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Protein

Ultraviolet-B receptor UVR8

Gene

UVR8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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
  • identical protein binding Source: IntAct
  • 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

Keywordsi

Molecular functionPhotoreceptor protein, Receptor
Biological processSensory transduction
LigandChromophore

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

AraportiAT5G63860
TAIRilocus:2163986 AT5G63860

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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

ExpressionAtlasiQ9FN03 baseline and differential
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

Show more details

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: TAIR
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: TAIR

Protein-protein interaction databases

BioGridi21748, 8 interactors
DIPiDIP-59667N
IntActiQ9FN03, 3 interactors
MINTiQ9FN03
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 strandi205 – 209Combined sources5
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 – 312Combined sources3
Beta strandi316 – 322Combined sources7
Helixi325 – 327Combined sources3
Beta strandi330 – 335Combined sources6
Beta strandi337 – 344Combined sources8
Beta strandi349 – 353Combined sources5
Beta strandi361 – 364Combined sources4
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[»]
4NAAX-ray1.67A/B/C/D13-381[»]
4NBMX-ray1.61A/B/C/D13-381[»]
4NC4X-ray1.75A/B/C/D13-381[»]
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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1426 Eukaryota
COG5184 LUCA
HOGENOMiHOG000240817
InParanoidiQ9FN03
OMAiRHTMAAD
OrthoDBiEOG0936083F
PhylomeDBiQ9FN03

Family and domain databases

Gene3Di2.130.10.30, 1 hit
InterProiView protein in InterPro
IPR009091 RCC1/BLIP-II
IPR000408 Reg_chr_condens
IPR032996 UVR8
PANTHERiPTHR22870:SF317 PTHR22870:SF317, 1 hit
PfamiView protein in Pfam
PF00415 RCC1, 7 hits
PRINTSiPR00633 RCCNDNSATION
SUPFAMiSSF50985 SSF50985, 1 hit
PROSITEiView protein in PROSITE
PS00626 RCC1_2, 5 hits
PS50012 RCC1_3, 7 hits

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

Similar proteinsi

Entry informationi

Entry nameiUVR8_ARATH
AccessioniPrimary (citable) accession number: Q9FN03
Secondary accession number(s): Q9XHD7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2001
Last modified: April 25, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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