UVR8_ARATH
ID UVR8_ARATH Reviewed; 440 AA.
AC Q9FN03; Q9XHD7;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ultraviolet-B receptor UVR8 {ECO:0000303|PubMed:12226503};
DE AltName: Full=Protein UV-B RESISTANCE 8 {ECO:0000303|PubMed:12226503};
DE AltName: Full=RCC1 domain-containing protein UVR8 {ECO:0000303|PubMed:12226503};
GN Name=UVR8 {ECO:0000303|PubMed:12226503};
GN OrderedLocusNames=At5g63860 {ECO:0000312|Araport:AT5G63860};
GN ORFNames=MGI19.7 {ECO:0000312|EMBL:BAB11034.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 196-TRP--ARG-200.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12226503; DOI=10.1104/pp.005041;
RA Kliebenstein D.J., Lim J.E., Landry L.G., Last R.L.;
RT "Arabidopsis UVR8 regulates ultraviolet-B signal transduction and tolerance
RT and contains sequence similarity to human regulator of chromatin
RT condensation 1.";
RL Plant Physiol. 130:234-243(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16330762; DOI=10.1073/pnas.0507187102;
RA Brown B.A., Cloix C., Jiang G.H., Kaiserli E., Herzyk P.,
RA Kliebenstein D.J., Jenkins G.I.;
RT "A UV-B-specific signaling component orchestrates plant UV protection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18225-18230(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17720867; DOI=10.1105/tpc.107.053330;
RA Kaiserli E., Jenkins G.I.;
RT "UV-B promotes rapid nuclear translocation of the Arabidopsis UV-B specific
RT signaling component UVR8 and activates its function in the nucleus.";
RL Plant Cell 19:2662-2673(2007).
RN [7]
RP FUNCTION.
RX PubMed=18055587; DOI=10.1104/pp.107.108456;
RA Brown B.A., Jenkins G.I.;
RT "UV-B signaling pathways with different fluence-rate response profiles are
RT distinguished in mature Arabidopsis leaf tissue by requirement for UVR8,
RT HY5, and HYH.";
RL Plant Physiol. 146:576-588(2008).
RN [8]
RP INTERACTION WITH HISTONE H2B.
RX PubMed=20031919; DOI=10.1093/mp/ssm012;
RA Cloix C., Jenkins G.I.;
RT "Interaction of the Arabidopsis UV-B-specific signaling component UVR8 with
RT chromatin.";
RL Mol. Plant 1:118-128(2008).
RN [9]
RP FUNCTION, AND INTERACTION WITH COP1.
RC STRAIN=cv. Wassilewskija;
RX PubMed=19165148; DOI=10.1038/emboj.2009.4;
RA Favory J.J., Stec A., Gruber H., Rizzini L., Oravecz A., Funk M.,
RA Albert A., Cloix C., Jenkins G.I., Oakeley E.J., Seidlitz H.K., Nagy F.,
RA Ulm R.;
RT "Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and
RT stress acclimation in Arabidopsis.";
RL EMBO J. 28:591-601(2009).
RN [10]
RP FUNCTION.
RX PubMed=19402876; DOI=10.1111/j.1469-8137.2009.02855.x;
RA Wargent J.J., Gegas V.C., Jenkins G.I., Doonan J.H., Paul N.D.;
RT "UVR8 in Arabidopsis thaliana regulates multiple aspects of cellular
RT differentiation during leaf development in response to ultraviolet B
RT radiation.";
RL New Phytol. 183:315-326(2009).
RN [11]
RP FUNCTION, AND INTERACTION WITH RUP1 AND RUP2.
RX PubMed=21041653; DOI=10.1073/pnas.0914532107;
RA Gruber H., Heijde M., Heller W., Albert A., Seidlitz H.K., Ulm R.;
RT "Negative feedback regulation of UV-B-induced photomorphogenesis and stress
RT acclimation in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20132-20137(2010).
RN [12]
RP FUNCTION.
RX PubMed=21395889; DOI=10.1111/j.1365-313x.2011.04573.x;
RA Feher B., Kozma-Bognar L., Kevei E., Hajdu A., Binkert M., Davis S.J.,
RA Schaefer E., Ulm R., Nagy F.;
RT "Functional interaction of the circadian clock and UV RESISTANCE LOCUS 8-
RT controlled UV-B signaling pathways in Arabidopsis thaliana.";
RL Plant J. 67:37-48(2011).
RN [13]
RP FUNCTION, SUBUNIT, INTERACTION WITH COP1, AND MUTAGENESIS OF GLY-145;
RP GLY-202 AND TRP-285.
RX PubMed=21454788; DOI=10.1126/science.1200660;
RA Rizzini L., Favory J.J., Cloix C., Faggionato D., O'Hara A., Kaiserli E.,
RA Baumeister R., Schaefer E., Nagy F., Jenkins G.I., Ulm R.;
RT "Perception of UV-B by the Arabidopsis UVR8 protein.";
RL Science 332:103-106(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP FUNCTION.
RX PubMed=22447155; DOI=10.1093/mp/sss025;
RA Demkura P.V., Ballare C.L.;
RT "UVR8 mediates UV-B-induced Arabidopsis defense responses against Botrytis
RT cinerea by controlling sinapate accumulation.";
RL Mol. Plant 5:642-652(2012).
RN [16]
RP FUNCTION.
RX PubMed=23161229; DOI=10.1007/s11120-012-9785-y;
RA Davey M.P., Susanti N.I., Wargent J.J., Findlay J.E., Paul Quick W.,
RA Paul N.D., Jenkins G.I.;
RT "The UV-B photoreceptor UVR8 promotes photosynthetic efficiency in
RT Arabidopsis thaliana exposed to elevated levels of UV-B.";
RL Photosyn. Res. 114:121-131(2012).
RN [17]
RP FUNCTION, SUBUNIT, INTERACTION WITH COP1, AND MUTAGENESIS OF TRP-39;
RP TRP-92; TRP-94; TRP-144; TRP-196; TRP-198; TRP-233; TRP-250; TRP-285;
RP TRP-300; TRP-302; TRP-337; TRP-352 AND TRP-400.
RX PubMed=23012433; DOI=10.1105/tpc.112.101451;
RA O'Hara A., Jenkins G.I.;
RT "In vivo function of tryptophans in the Arabidopsis UV-B photoreceptor
RT UVR8.";
RL Plant Cell 24:3755-3766(2012).
RN [18]
RP FUNCTION, INTERACTION WITH COP1; RUP1 AND RUP2, AND MUTAGENESIS OF GLY-283.
RX PubMed=22988111; DOI=10.1073/pnas.1210898109;
RA Cloix C., Kaiserli E., Heilmann M., Baxter K.J., Brown B.A., O'Hara A.,
RA Smith B.O., Christie J.M., Jenkins G.I.;
RT "C-terminal region of the UV-B photoreceptor UVR8 initiates signaling
RT through interaction with the COP1 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:16366-16370(2012).
RN [19]
RP SUBUNIT.
RX PubMed=23129206; DOI=10.1104/pp.112.206805;
RA Heilmann M., Jenkins G.I.;
RT "Rapid reversion from monomer to dimer regenerates the ultraviolet-B
RT photoreceptor UV RESISTANCE LOCUS8 in intact Arabidopsis plants.";
RL Plant Physiol. 161:547-555(2013).
RN [20]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28735869; DOI=10.1016/j.bbrc.2017.07.110;
RA Kim S.-H., Kim H., Chung S., Lee J.-H.;
RT "DHU1 negatively regulates UV-B signaling via its direct interaction with
RT COP1 and RUP1.";
RL Biochem. Biophys. Res. Commun. 491:285-290(2017).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 10-381, SUBUNIT, AND MUTAGENESIS
RP OF TRP-233; TRP-285 AND TRP-337.
RX PubMed=22388820; DOI=10.1038/nature10931;
RA Wu D., Hu Q., Yan Z., Chen W., Yan C., Huang X., Zhang J., Yang P.,
RA Deng H., Wang J., Deng X., Shi Y.;
RT "Structural basis of ultraviolet-B perception by UVR8.";
RL Nature 484:214-219(2012).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-405, AND SUBUNIT.
RX PubMed=22323738; DOI=10.1126/science.1218091;
RA Christie J.M., Arvai A.S., Baxter K.J., Heilmann M., Pratt A.J., O'Hara A.,
RA Kelly S.M., Hothorn M., Smith B.O., Hitomi K., Jenkins G.I., Getzoff E.D.;
RT "Plant UVR8 photoreceptor senses UV-B by tryptophan-mediated disruption of
RT cross-dimer salt bridges.";
RL Science 335:1492-1496(2012).
CC -!- FUNCTION: UV-B specific signaling component that acts as UV-B
CC photoreceptor and plays a key role in establishing UV-protective
CC responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate
CC switch from homodimer to monomer, accumulates in the nucleus, interacts
CC with the photomorphogenic repressor COP1 and regulates the expression
CC of the transcription factor HY5 by associating with chromatin (through
CC histone H2B binding) in the HY5 promoter region. UVR8 is involved in
CC controlling aspects of leaf growth and morphogenesis in response to UV-
CC B, is required for normal progression of endocycle and has a regulatory
CC role in stomatal differentiation. Is required for plant circadian clock
CC response to photomorphogenic UV-B light, partly through the
CC transcriptional activation of responsive clock genes. Promotes
CC photosynthetic efficiency at elevated levels of UV-B. Plays a role in
CC mediating the effects of UV-B radiation on pathogen resistance by
CC controlling the expression of the sinapate biosynthetic pathway. The
CC two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B
CC chromophore. {ECO:0000269|PubMed:16330762, ECO:0000269|PubMed:17720867,
CC ECO:0000269|PubMed:18055587, ECO:0000269|PubMed:19165148,
CC ECO:0000269|PubMed:19402876, ECO:0000269|PubMed:21041653,
CC ECO:0000269|PubMed:21395889, ECO:0000269|PubMed:21454788,
CC ECO:0000269|PubMed:22447155, ECO:0000269|PubMed:22988111,
CC ECO:0000269|PubMed:23012433, ECO:0000269|PubMed:23161229}.
CC -!- SUBUNIT: Homodimer in the absence of UV-B, but absorption of UV-B
CC induces monomerization of UVR8 and interaction with COP1. Interacts
CC with RUP1, RUP2 and histone H2B. {ECO:0000269|PubMed:19165148,
CC ECO:0000269|PubMed:20031919, ECO:0000269|PubMed:21041653,
CC ECO:0000269|PubMed:21454788, ECO:0000269|PubMed:22323738,
CC ECO:0000269|PubMed:22388820, ECO:0000269|PubMed:22988111,
CC ECO:0000269|PubMed:23012433, ECO:0000269|PubMed:23129206}.
CC -!- INTERACTION:
CC Q9FN03; P43254: COP1; NbExp=4; IntAct=EBI-2407499, EBI-301649;
CC Q9FN03; Q9FFA7: RUP2; NbExp=3; IntAct=EBI-2407499, EBI-15889073;
CC Q9FN03; Q9FN03: UVR8; NbExp=3; IntAct=EBI-2407499, EBI-2407499;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17720867}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:17720867}. Note=UV-B promotes rapid
CC accumulation of UVR8 in the nucleus. {ECO:0000269|PubMed:17720867}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to ultraviolet-B (UV-B)
CC illumination (PubMed:12226503, PubMed:28735869). Abrogated induction of
CC DHU1 in response to UV-B (PubMed:28735869). Disruption in a plant
CC lacking DHU1 alleviates its hypersensitivity to UV-B (PubMed:28735869).
CC {ECO:0000269|PubMed:12226503, ECO:0000269|PubMed:28735869}.
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DR EMBL; AF130441; AAD43920.1; -; mRNA.
DR EMBL; AB007646; BAB11034.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97805.1; -; Genomic_DNA.
DR EMBL; AY125497; AAM78089.1; -; mRNA.
DR EMBL; BT000600; AAN18169.1; -; mRNA.
DR PIR; T50662; T50662.
DR RefSeq; NP_201191.1; NM_125781.4.
DR PDB; 4D9S; X-ray; 1.70 A; A/B=1-405.
DR PDB; 4DNU; X-ray; 1.76 A; A=10-381.
DR PDB; 4DNV; X-ray; 2.00 A; A/B/C/D=12-381.
DR PDB; 4DNW; X-ray; 1.77 A; A/B=12-385.
DR PDB; 4NAA; X-ray; 1.67 A; A/B/C/D=13-381.
DR PDB; 4NBM; X-ray; 1.61 A; A/B/C/D=13-381.
DR PDB; 4NC4; X-ray; 1.75 A; A/B/C/D=13-381.
DR PDB; 6DD7; X-ray; 2.00 A; A/B/C/D=13-381.
DR PDB; 6QTQ; X-ray; 1.30 A; B=406-413.
DR PDB; 6QTS; X-ray; 1.11 A; B=406-413.
DR PDB; 6XZL; X-ray; 1.39 A; A=12-381.
DR PDB; 6XZM; X-ray; 2.10 A; A/B=12-381.
DR PDB; 6XZN; X-ray; 1.75 A; A/B=12-381.
DR PDBsum; 4D9S; -.
DR PDBsum; 4DNU; -.
DR PDBsum; 4DNV; -.
DR PDBsum; 4DNW; -.
DR PDBsum; 4NAA; -.
DR PDBsum; 4NBM; -.
DR PDBsum; 4NC4; -.
DR PDBsum; 6DD7; -.
DR PDBsum; 6QTQ; -.
DR PDBsum; 6QTS; -.
DR PDBsum; 6XZL; -.
DR PDBsum; 6XZM; -.
DR PDBsum; 6XZN; -.
DR AlphaFoldDB; Q9FN03; -.
DR SMR; Q9FN03; -.
DR BioGRID; 21748; 13.
DR DIP; DIP-59667N; -.
DR IntAct; Q9FN03; 3.
DR MINT; Q9FN03; -.
DR STRING; 3702.AT5G63860.1; -.
DR iPTMnet; Q9FN03; -.
DR PaxDb; Q9FN03; -.
DR PRIDE; Q9FN03; -.
DR ProteomicsDB; 228668; -.
DR EnsemblPlants; AT5G63860.1; AT5G63860.1; AT5G63860.
DR GeneID; 836506; -.
DR Gramene; AT5G63860.1; AT5G63860.1; AT5G63860.
DR KEGG; ath:AT5G63860; -.
DR Araport; AT5G63860; -.
DR TAIR; locus:2163986; AT5G63860.
DR eggNOG; KOG1426; Eukaryota.
DR HOGENOM; CLU_005210_1_1_1; -.
DR InParanoid; Q9FN03; -.
DR OMA; NDRWIPE; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q9FN03; -.
DR PRO; PR:Q9FN03; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN03; baseline and differential.
DR Genevisible; Q9FN03; AT.
DR GO; GO:0000785; C:chromatin; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0009649; P:entrainment of circadian clock; IMP:TAIR.
DR GO; GO:0009411; P:response to UV; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IGI:TAIR.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR032996; UVR8.
DR PANTHER; PTHR22870:SF412; PTHR22870:SF412; 1.
DR Pfam; PF00415; RCC1; 7.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 5.
DR PROSITE; PS50012; RCC1_3; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromophore; Cytoplasm; Nucleus;
KW Photoreceptor protein; Receptor; Reference proteome; Repeat;
KW Sensory transduction.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..440
FT /note="Ultraviolet-B receptor UVR8"
FT /id="PRO_0000421722"
FT REPEAT 2..31
FT /note="RCC1 1"
FT /evidence="ECO:0000255"
FT REPEAT 32..84
FT /note="RCC1 2"
FT /evidence="ECO:0000255"
FT REPEAT 86..137
FT /note="RCC1 3"
FT /evidence="ECO:0000255"
FT REPEAT 139..189
FT /note="RCC1 4"
FT /evidence="ECO:0000255"
FT REPEAT 190..241
FT /note="RCC1 5"
FT /evidence="ECO:0000255"
FT REPEAT 243..293
FT /note="RCC1 6"
FT /evidence="ECO:0000255"
FT REPEAT 294..345
FT /note="RCC1 7"
FT /evidence="ECO:0000255"
FT REPEAT 347..399
FT /note="RCC1 8"
FT /evidence="ECO:0000255"
FT REGION 397..423
FT /note="Required for interaction with COP1"
FT REGION 413..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 39
FT /note="W->A: Loss of function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 39
FT /note="W->F: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 39
FT /note="W->Y: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 92
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 94
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 144
FT /note="W->A: Cannot interact with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 144
FT /note="W->F: No effect on the interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 144
FT /note="W->Y: No effect on the interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 145
FT /note="G->S: In uvr8-15; loss of function and interaction
FT with COP1."
FT /evidence="ECO:0000269|PubMed:21454788"
FT MUTAGEN 196..200
FT /note="Missing: In uvr8-1; loss of function."
FT /evidence="ECO:0000269|PubMed:12226503"
FT MUTAGEN 196
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 198
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 202
FT /note="G->R: In uvr8-9; loss of function and interaction
FT with COP1."
FT /evidence="ECO:0000269|PubMed:21454788"
FT MUTAGEN 233
FT /note="W->A: Reduces response to UV-B."
FT /evidence="ECO:0000269|PubMed:22388820,
FT ECO:0000269|PubMed:23012433"
FT MUTAGEN 250
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 283
FT /note="G->E: In uvr8-5; loss of response to UV-B."
FT /evidence="ECO:0000269|PubMed:22988111"
FT MUTAGEN 285
FT /note="W->A: Loss of function. Constitutive monomer."
FT /evidence="ECO:0000269|PubMed:21454788,
FT ECO:0000269|PubMed:22388820, ECO:0000269|PubMed:23012433"
FT MUTAGEN 285
FT /note="W->F: Loss of function. Constitutive homodimer and
FT no interaction with COP1."
FT /evidence="ECO:0000269|PubMed:21454788,
FT ECO:0000269|PubMed:22388820, ECO:0000269|PubMed:23012433"
FT MUTAGEN 300
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 302
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 337
FT /note="W->A: Reduces response to UV-B."
FT /evidence="ECO:0000269|PubMed:22388820,
FT ECO:0000269|PubMed:23012433"
FT MUTAGEN 352
FT /note="W->A: Cannot interact with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 352
FT /note="W->F: No effect on the interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 352
FT /note="W->Y: No effect on the interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT MUTAGEN 400
FT /note="W->A: No effect on function, homodimerization and
FT interaction with COP1."
FT /evidence="ECO:0000269|PubMed:23012433"
FT CONFLICT 173
FT /note="R -> P (in Ref. 1; AAD43920)"
FT /evidence="ECO:0000305"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:6XZL"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:6XZL"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6DD7"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:6DD7"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:6XZL"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:6XZL"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6XZL"
SQ SEQUENCE 440 AA; 47118 MW; D2EA103CCFC92E98 CRC64;
MAEDMAADEV TAPPRKVLII SAGASHSVAL LSGDIVCSWG RGEDGQLGHG DAEDRPSPTQ
LSALDGHQIV SVTCGADHTV AYSQSGMEVY SWGWGDFGRL GHGNSSDLFT PLPIKALHGI
RIKQIACGDS HCLAVTMEGE VQSWGRNQNG QLGLGDTEDS LVPQKIQAFE GIRIKMVAAG
AEHTAAVTED GDLYGWGWGR YGNLGLGDRT DRLVPERVTS TGGEKMSMVA CGWRHTISVS
YSGALYTYGW SKYGQLGHGD LEDHLIPHKL EALSNSFISQ ISGGWRHTMA LTSDGKLYGW
GWNKFGQVGV GNNLDQCSPV QVRFPDDQKV VQVSCGWRHT LAVTERNNVF AWGRGTNGQL
GIGESVDRNF PKIIEALSVD GASGQHIESS NIDPSSGKSW VSPAERYAVV PDETGLTDGS
SKGNGGDISV PQTDVKRVRI
