanegae H., Takano M., Christie J.M., Nagatani A., Briggs W.R. Plant Physiol. 129:762-773(2002) [PubMed: 12068117] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-512.
[11]	"Phototropin 1 is required for high-fluence blue-light-mediated mRNA destabilization." Folta K.M., Kaufman L.S. Plant Mol. Biol. 51:609-618(2003) [PubMed: 12650626] [Abstract] Cited for: FUNCTION.
[12]	"Phot1 and phot2 mediate blue light-induced transient increases in cytosolic Ca2+ differently in Arabidopsis leaves." Harada A., Sakai T., Okada K. Proc. Natl. Acad. Sci. U.S.A. 100:8583-8588(2003) [PubMed: 12821778] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[13]	"RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana." Inada S., Ohgishi M., Mayama T., Okada K., Sakai T. Plant Cell 16:887-896(2004) [PubMed: 15031408] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RPT2.
[14]	"Functional analysis of each blue light receptor, cry1, cry2, phot1, and phot2, by using combinatorial multiple mutants in Arabidopsis." Ohgishi M., Saji K., Okada K., Sakai T. Proc. Natl. Acad. Sci. U.S.A. 101:2223-2228(2004) [PubMed: 14982991] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF030864 mRNA. Translation: AAC01753.1.
AL157735 Genomic DNA. Translation: CAB75791.1.
AF360218 mRNA. Translation: AAK25928.1.
AY040062 mRNA. Translation: AAK64120.1.

IPI

IPI00539117.

PIR

T47518.

RefSeq

NP_001030814.1.
NP_190164.1.

UniGene

At.3720
At.67829

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z6C	X-ray	2.10	A/B	180-308	[»]

SMR

O48963. Positions 475-575.

ModBase

Search...

Protein-protein interaction databases

IntAct

O48963. 3 interactions.

Proteomic databases

PRIDE

O48963.

ProMEX

O48963.

Genome annotation databases

GeneID

823721.

GenomeReviews

Gene locus AT3G45780 in contig BA000014_GR.

KEGG

ath:AT3G45780.

NMPDR

fig|3702.1.peg.15792.

Organism-specific databases

TAIR

At3g45780.

Phylogenomic databases

OMA

O48963. PEDLWAN.

Enzyme and pathway databases

BRENDA

2.7.11.1. 302.

Gene expression databases

ArrayExpress

O48963.

GermOnline

AT3G45780. Arabidopsis thaliana.

Family and domain databases

InterPro

IPR001610. PAC.
IPR000014. PAS.
IPR000700. PAS-assoc_C.
IPR013767. PAS_fold.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]

Pfam

PF00989. PAS. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00086. PAC. 2 hits.
SM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00229. sensory_box. 2 hits.

PROSITE

PS50113. 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]

ProtoNet

Search...

Entry information

Entry name

PHOT1_ARATH

Accession

Primary (citable) accession number: O48963

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	June 1, 1998
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)