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Protein

Ultraviolet-B receptor UVR8

Gene

UVR8

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

Functioni

UV-B specific signaling component that acts as UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV-B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore.12 Publications

GO - Molecular functioni

  • chromatin binding Source: TAIR
  • guanyl-nucleotide exchange factor activity Source: TAIR
  • photoreceptor activity Source: UniProtKB-KW
  • protein homodimerization activity Source: TAIR

GO - Biological processi

  • entrainment of circadian clock Source: TAIR
  • protein-chromophore linkage Source: UniProtKB-KW
  • response to UV Source: TAIR
  • response to UV-B Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Photoreceptor protein, Receptor

Keywords - Biological processi

Sensory transduction

Keywords - Ligandi

Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
Ultraviolet-B receptor UVR8
Alternative name(s):
Protein UV-B RESISTANCE 8
RCC1 domain-containing protein UVR8
Gene namesi
Name:UVR8
Ordered Locus Names:At5g63860
ORF Names:MGI19.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G63860.

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: TAIR
  • cytosol Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Hypersensitivity to UV-B.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi39W → A: Loss of function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi39W → F: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi39W → Y: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi92W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi94W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi144W → A: Cannot interact with COP1. 1 Publication1
Mutagenesisi144W → F: No effect on the interaction with COP1. 1 Publication1
Mutagenesisi144W → Y: No effect on the interaction with COP1. 1 Publication1
Mutagenesisi145G → S in uvr8-15; loss of function and interaction with COP1. 1 Publication1
Mutagenesisi196 – 200Missing in uvr8-1; loss of function. 1 Publication5
Mutagenesisi196W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi198W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi202G → R in uvr8-9; loss of function and interaction with COP1. 1 Publication1
Mutagenesisi233W → A: Reduces response to UV-B. 2 Publications1
Mutagenesisi250W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi283G → E in uvr8-5; loss of response to UV-B. 1 Publication1
Mutagenesisi285W → A: Loss of function. Constitutive monomer. 3 Publications1
Mutagenesisi285W → F: Loss of function. Constitutive homodimer and no interaction with COP1. 3 Publications1
Mutagenesisi300W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi302W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1
Mutagenesisi337W → A: Reduces response to UV-B. 2 Publications1
Mutagenesisi352W → A: Cannot interact with COP1. 1 Publication1
Mutagenesisi352W → F: No effect on the interaction with COP1. 1 Publication1
Mutagenesisi352W → Y: No effect on the interaction with COP1. 1 Publication1
Mutagenesisi400W → A: No effect on function, homodimerization and interaction with COP1. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00004217222 – 440Ultraviolet-B receptor UVR8Add BLAST439

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9FN03.
PRIDEiQ9FN03.

PTM databases

iPTMnetiQ9FN03.

Expressioni

Gene expression databases

GenevisibleiQ9FN03. AT.

Interactioni

Subunit structurei

Homodimer in the absence of UV-B, but absorption of UV-B induces monomerization of UVR8 and interaction with COP1. Interacts with RUP1, RUP2 and histone H2B.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COP1P432543EBI-2407499,EBI-301649

GO - Molecular functioni

  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi21748. 8 interactors.
DIPiDIP-59667N.
IntActiQ9FN03. 1 interactor.
MINTiMINT-7033609.
STRINGi3702.AT5G63860.1.

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 22Combined sources6
Beta strandi24 – 31Combined sources8
Turni32 – 34Combined sources3
Beta strandi35 – 40Combined sources6
Beta strandi49 – 51Combined sources3
Beta strandi55 – 60Combined sources6
Helixi62 – 64Combined sources3
Beta strandi69 – 74Combined sources6
Beta strandi76 – 83Combined sources8
Turni84 – 87Combined sources4
Beta strandi88 – 93Combined sources6
Helixi96 – 98Combined sources3
Beta strandi102 – 104Combined sources3
Beta strandi108 – 113Combined sources6
Helixi115 – 117Combined sources3
Beta strandi122 – 127Combined sources6
Beta strandi129 – 136Combined sources8
Beta strandi141 – 145Combined sources5
Beta strandi154 – 156Combined sources3
Beta strandi160 – 165Combined sources6
Helixi167 – 169Combined sources3
Beta strandi174 – 179Combined sources6
Beta strandi181 – 188Combined sources8
Beta strandi193 – 197Combined sources5
Beta strandi206 – 209Combined sources4
Beta strandi212 – 217Combined sources6
Beta strandi226 – 231Combined sources6
Beta strandi233 – 240Combined sources8
Beta strandi245 – 249Combined sources5
Beta strandi258 – 260Combined sources3
Beta strandi264 – 269Combined sources6
Helixi271 – 273Combined sources3
Beta strandi278 – 283Combined sources6
Beta strandi285 – 292Combined sources8
Beta strandi297 – 301Combined sources5
Beta strandi310 – 314Combined sources5
Beta strandi316 – 322Combined sources7
Helixi325 – 327Combined sources3
Beta strandi330 – 335Combined sources6
Beta strandi337 – 344Combined sources8
Beta strandi349 – 353Combined sources5
Beta strandi362 – 364Combined sources3
Beta strandi368 – 373Combined sources6
Helixi375 – 377Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D9SX-ray1.70A/B1-405[»]
4DNUX-ray1.76A10-381[»]
4DNVX-ray2.00A/B/C/D12-381[»]
4DNWX-ray1.77A/B12-385[»]
ProteinModelPortaliQ9FN03.
SMRiQ9FN03.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati32 – 84RCC1 1Add BLAST53
Repeati86 – 137RCC1 2Add BLAST52
Repeati139 – 189RCC1 3Add BLAST51
Repeati190 – 241RCC1 4Add BLAST52
Repeati243 – 293RCC1 5Add BLAST51
Repeati294 – 345RCC1 6Add BLAST52
Repeati347 – 399RCC1 7Add BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni397 – 423Required for interaction with COP1Add BLAST27

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
HOGENOMiHOG000240817.
InParanoidiQ9FN03.
OMAiHGIRIKQ.
OrthoDBiEOG0936083F.
PhylomeDBiQ9FN03.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR032996. UVR8.
[Graphical view]
PANTHERiPTHR22870:SF193. PTHR22870:SF193. 1 hit.
PfamiPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00626. RCC1_2. 5 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9FN03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEDMAADEV TAPPRKVLII SAGASHSVAL LSGDIVCSWG RGEDGQLGHG
60 70 80 90 100
DAEDRPSPTQ LSALDGHQIV SVTCGADHTV AYSQSGMEVY SWGWGDFGRL
110 120 130 140 150
GHGNSSDLFT PLPIKALHGI RIKQIACGDS HCLAVTMEGE VQSWGRNQNG
160 170 180 190 200
QLGLGDTEDS LVPQKIQAFE GIRIKMVAAG AEHTAAVTED GDLYGWGWGR
210 220 230 240 250
YGNLGLGDRT DRLVPERVTS TGGEKMSMVA CGWRHTISVS YSGALYTYGW
260 270 280 290 300
SKYGQLGHGD LEDHLIPHKL EALSNSFISQ ISGGWRHTMA LTSDGKLYGW
310 320 330 340 350
GWNKFGQVGV GNNLDQCSPV QVRFPDDQKV VQVSCGWRHT LAVTERNNVF
360 370 380 390 400
AWGRGTNGQL GIGESVDRNF PKIIEALSVD GASGQHIESS NIDPSSGKSW
410 420 430 440
VSPAERYAVV PDETGLTDGS SKGNGGDISV PQTDVKRVRI
Length:440
Mass (Da):47,118
Last modified:March 1, 2001 - v1
Checksum:iD2EA103CCFC92E98
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173R → P in AAD43920 (PubMed:12226503).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130441 mRNA. Translation: AAD43920.1.
AB007646 Genomic DNA. Translation: BAB11034.1.
CP002688 Genomic DNA. Translation: AED97805.1.
AY125497 mRNA. Translation: AAM78089.1.
BT000600 mRNA. Translation: AAN18169.1.
PIRiT50662.
RefSeqiNP_201191.1. NM_125781.4.
UniGeneiAt.49214.

Genome annotation databases

EnsemblPlantsiAT5G63860.1; AT5G63860.1; AT5G63860.
GeneIDi836506.
GrameneiAT5G63860.1; AT5G63860.1; AT5G63860.
KEGGiath:AT5G63860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130441 mRNA. Translation: AAD43920.1.
AB007646 Genomic DNA. Translation: BAB11034.1.
CP002688 Genomic DNA. Translation: AED97805.1.
AY125497 mRNA. Translation: AAM78089.1.
BT000600 mRNA. Translation: AAN18169.1.
PIRiT50662.
RefSeqiNP_201191.1. NM_125781.4.
UniGeneiAt.49214.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D9SX-ray1.70A/B1-405[»]
4DNUX-ray1.76A10-381[»]
4DNVX-ray2.00A/B/C/D12-381[»]
4DNWX-ray1.77A/B12-385[»]
ProteinModelPortaliQ9FN03.
SMRiQ9FN03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21748. 8 interactors.
DIPiDIP-59667N.
IntActiQ9FN03. 1 interactor.
MINTiMINT-7033609.
STRINGi3702.AT5G63860.1.

PTM databases

iPTMnetiQ9FN03.

Proteomic databases

PaxDbiQ9FN03.
PRIDEiQ9FN03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G63860.1; AT5G63860.1; AT5G63860.
GeneIDi836506.
GrameneiAT5G63860.1; AT5G63860.1; AT5G63860.
KEGGiath:AT5G63860.

Organism-specific databases

TAIRiAT5G63860.

Phylogenomic databases

eggNOGiKOG1426. Eukaryota.
COG5184. LUCA.
HOGENOMiHOG000240817.
InParanoidiQ9FN03.
OMAiHGIRIKQ.
OrthoDBiEOG0936083F.
PhylomeDBiQ9FN03.

Miscellaneous databases

PROiQ9FN03.

Gene expression databases

GenevisibleiQ9FN03. AT.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
IPR032996. UVR8.
[Graphical view]
PANTHERiPTHR22870:SF193. PTHR22870:SF193. 1 hit.
PfamiPF00415. RCC1. 7 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00626. RCC1_2. 5 hits.
PS50012. RCC1_3. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUVR8_ARATH
AccessioniPrimary (citable) accession number: Q9FN03
Secondary accession number(s): Q9XHD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.