CRY2_ARATH
ID CRY2_ARATH Reviewed; 612 AA.
AC Q96524; B0LQ23; B0LQ24; B0LQ25; B0LQ29; Q42549; Q42603; Q42604; Q56ZL8;
AC Q696X6; Q696X8; Q696Z7; Q697A2; Q8VWL9; Q8VZY9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cryptochrome-2 {ECO:0000303|Ref.2};
DE Short=Atcry2 {ECO:0000303|Ref.2};
DE AltName: Full=Blue light photoreceptor {ECO:0000303|PubMed:9003312};
DE AltName: Full=Protein PHR homolog 1 {ECO:0000303|PubMed:9003312};
DE Short=AtPHH1 {ECO:0000303|PubMed:9003312};
DE AltName: Full=Protein SUPPRESSOR OF elf3 20 {ECO:0000303|PubMed:21296763};
GN Name=CRY2 {ECO:0000303|Ref.2};
GN Synonyms=PHH1 {ECO:0000303|PubMed:9003312},
GN SEL20 {ECO:0000303|PubMed:21296763};
GN OrderedLocusNames=At1g04400 {ECO:0000312|Araport:AT1G04400};
GN ORFNames=F19P19.14 {ECO:0000312|EMBL:AAB70435.1};
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9003312; DOI=10.1007/s004380050321;
RA Hoffman P.D., Batschauer A., Hays J.B.;
RT "PHH1, a novel gene from Arabidopsis thaliana that encodes a protein
RT similar to plant blue-light photoreceptors and microbial photolyases.";
RL Mol. Gen. Genet. 253:259-265(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lin C., Ahmad M., Chan J., Cashmore A.R.;
RT "CRY2: a second member of the Arabidopsis cryptochrome gene family.";
RL (er) Plant Gene Register PGR96-001(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=cv. Cvi-0, and cv. Landsberg erecta;
RX PubMed=11726930; DOI=10.1038/ng767;
RA El-Din El-Assal S., Alonso-Blanco C., Peeters A.J.M., Raz V., Koornneef M.;
RT "A QTL for flowering time in Arabidopsis reveals a novel allele of CRY2.";
RL Nat. Genet. 29:435-440(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
RC STRAIN=cv. Bla-10, cv. Bsch-0, cv. Bu-0, cv. Bu-2, cv. Chi-1, cv. Co-1,
RC cv. Columbia, cv. Cvi-0, cv. Da(1)-12, cv. Di-G, cv. El-0, cv. Fe-1,
RC cv. Gr-3, cv. Hn-0, cv. Kon, cv. Kr-0, cv. Landsberg erecta, cv. Le-0,
RC cv. Li-3, cv. Lip-0, cv. Lz-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. Ove-0,
RC cv. PHW-1, cv. PHW-32, cv. PHW-36, cv. Sha, cv. Stw-0, cv. Ta-0, and
RC cv. Wassilewskija-3;
RX PubMed=18273534; DOI=10.1007/s00239-007-9063-3;
RA Moore R.C., Stevens M.H.H.;
RT "Local patterns of nucleotide polymorphism are highly variable in the
RT selfing species Arabidopsis thaliana.";
RL J. Mol. Evol. 66:116-129(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-612.
RC STRAIN=cv. Bla-10, cv. Bsch-0, cv. Bu-0, cv. Bu-2, cv. Chi-1, cv. Co-1,
RC cv. Cvi-0, cv. Da(1)-12, cv. Di-G, cv. El-0, cv. Fe-1, cv. Gr-3, cv. Hn-0,
RC cv. Kon, cv. Kr-0, cv. Landsberg erecta, cv. Le-0, cv. Li-3, cv. Lip-0,
RC cv. Lz-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0, cv. Ove-0, cv. Oy-1, cv. PHW-1,
RC cv. PHW-33, cv. PHW-36, cv. Sha, cv. Stw-0, and cv. Ta-0;
RX PubMed=15280248; DOI=10.1534/genetics.103.024950;
RA Olsen K.M., Halldorsdottir S.S., Stinchcombe J.R., Weinig C., Schmitt J.,
RA Purugganan M.D.;
RT "Linkage disequilibrium mapping of Arabidopsis CRY2 flowering time
RT alleles.";
RL Genetics 167:1361-1369(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-612.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, AND MUTAGENESIS OF GLY-337.
RX PubMed=9565033; DOI=10.1038/33701;
RA Ahmad M., Jarillo J.A., Smirnova O., Cashmore A.R.;
RT "Cryptochrome blue-light photoreceptors of Arabidopsis implicated in
RT phototropism.";
RL Nature 392:720-723(1998).
RN [11]
RP PHOSPHORYLATION.
RX PubMed=9651577; DOI=10.1016/s1097-2765(00)80094-5;
RA Ahmad M., Jarillo J.A., Smirnova O., Cashmore A.R.;
RT "The CRY1 blue light photoreceptor of Arabidopsis interacts with
RT phytochrome A in vitro.";
RL Mol. Cell 1:939-948(1998).
RN [12]
RP FUNCTION.
RX PubMed=9482948; DOI=10.1073/pnas.95.5.2686;
RA Lin C., Yang H., Guo H., Mockler T., Chen J., Cashmore A.R.;
RT "Enhancement of blue-light sensitivity of Arabidopsis seedlings by a blue
RT light receptor cryptochrome 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2686-2690(1998).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=10476076; DOI=10.1046/j.1365-313x.1999.00535.x;
RA Kleiner O., Kircher S., Harter K., Batschauer A.;
RT "Nuclear localization of the Arabidopsis blue light receptor cryptochrome
RT 2.";
RL Plant J. 19:289-296(1999).
RN [14]
RP DOMAINS.
RX PubMed=11114337; DOI=10.1016/s0092-8674(00)00184-7;
RA Yang H.-Q., Wu Y.-J., Tang R.-H., Liu D., Liu Y., Cashmore A.R.;
RT "The C termini of Arabidopsis cryptochromes mediate a constitutive light
RT response.";
RL Cell 103:815-827(2000).
RN [15]
RP INTERACTION WITH PHYB.
RX PubMed=11089975; DOI=10.1038/35041583;
RA Mas P., Devlin P.F., Panda S., Kay S.A.;
RT "Functional interaction of phytochrome B and cryptochrome 2.";
RL Nature 408:207-211(2000).
RN [16]
RP INDUCTION BY CIRCADIAN CLOCK AND LIGHT, AND TISSUE SPECIFICITY.
RX PubMed=11743105; DOI=10.1104/pp.010467;
RA Toth R., Kevei E., Hall A., Millar A.J., Nagy F., Kozma-Bognar L.;
RT "Circadian clock-regulated expression of phytochrome and cryptochrome genes
RT in Arabidopsis.";
RL Plant Physiol. 127:1607-1616(2001).
RN [17]
RP INTERACTION WITH COP1.
RX PubMed=11509693; DOI=10.1126/science.1063630;
RA Wang H., Ma L.-G., Li J.-M., Zhao H.-Y., Deng X.W.;
RT "Direct interaction of Arabidopsis cryptochromes with COP1 in light control
RT development.";
RL Science 294:154-158(2001).
RN [18]
RP PHOSPHORYLATION.
RX PubMed=12066190; DOI=10.1038/nature00815;
RA Shalitin D., Yang H., Mockler T.C., Maymon M., Guo H., Whitelam G.C.,
RA Lin C.;
RT "Regulation of Arabidopsis cryptochrome 2 by blue-light-dependent
RT phosphorylation.";
RL Nature 417:763-767(2002).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12857830; DOI=10.1104/pp.102.018481;
RA Whippo C.W., Hangarter R.P.;
RT "Second positive phototropism results from coordinated co-action of the
RT phototropins and cryptochromes.";
RL Plant Physiol. 132:1499-1507(2003).
RN [20]
RP FUNCTION.
RX PubMed=14605222; DOI=10.1104/pp.103.029819;
RA El-Din El-Assal S., Alonso-Blanco C., Peeters A.J., Wagemaker C.,
RA Weller J.L., Koornneef M.;
RT "The role of cryptochrome 2 in flowering in Arabidopsis.";
RL Plant Physiol. 133:1504-1516(2003).
RN [21]
RP INDUCTION.
RX PubMed=12578985; DOI=10.1073/pnas.0437826100;
RA Mockler T., Yang H., Yu X., Parikh D., Cheng Y.C., Dolan S., Lin C.;
RT "Regulation of photoperiodic flowering by Arabidopsis photoreceptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2140-2145(2003).
RN [22]
RP FUNCTION.
RX PubMed=16093319; DOI=10.1073/pnas.0501011102;
RA Mao J., Zhang Y.C., Sang Y., Li Q.H., Yang H.Q.;
RT "A role for Arabidopsis cryptochromes and COP1 in the regulation of
RT stomatal opening.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12270-12275(2005).
RN [23]
RP PTM, COFACTOR, AND ATP-BINDING.
RX PubMed=17073458; DOI=10.1021/bi061556n;
RA Ozguer S., Sancar A.;
RT "Analysis of autophosphorylating kinase activities of Arabidopsis and human
RT cryptochromes.";
RL Biochemistry 45:13369-13374(2006).
RN [24]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16703358; DOI=10.1007/s00425-006-0280-6;
RA Canamero R.C., Bakrim N., Bouly J.-P., Garay A., Dudkin E.E., Habricot Y.,
RA Ahmad M.;
RT "Cryptochrome photoreceptors cry1 and cry2 antagonistically regulate
RT primary root elongation in Arabidopsis thaliana.";
RL Planta 224:995-1003(2006).
RN [25]
RP COFACTOR.
RX PubMed=17355959; DOI=10.1074/jbc.m700616200;
RA Banerjee R., Schleicher E., Meier S., Viana R.M., Pokorny R., Ahmad M.,
RA Bittl R., Batschauer A.;
RT "The signaling state of Arabidopsis cryptochrome 2 contains flavin
RT semiquinone.";
RL J. Biol. Chem. 282:14916-14922(2007).
RN [26]
RP FUNCTION.
RX PubMed=17470059; DOI=10.1111/j.1365-313x.2007.03093.x;
RA Tessadori F., Schulkes R.K., van Driel R., Fransz P.;
RT "Light-regulated large-scale reorganization of chromatin during the floral
RT transition in Arabidopsis.";
RL Plant J. 50:848-857(2007).
RN [27]
RP SUBCELLULAR LOCATION, SUBUNIT, AND PHOSPHORYLATION.
RX PubMed=17438275; DOI=10.1073/pnas.0701912104;
RA Yu X., Shalitin D., Liu X., Maymon M., Klejnot J., Yang H., Lopez J.,
RA Zhao X., Bendehakkalu K.T., Lin C.;
RT "Derepression of the NC80 motif is critical for the photoactivation of
RT Arabidopsis CRY2.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7289-7294(2007).
RN [28]
RP SUBCELLULAR LOCATION, UBIQUITINATION, AND PHOSPHORYLATION.
RX PubMed=17965271; DOI=10.1105/tpc.107.053017;
RA Yu X., Klejnot J., Zhao X., Shalitin D., Maymon M., Yang H., Lee J.,
RA Liu X., Lopez J., Lin C.;
RT "Arabidopsis cryptochrome 2 completes its posttranslational life cycle in
RT the nucleus.";
RL Plant Cell 19:3146-3156(2007).
RN [29]
RP FUNCTION.
RX PubMed=17259260; DOI=10.1105/tpc.106.048157;
RA Endo M., Mochizuki N., Suzuki T., Nagatani A.;
RT "CRYPTOCHROME2 in vascular bundles regulates flowering in Arabidopsis.";
RL Plant Cell 19:84-93(2007).
RN [30]
RP INTERACTION WITH BHLH63/CIB1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-387.
RX PubMed=18988809; DOI=10.1126/science.1163927;
RA Liu H., Yu X., Li K., Klejnot J., Yang H., Lisiero D., Lin C.;
RT "Photoexcited CRY2 interacts with CIB1 to regulate transcription and floral
RT initiation in Arabidopsis.";
RL Science 322:1535-1539(2008).
RN [31]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19558423; DOI=10.1111/j.1469-8137.2009.02921.x;
RA Millenaar F.F., van Zanten M., Cox M.C., Pierik R., Voesenek L.A.,
RA Peeters A.J.;
RT "Differential petiole growth in Arabidopsis thaliana: photocontrol and
RT hormonal regulation.";
RL New Phytol. 184:141-152(2009).
RN [32]
RP REVIEW ON CRYPTOCHROMES.
RX PubMed=21841916; DOI=10.1199/tab.0135;
RA Yu X., Liu H., Klejnot J., Lin C.;
RT "The cryptochrome blue light receptors.";
RL Arabidopsis Book 8:E0135-E0135(2010).
RN [33]
RP REVIEW ON PHOTORECEPTORS.
RX PubMed=20705178; DOI=10.1016/s0070-2153(10)91002-8;
RA Kami C., Lorrain S., Hornitschek P., Fankhauser C.;
RT "Light-regulated plant growth and development.";
RL Curr. Top. Dev. Biol. 91:29-66(2010).
RN [34]
RP BIOTECHNOLOGY.
RX PubMed=21037589; DOI=10.1038/nmeth.1524;
RA Kennedy M.J., Hughes R.M., Peteya L.A., Schwartz J.W., Ehlers M.D.,
RA Tucker C.L.;
RT "Rapid blue-light-mediated induction of protein interactions in living
RT cells.";
RL Nat. Methods 7:973-975(2010).
RN [35]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY LOW LIGHT.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=20935177; DOI=10.1104/pp.110.164616;
RA van Zanten M., Tessadori F., McLoughlin F., Smith R., Millenaar F.F.,
RA van Driel R., Voesenek L.A.C.J., Peeters A.J.M., Fransz P.;
RT "Photoreceptors CRYTOCHROME2 and phytochrome B control chromatin compaction
RT in Arabidopsis.";
RL Plant Physiol. 154:1686-1696(2010).
RN [36]
RP FUNCTION, DISRUPTION PHENOTYPE, REGULATION BY BLUE-LIGHT AND DARKNESS,
RP INTERACTION WITH COP1, AND SUBCELLULAR LOCATION.
RX PubMed=20624951; DOI=10.1073/pnas.1004529107;
RA Jeong R.-D., Chandra-Shekara A.C., Barman S.R., Navarre D., Klessig D.F.,
RA Kachroo A., Kachroo P.;
RT "Cryptochrome 2 and phototropin 2 regulate resistance protein-mediated
RT viral defense by negatively regulating an E3 ubiquitin ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13538-13543(2010).
RN [37]
RP FUNCTION, INTERACTION WITH SPA1, AND MUTAGENESIS OF ASP-387.
RX PubMed=21514160; DOI=10.1016/j.cub.2011.03.048;
RA Zuo Z., Liu H., Liu B., Liu X., Lin C.;
RT "Blue light-dependent interaction of CRY2 with SPA1 regulates COP1 activity
RT and floral initiation in Arabidopsis.";
RL Curr. Biol. 21:841-847(2011).
RN [38]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP SPA1.
RC STRAIN=cv. Columbia;
RX PubMed=21511872; DOI=10.1101/gad.2025111;
RA Lian H.-L., He S.-B., Zhang Y.-C., Zhu D.-M., Zhang J.-Y., Jia K.-P.,
RA Sun S.-X., Li L., Yang H.-Q.;
RT "Blue-light-dependent interaction of cryptochrome 1 with SPA1 defines a
RT dynamic signaling mechanism.";
RL Genes Dev. 25:1023-1028(2011).
RN [39]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21296763; DOI=10.1093/jxb/erq450;
RA Nefissi R., Natsui Y., Miyata K., Oda A., Hase Y., Nakagawa M., Ghorbel A.,
RA Mizoguchi T.;
RT "Double loss-of-function mutation in EARLY FLOWERING 3 and CRYPTOCHROME 2
RT genes delays flowering under continuous light but accelerates it under long
RT days and short days: an important role for Arabidopsis CRY2 to accelerate
RT flowering time in continuous light.";
RL J. Exp. Bot. 62:2731-2744(2011).
RN [40]
RP MUTAGENESIS OF TRP-321; TRP-374 AND TRP-397, AND INTERACTION WITH SPA1 AND
RP BHLH63/CIB1.
RC STRAIN=cv. Columbia;
RX PubMed=22139370; DOI=10.1073/pnas.1114579108;
RA Li X., Wang Q., Yu X., Liu H., Yang H., Zhao C., Liu X., Tan C.,
RA Klejnot J., Zhong D., Lin C.;
RT "Arabidopsis cryptochrome 2 (CRY2) functions by the photoactivation
RT mechanism distinct from the tryptophan (trp) triad-dependent
RT photoreduction.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20844-20849(2011).
RN [41]
RP MUTAGENESIS OF GLY-377.
RX PubMed=21765176; DOI=10.1093/mp/ssr052;
RA Gu N.-N., Zhang Y.-C., Yang H.-Q.;
RT "Substitution of a conserved glycine in the PHR domain of Arabidopsis
RT cryptochrome 1 confers a constitutive light response.";
RL Mol. Plant 5:85-97(2012).
RN [42]
RP SUBCELLULAR LOCATION, REGULATION BY BLUE LIGHT, AND MUTAGENESIS OF LYS-541
RP AND 554-LYS-LYS-555.
RC STRAIN=cv. Columbia;
RX PubMed=22311776; DOI=10.1093/mp/sss007;
RA Zuo Z.-C., Meng Y.-Y., Yu X.-H., Zhang Z.-L., Feng D.-S., Sun S.-F.,
RA Liu B., Lin C.-T.;
RT "A study of the blue-light-dependent phosphorylation, degradation, and
RT photobody formation of Arabidopsis CRY2.";
RL Mol. Plant 5:726-733(2012).
RN [43]
RP INTERACTION WITH SPA1, AND SUBCELLULAR LOCATION.
RX PubMed=22739826; DOI=10.1105/tpc.112.098210;
RA Weidler G., Zur Oven-Krockhaus S., Heunemann M., Orth C., Schleifenbaum F.,
RA Harter K., Hoecker U., Batschauer A.;
RT "Degradation of Arabidopsis CRY2 is regulated by SPA proteins and
RT phytochrome A.";
RL Plant Cell 24:2610-2623(2012).
RN [44]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=22147516; DOI=10.1104/pp.111.187237;
RA Boccalandro H.E., Giordano C.V., Ploschuk E.L., Piccoli P.N., Bottini R.,
RA Casal J.J.;
RT "Phototropins but not cryptochromes mediate the blue light-specific
RT promotion of stomatal conductance, while both enhance photosynthesis and
RT transpiration under full sunlight.";
RL Plant Physiol. 158:1475-1484(2012).
RN [45]
RP BIOTECHNOLOGY.
RX PubMed=22847441; DOI=10.1073/pnas.1211305109;
RA Idevall-Hagren O., Dickson E.J., Hille B., Toomre D.K., De Camilli P.;
RT "Optogenetic control of phosphoinositide metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2316-E2323(2012).
RN [46]
RP SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=23833191; DOI=10.1074/jbc.m113.493361;
RA Ozkan-Dagliyan I., Chiou Y.-Y., Ye R., Hassan B.H., Ozturk N., Sancar A.;
RT "Formation of Arabidopsis Cryptochrome 2 photobodies in mammalian nuclei:
RT application as an optogenetic DNA damage checkpoint switch.";
RL J. Biol. Chem. 288:23244-23251(2013).
RN [47]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY TEMPERATURE.
RC STRAIN=cv. Columbia;
RX PubMed=23511208; DOI=10.1038/msb.2013.7;
RA Gould P.D., Ugarte N., Domijan M., Costa M., Foreman J., Macgregor D.,
RA Rose K., Griffiths J., Millar A.J., Finkenstaedt B., Penfield S.,
RA Rand D.A., Halliday K.J., Hall A.J.W.;
RT "Network balance via CRY signalling controls the Arabidopsis circadian
RT clock over ambient temperatures.";
RL Mol. Syst. Biol. 9:650-650(2013).
RN [48]
RP PHOSPHORYLATION AT SER-587 AND THR-603 BY CK1.3 AND CK1.4, AND MUTAGENESIS
RP OF SER-587 AND THR-603.
RX PubMed=23897926; DOI=10.1105/tpc.113.114322;
RA Tan S.-T., Dai C., Liu H.-T., Xue H.-W.;
RT "Arabidopsis casein kinase1 proteins CK1.3 and CK1.4 phosphorylate
RT cryptochrome2 to regulate blue light signaling.";
RL Plant Cell 25:2618-2632(2013).
RN [49]
RP FUNCTION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=23398192; DOI=10.1111/tpj.12144;
RA Herbel V., Orth C., Wenzel R., Ahmad M., Bittl R., Batschauer A.;
RT "Lifetimes of Arabidopsis cryptochrome signaling states in vivo.";
RL Plant J. 74:583-592(2013).
RN [50]
RP FUNCTION, AND INTERACTION WITH BHLH63/CIB1; BHLH78/CIB2; BHLH74/CIB4 AND
RP BHLH76/CIB5.
RC STRAIN=cv. Columbia;
RX PubMed=24130508; DOI=10.1371/journal.pgen.1003861;
RA Liu Y., Li X., Li K., Liu H., Lin C.;
RT "Multiple bHLH proteins form heterodimers to mediate CRY2-dependent
RT regulation of flowering-time in Arabidopsis.";
RL PLoS Genet. 9:E1003861-E1003861(2013).
RN [51]
RP INTERACTION WITH BHLH63/CIB1.
RX PubMed=24780222; DOI=10.1016/j.ab.2014.04.023;
RA Cui Y., Choudhury S.R., Irudayaraj J.;
RT "Quantitative real-time kinetics of optogenetic proteins CRY2 and CIB1/N
RT using single-molecule tools.";
RL Anal. Biochem. 458:58-60(2014).
RN [52]
RP BIOTECHNOLOGY.
RX PubMed=24718798; DOI=10.1007/978-1-4939-0470-9_8;
RA Idevall-Hagren O., Decamilli P.;
RT "Manipulation of plasma membrane phosphoinositides using photoinduced
RT protein-protein interactions.";
RL Methods Mol. Biol. 1148:109-128(2014).
RN [53]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24126495; DOI=10.1093/mp/sst093;
RA Jia K.-P., Luo Q., He S.-B., Lu X.-D., Yang H.-Q.;
RT "Strigolactone-regulated hypocotyl elongation is dependent on cryptochrome
RT and phytochrome signaling pathways in Arabidopsis.";
RL Mol. Plant 7:528-540(2014).
RN [54]
RP FUNCTION, COFACTOR, AND MUTAGENESIS OF TRP-321; TRP-331; TRP-374; TRP-376;
RP TRP-397 AND TYR-399.
RX PubMed=25428980; DOI=10.1105/tpc.114.129809;
RA Engelhard C., Wang X., Robles D., Moldt J., Essen L.-O., Batschauer A.,
RA Bittl R., Ahmad M.;
RT "Cellular metabolites enhance the light sensitivity of Arabidopsis
RT cryptochrome through alternate electron transfer pathways.";
RL Plant Cell 26:4519-4531(2014).
RN [55]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26095447; DOI=10.1002/bem.21927;
RA Xu C., Li Y., Yu Y., Zhang Y., Wei S.;
RT "Suppression of Arabidopsis flowering by near-null magnetic field is
RT affected by light.";
RL Bioelectromagnetics 36:476-479(2015).
RN [56]
RP BIOTECHNOLOGY.
RX PubMed=25963241; DOI=10.1016/j.chembiol.2015.04.014;
RA Duan L., Che D., Zhang K., Ong Q., Guo S., Cui B.;
RT "Optogenetic control of molecular motors and organelle distributions in
RT cells.";
RL Chem. Biol. 22:671-682(2015).
RN [57]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-598; SER-599 AND SER-605,
RP MUTAGENESIS OF 570-SER--SER-575; SER-580; SER-582; SER-584; SER-587;
RP 598-SER-SER-599 AND SER-605, IDENTIFICATION BY MASS SPECTROMETRY,
RP UBIQUITINATION, AND REGULATION BY BLUE LIGHT.
RX PubMed=25792146; DOI=10.1016/j.molp.2015.03.005;
RA Wang Q., Barshop W.D., Bian M., Vashisht A.A., He R., Yu X., Liu B.,
RA Nguyen P., Liu X., Zhao X., Wohlschlegel J.A., Lin C.;
RT "The blue light-dependent phosphorylation of the CCE domain determines the
RT photosensitivity of Arabidopsis CRY2.";
RL Mol. Plant 8:631-643(2015).
RN [58]
RP DOMAINS.
RX PubMed=25721730; DOI=10.1016/j.molp.2015.02.008;
RA He S.B., Wang W.X., Zhang J.Y., Xu F., Lian H.L., Li L., Yang H.Q.;
RT "The CNT1 domain of Arabidopsis CRY1 Alone is sufficient to mediate blue
RT light inhibition of hypocotyl elongation.";
RL Mol. Plant 8:822-825(2015).
RN [59]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26179959; DOI=10.1080/15592324.2015.1042647;
RA Jourdan N., Martino C.F., El-Esawi M., Witczak J., Bouchet P.-E.,
RA d'Harlingue A., Ahmad M.;
RT "Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may
RT contribute toward its signaling role.";
RL Plant Signal. Behav. 10:E1042647-E1042647(2015).
RN [60]
RP FUNCTION, INDUCTION BY LOW BLUE LIGHT, INTERACTION WITH PIF4 AND PIF5, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26724867; DOI=10.1016/j.cell.2015.12.018;
RA Pedmale U.V., Huang S.S., Zander M., Cole B.J., Hetzel J., Ljung K.,
RA Reis P.A., Sridevi P., Nito K., Nery J.R., Ecker J.R., Chory J.;
RT "Cryptochromes interact directly with PIFs to control plant growth in
RT limiting blue light.";
RL Cell 164:233-245(2016).
RN [61]
RP INTERACTION WITH BIC1, AND SUBUNIT.
RX PubMed=27846570; DOI=10.1126/science.aaf9030;
RA Wang Q., Zuo Z., Wang X., Gu L., Yoshizumi T., Yang Z., Yang L., Liu Q.,
RA Liu W., Han Y.J., Kim J.I., Liu B., Wohlschlegel J.A., Matsui M., Oka Y.,
RA Lin C.;
RT "Photoactivation and inactivation of Arabidopsis cryptochrome 2.";
RL Science 354:343-347(2016).
RN [62]
RP INTERACTION WITH NRP.
RX PubMed=28633330; DOI=10.1093/jxb/erx192;
RA Zhou R., Zhu T., Han L., Liu M., Xu M., Liu Y., Han D., Qiu D., Gong Q.,
RA Liu X.;
RT "The asparagine-rich protein NRP interacts with the Verticillium effector
RT PevD1 and regulates the subcellular localization of cryptochrome 2.";
RL J. Exp. Bot. 68:3427-3440(2017).
RN [63]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS)IN COMPLEX WITH FAD AND ATP.
RX PubMed=32398826; DOI=10.1038/s41594-020-0410-z;
RA Ma L., Wang X., Guan Z., Wang L., Wang Y., Zheng L., Gong Z., Shen C.,
RA Wang J., Zhang D., Liu Z., Yin P.;
RT "Structural insights into BIC-mediated inactivation of Arabidopsis
RT cryptochrome 2.";
RL Nat. Struct. Mol. Biol. 27:472-479(2020).
CC -!- FUNCTION: Photoreceptor that mediates primarily blue light inhibition
CC of hypocotyl elongation and photoperiodic control of floral initiation,
CC and regulates other light responses, including circadian rhythms,
CC tropic growth, stomata opening, guard cell development, root
CC development, bacterial and viral pathogen responses, abiotic stress
CC responses, cell cycles, programmed cell death, apical dominance, fruit
CC and ovule development, seed dormancy, and magnetoreception.
CC Photoexcited cryptochromes interact with signaling partner proteins to
CC alter gene expression at both transcriptional and post-translational
CC levels and, consequently, regulate the corresponding metabolic and
CC developmental programs (PubMed:21841916). Blue-light absorbing
CC flavoprotein that activates reversible flavin photoreduction via an
CC electron transport chain comprising a tryptophan triad (W-321, W-374
CC and W-397), or via an alternative electron transport that involves
CC small metabolites, including NADPH, NADH, and ATP. The half-life of the
CC activated signaling state is about 16 minutes (PubMed:25428980,
CC PubMed:23398192). Perceives low blue light (LBL) and responds by
CC directly contacting two bHLH transcription factors, PIF4 and PIF5, at
CC chromatin on E-box variant 5'-CA[CT]GTG-3' to promote their activity
CC and stimulate specific gene expression to adapt global physiology (e.g.
CC hypocotyl elongation and hyponastic growth in low blue light)
CC (PubMed:26724867, PubMed:19558423). In response to blue light, binds to
CC CIB proteins (e.g. BHLH63/CIB1 and BHLH76/CIB5) to activates
CC transcription and floral initiation (PubMed:24130508). Mediates blue
CC light-induced gene expression, floral initiation and hypocotyl
CC elongation through the interaction with SPA1 that prevents formation of
CC SPA1/COP1 complex but stimulates COP1 binding, and thus inhibits COP1-
CC mediated degradation of transcription factors (e.g. CO and HY5)
CC (PubMed:21514160, PubMed:21511872, PubMed:16093319). Promotes flowering
CC time in continuous light (LL) (PubMed:21296763). Involved in shortening
CC the circadian clock period, especially at 27 degrees Celsius, in blue
CC light (BL). Required to maintain clock genes expression rhythm
CC (PubMed:23511208). Triggers nuclear accumulation of ROS in response to
CC blue light illumination (PubMed:26179959). Involved in blue light-
CC dependent stomatal opening, transpiration and inhibition of stem and
CC root growth, probably by regulating abscisic acid (ABA)
CC (PubMed:22147516, PubMed:16093319, PubMed:16703358, PubMed:9482948,
CC PubMed:9565033). Regulates the timing of flowering by promoting the
CC expression of 'FLOWERING LOCUS T' (FT) in vascular bundles. Negatively
CC regulated by 'FLOWERING LOCUS C' (FLC) (PubMed:14605222,
CC PubMed:17259260). General positive regulator of reversible low light-
CC induced chromatin decompaction (PubMed:20935177). Involved in
CC triggering chromatin decondensation during floral transition
CC (PubMed:17470059). Together with phototropins, involved in phototropism
CC regulation by various blue light fluence; blue light attenuates
CC phototropism in high fluence rates (100 umol.m-2.s-1) but enhances
CC phototropism in low fluence rates (<1.0 umol.m-2.s-1)
CC (PubMed:12857830). The effect of near-null magnetic field on flowering
CC is altered by changes of blue light cycle and intensity in a CRY1/CRY2-
CC dependent manner (PubMed:26095447). Involved in the strigolactone
CC signaling that regulates hypocotyl growth in response to blue light
CC (PubMed:24126495). {ECO:0000269|PubMed:12857830,
CC ECO:0000269|PubMed:14605222, ECO:0000269|PubMed:16093319,
CC ECO:0000269|PubMed:16703358, ECO:0000269|PubMed:17259260,
CC ECO:0000269|PubMed:17470059, ECO:0000269|PubMed:19558423,
CC ECO:0000269|PubMed:20935177, ECO:0000269|PubMed:21296763,
CC ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:21514160,
CC ECO:0000269|PubMed:22147516, ECO:0000269|PubMed:23398192,
CC ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:24126495,
CC ECO:0000269|PubMed:24130508, ECO:0000269|PubMed:25428980,
CC ECO:0000269|PubMed:26095447, ECO:0000269|PubMed:26179959,
CC ECO:0000269|PubMed:26724867, ECO:0000269|PubMed:9482948,
CC ECO:0000269|PubMed:9565033, ECO:0000303|PubMed:21841916}.
CC -!- FUNCTION: Confers resistance to turnip crinkle virus (TCV) by
CC preventing COP1-mediated proteasome-mediated degradation of RPP8/HRT,
CC thus promoting its stability in light. Exposure to darkness or blue-
CC light induces degradation of CRY2, and in turn of RPP8/HRT, resulting
CC in susceptibility to TCV. {ECO:0000269|PubMed:20624951}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17073458, ECO:0000269|PubMed:17355959};
CC Note=Binds 1 FAD per subunit. The flavin in the dark is in the oxidized
CC (bright yellow) redox state, whereas it becomes reduced subsequent to
CC light activation and formation of the neutral radical (pale yellow).
CC {ECO:0000269|PubMed:17073458, ECO:0000269|PubMed:17355959,
CC ECO:0000269|PubMed:25428980};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Homodimer (PubMed:11089975, PubMed:11509693, PubMed:17438275,
CC PubMed:27846570). Blue-light dependent dimerization (PubMed:27846570).
CC Interacts with COP1 and PHYB in the nucleus (PubMed:11089975,
CC PubMed:11509693, PubMed:17438275, PubMed:20624951). Binds reversibly to
CC CIBs proteins such as BHLH63/CIB1, BHLH78/CIB2, BHLH74/CIB4 and
CC BHLH76/CIB5 after blue light illumination to stimulate their
CC transcription factor activities (PubMed:18988809, PubMed:22139370,
CC PubMed:24130508, PubMed:24780222). Interacts with PIF4 and PIF5 in the
CC nucleus in response to low blue light (LBL) (PubMed:26724867). Binds to
CC SPA1 in response to blue light, this interaction prevents SPA1/COP1
CC complex formation but stimulates interaction with COP1, and thus avoid
CC COP1-dependent degradation of the transcription factors CO and HY5 by
CC the proteasome and promotes hypocotyl elongation and floral initiation
CC (PubMed:21514160, PubMed:22139370, PubMed:21511872, PubMed:22739826).
CC Binding to ATP mediates conformational changes which facilitate flavin
CC binding (PubMed:17073458). Interacts with BIC1 in both darkness and
CC light (PubMed:27846570, PubMed:11089975, PubMed:11509693,
CC PubMed:17073458, PubMed:17438275, PubMed:18988809, PubMed:20624951,
CC PubMed:21511872, PubMed:21514160, PubMed:22139370, PubMed:22739826,
CC PubMed:24130508, PubMed:24780222, PubMed:26724867). Interacts with NRP
CC (PubMed:28633330). {ECO:0000269|PubMed:11089975,
CC ECO:0000269|PubMed:11509693, ECO:0000269|PubMed:17073458,
CC ECO:0000269|PubMed:17438275, ECO:0000269|PubMed:18988809,
CC ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:21511872,
CC ECO:0000269|PubMed:21514160, ECO:0000269|PubMed:22139370,
CC ECO:0000269|PubMed:22739826, ECO:0000269|PubMed:24130508,
CC ECO:0000269|PubMed:24780222, ECO:0000269|PubMed:26724867,
CC ECO:0000269|PubMed:27846570, ECO:0000269|PubMed:28633330}.
CC -!- INTERACTION:
CC Q96524; Q8GY61: BHLH63; NbExp=3; IntAct=EBI-531555, EBI-4469930;
CC Q96524; P43254: COP1; NbExp=3; IntAct=EBI-531555, EBI-301649;
CC Q96524; Q96524: CRY2; NbExp=4; IntAct=EBI-531555, EBI-531555;
CC Q96524; P14713: PHYB; NbExp=3; IntAct=EBI-531555, EBI-300727;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:10476076, ECO:0000269|PubMed:17438275,
CC ECO:0000269|PubMed:17965271, ECO:0000269|PubMed:18988809,
CC ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:22311776,
CC ECO:0000269|PubMed:22739826, ECO:0000269|PubMed:25792146,
CC ECO:0000269|PubMed:26179959, ECO:0000269|PubMed:26724867}. Nucleus, PML
CC body {ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:23833191}.
CC Cytoplasm {ECO:0000269|PubMed:26179959}. Note=Present in nuclear bodies
CC (NBs) in blue light (e.g. photobodies) (PubMed:21511872,
CC PubMed:23833191, PubMed:22311776). Translocates from the cytosol to the
CC nucleus in response to blue light illumination (PubMed:26179959).
CC {ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:22311776,
CC ECO:0000269|PubMed:23833191, ECO:0000269|PubMed:26179959}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in the shoot meristems and root
CC tips, and, to a lower extent, in the cotyledons, hypocotyls, and roots.
CC {ECO:0000269|PubMed:11743105}.
CC -!- INDUCTION: Daily oscillation of protein abundance in plants grown in
CC short days (SD) but not in long days (LD) (PubMed:12578985). Expression
CC levels display circadian oscillations under constant conditions, with a
CC low amplitude and a late phase, with maximal expression around the end
CC of the light phase. Repressed by light (PubMed:11743105). In response
CC to blue light and darkness, phosphorylated, ubiquitinated, and
CC subsequently degraded (at protein level) in a SPA proteins-dependent
CC manner (PubMed:20624951, PubMed:25792146, PubMed:22739826,
CC PubMed:22311776). Transcripts levels oscillate weakly and
CC proportionally to temperature, but protein levels are stable
CC (PubMed:23511208). Accumulates in response to low blue light (LBL) and
CC in low light (PubMed:26724867, PubMed:20935177).
CC {ECO:0000269|PubMed:11743105, ECO:0000269|PubMed:12578985,
CC ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:20935177,
CC ECO:0000269|PubMed:22311776, ECO:0000269|PubMed:22739826,
CC ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:25792146,
CC ECO:0000269|PubMed:26724867}.
CC -!- DOMAIN: The NC80 domain (486-565) contains a major active site
CC responsible for the signal transduction processes regulating both
CC hypocotyl inhibition and floral promotion. The C-terminal tail (564-
CC 612) is not required for physiological activity of the protein.
CC -!- PTM: Phosphorylated by CK1.3 and CK1.4; in response to blue light.
CC Required for degradation (PubMed:12066190, PubMed:17438275,
CC PubMed:17965271, PubMed:9651577, PubMed:25792146, PubMed:23897926).
CC Adopts an open conformation when phosphorylated upon photoexcitation
CC and thus interacts with signaling partner proteins (PubMed:21841916).
CC Not autophosphorylated, even in complex with FAD cofactor
CC (PubMed:17073458). {ECO:0000269|PubMed:12066190,
CC ECO:0000269|PubMed:17073458, ECO:0000269|PubMed:17438275,
CC ECO:0000269|PubMed:17965271, ECO:0000269|PubMed:23897926,
CC ECO:0000269|PubMed:25792146, ECO:0000269|PubMed:9651577,
CC ECO:0000303|PubMed:21841916}.
CC -!- PTM: Ubiquitinated; in response to blue light.
CC {ECO:0000269|PubMed:17965271, ECO:0000269|PubMed:25792146}.
CC -!- DISRUPTION PHENOTYPE: Plants show increased root elongation in blue
CC light (PubMed:16703358, PubMed:21511872). Reduced attenuating effect of
CC high fluence rates of blue light in the cry1 cry2 double mutant. Slow
CC rate of curvature at low fluence rates of blue light in cry1 cry2
CC (PubMed:12857830). The double mutant cry1 cry2 exhibits a reduced
CC impact of near-null magnetic field on flowering in lower blue light
CC intensity and short days (PubMed:26095447). Little detectable phenotype
CC on circadian clock in blue light (BL). The double mutant cry1 cry2 is
CC impaired in blue light signaling, resulting in long-period, lower-
CC amplitude oscillations at 12 and 17 degrees Celsius and completely
CC abolishing rhythms at 27 degrees Celsius (PubMed:23511208). Reduced
CC hyponastic growth (differential growth-driven upward leaf movement) in
CC low blue light fluence (PubMed:19558423). The double mutant cry1 cry2
CC is hyposensitive to the strigolactone analog GR24 (PubMed:24126495).
CC The mutant cry2 exposed to a background of red light show severely
CC impaired stomatal opening responses to blue light. The double mutant
CC cry1 cry2 has reduced stomatal conductance, transpiration, and
CC photosynthesis, particularly under the high irradiance of full sunlight
CC at midday, associated with elevated abscisic acid levels
CC (PubMed:22147516). Mutation sel20 suppresses the inhibitory effect of
CC continuous light (LL) on the hypocotyl elongation of elf3-1. The double
CC mutant elf3 sel20 exhibits a late-flowering phenotype
CC (PubMed:21296763). Impaired chromatin decondensation during the floral
CC transition and in low light conditions (PubMed:20935177). Increased
CC sensitivity to turnip crinkle virus (TCV) and associated with reduced
CC HRT levels and stability, and characterized by hypersensitive response
CC (HR) symptoms (PubMed:20624951). {ECO:0000269|PubMed:12857830,
CC ECO:0000269|PubMed:16703358, ECO:0000269|PubMed:19558423,
CC ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:20935177,
CC ECO:0000269|PubMed:21296763, ECO:0000269|PubMed:21511872,
CC ECO:0000269|PubMed:22147516, ECO:0000269|PubMed:23511208,
CC ECO:0000269|PubMed:24126495, ECO:0000269|PubMed:26095447}.
CC -!- BIOTECHNOLOGY: The rapid blue light-mediated reversible interaction
CC between CRY2 and BHLH63/CIB1 is used to design an optogenetic control
CC of target proteins or organelles. {ECO:0000269|PubMed:21037589,
CC ECO:0000269|PubMed:22847441, ECO:0000269|PubMed:23833191,
CC ECO:0000269|PubMed:24718798, ECO:0000269|PubMed:25963241}.
CC -!- MISCELLANEOUS: Phosphorylation of the C-terminal tail and resulting
CC derepression of NC80 domain may both depend on homodimerization.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a DNA photolyase.
CC {ECO:0000305|PubMed:9003312}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT80593.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80594.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80595.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80596.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80597.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80598.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80600.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80601.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80602.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80603.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80604.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80606.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80607.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80608.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80609.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80610.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80611.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80612.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80613.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80614.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80615.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80616.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80617.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80618.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80620.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80621.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80622.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAT80623.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD94467.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U62549; AAB04996.1; -; mRNA.
DR EMBL; U62550; AAB04997.1; -; mRNA.
DR EMBL; X99061; CAA67508.1; -; Genomic_DNA.
DR EMBL; U43397; AAD09837.1; -; mRNA.
DR EMBL; AY057440; AAL16377.1; -; mRNA.
DR EMBL; AY057441; AAL16378.1; -; Genomic_DNA.
DR EMBL; AY057442; AAL16379.1; -; Genomic_DNA.
DR EMBL; EU351967; ABY77601.1; -; Genomic_DNA.
DR EMBL; EU351968; ABY77602.1; -; Genomic_DNA.
DR EMBL; EU351969; ABY77603.1; -; Genomic_DNA.
DR EMBL; EU351970; ABY77604.1; -; Genomic_DNA.
DR EMBL; EU351971; ABY77605.1; -; Genomic_DNA.
DR EMBL; EU351972; ABY77606.1; -; Genomic_DNA.
DR EMBL; EU351973; ABY77607.1; -; Genomic_DNA.
DR EMBL; EU351974; ABY77608.1; -; Genomic_DNA.
DR EMBL; EU351975; ABY77609.1; -; Genomic_DNA.
DR EMBL; EU351976; ABY77610.1; -; Genomic_DNA.
DR EMBL; EU351977; ABY77611.1; -; Genomic_DNA.
DR EMBL; EU351978; ABY77612.1; -; Genomic_DNA.
DR EMBL; EU351979; ABY77613.1; -; Genomic_DNA.
DR EMBL; EU351980; ABY77614.1; -; Genomic_DNA.
DR EMBL; EU351981; ABY77615.1; -; Genomic_DNA.
DR EMBL; EU351982; ABY77616.1; -; Genomic_DNA.
DR EMBL; EU351983; ABY77617.1; -; Genomic_DNA.
DR EMBL; EU351984; ABY77618.1; -; Genomic_DNA.
DR EMBL; EU351985; ABY77619.1; -; Genomic_DNA.
DR EMBL; EU351986; ABY77620.1; -; Genomic_DNA.
DR EMBL; EU351987; ABY77621.1; -; Genomic_DNA.
DR EMBL; EU351988; ABY77622.1; -; Genomic_DNA.
DR EMBL; EU351989; ABY77623.1; -; Genomic_DNA.
DR EMBL; EU351990; ABY77624.1; -; Genomic_DNA.
DR EMBL; EU351991; ABY77625.1; -; Genomic_DNA.
DR EMBL; EU351993; ABY77627.1; -; Genomic_DNA.
DR EMBL; EU351992; ABY77626.1; -; Genomic_DNA.
DR EMBL; EU351994; ABY77628.1; -; Genomic_DNA.
DR EMBL; EU351995; ABY77629.1; -; Genomic_DNA.
DR EMBL; EU351996; ABY77630.1; -; Genomic_DNA.
DR EMBL; EU351997; ABY77631.1; -; Genomic_DNA.
DR EMBL; EU351998; ABY77632.1; -; Genomic_DNA.
DR EMBL; AC000104; AAB70435.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27692.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27693.1; -; Genomic_DNA.
DR EMBL; BT008576; AAP40403.1; -; mRNA.
DR EMBL; BT008648; AAP40463.1; -; mRNA.
DR EMBL; AY576241; AAT80593.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576242; AAT80594.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576243; AAT80595.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576244; AAT80596.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576245; AAT80597.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576246; AAT80598.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576247; AAT80599.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576248; AAT80600.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576249; AAT80601.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576250; AAT80602.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576251; AAT80603.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576252; AAT80604.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576253; AAT80605.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576254; AAT80606.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576255; AAT80607.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576256; AAT80608.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576257; AAT80609.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576258; AAT80610.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576259; AAT80611.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576260; AAT80612.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576261; AAT80613.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576262; AAT80614.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576263; AAT80615.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576264; AAT80616.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576265; AAT80617.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576266; AAT80618.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576267; AAT80619.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576268; AAT80620.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576269; AAT80621.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576270; AAT80622.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY576271; AAT80623.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK220946; BAD94467.1; ALT_INIT; mRNA.
DR PIR; A86176; A86176.
DR PIR; S71221; S71221.
DR RefSeq; NP_171935.1; NM_100320.4.
DR RefSeq; NP_849588.1; NM_179257.2.
DR PDB; 6K8I; X-ray; 2.70 A; A/B=1-612.
DR PDB; 6K8K; X-ray; 2.50 A; A/B/D/G=1-612.
DR PDB; 6M79; EM; 3.10 A; A/B/C/D=1-612.
DR PDB; 6X24; X-ray; 3.25 A; A/B/C/D=1-498.
DR PDBsum; 6K8I; -.
DR PDBsum; 6K8K; -.
DR PDBsum; 6M79; -.
DR PDBsum; 6X24; -.
DR AlphaFoldDB; Q96524; -.
DR SMR; Q96524; -.
DR BioGRID; 24764; 11.
DR DIP; DIP-33589N; -.
DR IntAct; Q96524; 13.
DR STRING; 3702.AT1G04400.1; -.
DR iPTMnet; Q96524; -.
DR PaxDb; Q96524; -.
DR PRIDE; Q96524; -.
DR ProteomicsDB; 224501; -.
DR EnsemblPlants; AT1G04400.1; AT1G04400.1; AT1G04400.
DR EnsemblPlants; AT1G04400.2; AT1G04400.2; AT1G04400.
DR GeneID; 839529; -.
DR Gramene; AT1G04400.1; AT1G04400.1; AT1G04400.
DR Gramene; AT1G04400.2; AT1G04400.2; AT1G04400.
DR KEGG; ath:AT1G04400; -.
DR Araport; AT1G04400; -.
DR TAIR; locus:2018254; AT1G04400.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_5_0_1; -.
DR InParanoid; Q96524; -.
DR OMA; ETLIDWD; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; Q96524; -.
DR PRO; PR:Q96524; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q96524; baseline and differential.
DR Genevisible; Q96524; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0009882; F:blue light photoreceptor activity; ISS:TAIR.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0009785; P:blue light signaling pathway; IGI:TAIR.
DR GO; GO:0006325; P:chromatin organization; IMP:TAIR.
DR GO; GO:0006338; P:chromatin remodeling; IMP:TAIR.
DR GO; GO:0010617; P:circadian regulation of calcium ion oscillation; IMP:TAIR.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0072387; P:flavin adenine dinucleotide metabolic process; IMP:UniProtKB.
DR GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0009638; P:phototropism; IMP:UniProtKB.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IDA:TAIR.
DR GO; GO:1901371; P:regulation of leaf morphogenesis; IMP:UniProtKB.
DR GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IDA:UniProtKB.
DR GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:UniProtKB.
DR GO; GO:1902347; P:response to strigolactone; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
DR GO; GO:0010118; P:stomatal movement; IGI:TAIR.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR014134; Cryptochrome_pln.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; PTHR11455; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 1.
DR TIGRFAMs; TIGR02766; crypt_chrom_pln; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromatin regulator; Chromophore; Cytoplasm;
KW FAD; Flavoprotein; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Photoreceptor protein; Plant defense; Receptor;
KW Reference proteome; Sensory transduction; Ubl conjugation.
FT CHAIN 1..612
FT /note="Cryptochrome-2"
FT /id="PRO_0000085122"
FT DOMAIN 5..134
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000255"
FT REGION 1..485
FT /note="CNT2, binds chromophores to sense blue light and
FT mediate CRY dimerization"
FT /evidence="ECO:0000303|PubMed:25721730"
FT REGION 486..612
FT /note="CCT2/CCE2, mediates blue light signaling"
FT /evidence="ECO:0000269|PubMed:11114337,
FT ECO:0000303|PubMed:25721730"
FT REGION 539..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 541..555
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 540..564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32398826,
FT ECO:0007744|PDB:6K8I, ECO:0007744|PDB:6K8K"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q43125"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q43125"
FT BINDING 244..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32398826,
FT ECO:0007744|PDB:6K8I, ECO:0007744|PDB:6K8K"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q43125"
FT BINDING 356..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32398826,
FT ECO:0007744|PDB:6K8K"
FT BINDING 356
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32398826,
FT ECO:0007744|PDB:6K8I, ECO:0007744|PDB:6K8K"
FT BINDING 387..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:32398826,
FT ECO:0007744|PDB:6K8I, ECO:0007744|PDB:6K8K"
FT BINDING 406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q43125"
FT SITE 321
FT /note="Involved in electron transfer from the protein
FT surface to the FAD cofactor"
FT /evidence="ECO:0000269|PubMed:25428980"
FT SITE 374
FT /note="Involved in electron transfer from the protein
FT surface to the FAD cofactor"
FT /evidence="ECO:0000269|PubMed:25428980"
FT SITE 397
FT /note="Involved in electron transfer from the protein
FT surface to the FAD cofactor"
FT /evidence="ECO:0000269|PubMed:25428980"
FT MOD_RES 587
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:23897926"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25792146"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25792146"
FT MOD_RES 603
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000269|PubMed:23897926"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25792146"
FT VARIANT 83
FT /note="I -> V (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 127
FT /note="Q -> S (in strain: cv. Bu-0, cv. Da(1)-12, cv. Di-G,
FT cv. Landsberg erecta, cv. Le-0, cv. Lip-0, cv. Mrk-0, cv.
FT Stw-0 and cv. Ta-0)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 326
FT /note="D -> E (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 367
FT /note="V -> M (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 476
FT /note="T -> I (in strain: cv. Cvi-0)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 482
FT /note="A -> G (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 498
FT /note="A -> S (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 507
FT /note="F -> L (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 511
FT /note="G -> E (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 543
FT /note="V -> L (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT VARIANT 611
FT /note="C -> Y (in strain: cv. Chi-1, cv. Co-1, cv. Kon, cv.
FT PHW-1 and cv. Sha)"
FT /evidence="ECO:0000305|PubMed:18273534"
FT MUTAGEN 321
FT /note="W->A,F: Photochemically inactive in vitro. Undergo
FT robust light-dependent photoreduction in an in vivo context
FT via an alternative electron transport involving small
FT molecule activators including ATP, NADH, and NADPH."
FT /evidence="ECO:0000269|PubMed:22139370,
FT ECO:0000269|PubMed:25428980"
FT MUTAGEN 331
FT /note="W->A: Decreased light sensitivity. Enhanced
FT photoreduction in the presence of added ATP."
FT /evidence="ECO:0000269|PubMed:25428980"
FT MUTAGEN 337
FT /note="G->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9565033"
FT MUTAGEN 374
FT /note="W->A: Photochemically inactive in vitro. Undergo
FT robust light-dependent photoreduction in an in vivo context
FT via an alternative electron transport involving small
FT molecule activators including ATP, NADH, and NADPH.
FT Enhanced photoreduction in the presence of added ATP.
FT Constitutive interaction with SPA1 and BHLH63/CIB1."
FT /evidence="ECO:0000269|PubMed:22139370,
FT ECO:0000269|PubMed:25428980"
FT MUTAGEN 374
FT /note="W->F: Photochemically inactive in vitro. Undergo
FT robust light-dependent photoreduction in an in vivo context
FT via an alternative electron transport involving small
FT molecule activators including ATP, NADH, and NADPH.
FT Enhanced photoreduction in the presence of added ATP."
FT /evidence="ECO:0000269|PubMed:22139370,
FT ECO:0000269|PubMed:25428980"
FT MUTAGEN 376
FT /note="W->A: Decreased light sensitivity. Enhanced
FT photoreduction in the presence of added ATP."
FT /evidence="ECO:0000269|PubMed:25428980"
FT MUTAGEN 377
FT /note="G->R: Constitutive light response."
FT /evidence="ECO:0000269|PubMed:21765176"
FT MUTAGEN 387
FT /note="D->A: Impaired FAD-binding leading to impaired blue
FT light-mediated inhibition of hypocotyl elongation and loss
FT of blue light-induced degradation. Disturbed BHLH63/CIB1
FT and SPA1 interactions."
FT /evidence="ECO:0000269|PubMed:18988809,
FT ECO:0000269|PubMed:21514160"
FT MUTAGEN 397
FT /note="W->A: Photochemically inactive in vitro. Undergo
FT robust light-dependent photoreduction in an in vivo context
FT via an alternative electron transport involving small
FT molecule activators including ATP, NADH, and NADPH."
FT /evidence="ECO:0000269|PubMed:22139370,
FT ECO:0000269|PubMed:25428980"
FT MUTAGEN 397
FT /note="W->F: Photochemically inactive both in vitro and in
FT vivo."
FT /evidence="ECO:0000269|PubMed:22139370,
FT ECO:0000269|PubMed:25428980"
FT MUTAGEN 399
FT /note="Y->A,F: Impaired ATP-mediated enhanced
FT photoreduction and decreased affinity for ATP."
FT /evidence="ECO:0000269|PubMed:25428980"
FT MUTAGEN 541
FT /note="K->R: Impaired nuclear importation leading to
FT reduced phosphorylation, physiological activities, and
FT degradation in response to blue light. Forms protein bodies
FT (photobodies) in both the nucleus and cytosol in response
FT to blue light."
FT /evidence="ECO:0000269|PubMed:22311776"
FT MUTAGEN 554..555
FT /note="KK->RR: Impaired nuclear importation leading to
FT reduced phosphorylation, physiological activities, and
FT degradation in response to blue light. Forms protein bodies
FT (photobodies) in both the nucleus and cytosol in response
FT to blue light."
FT /evidence="ECO:0000269|PubMed:22311776"
FT MUTAGEN 570..575
FT /note="SSSSSS->AAAAAA: Reduced blue light-mediated
FT phosphorylation and impaired blue light-dependent
FT proteolysis and hypocotyl inhibition response; when
FT associated with A-580, A-582, A-584, A-587, 598-A-A-599 and
FT A-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 570..575
FT /note="SSSSSS->DDDDDD: Reduced blue light-mediated
FT phosphorylation and impaired blue light-dependent
FT proteolysis and hypocotyl inhibition response; when
FT associated with D-580, D-582, D-584, D-587, 598-D-D-599 and
FT D-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 580
FT /note="S->A: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-A--A-573, A-
FT 582, A-584, A-587, 598-A-A-599 and A-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 580
FT /note="S->D: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-D--D-573, D-
FT 582, D-584, D-587, 598-D-D-599 and D-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 582
FT /note="S->A: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-A--A-573, A-
FT 580, A-584, A-587, 598-A-A-599 and A-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 582
FT /note="S->D: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-D--D-573, D-
FT 580, D-584, D-587, 598-D-D-599 and D-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 584
FT /note="S->A: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-A--A-573, A-
FT 580, A-582, A-587, 598-A-A-599 and A-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 584
FT /note="S->D: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-D--D-573, D-
FT 580, D-582, D-587, 598-D-D-599 and D-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 587
FT /note="S->A: Impaired regulation of hypocotyl growth in
FT blue light. Phosphorylated by CK1 proteins CK1.3 and CK1.4.
FT Reduced phosphorylation by CK1 proteins CK1.3 and CK1.4;
FT when associated with A-603. Reduced blue light-mediated
FT phosphorylation and impaired blue light-dependent
FT proteolysis and hypocotyl inhibition response; when
FT associated with 570-A--A-573, A-580, A-582, A-584, 598-A-A-
FT 599 and A-605."
FT /evidence="ECO:0000269|PubMed:23897926,
FT ECO:0000269|PubMed:25792146"
FT MUTAGEN 587
FT /note="S->D: Constitutive regulation of hypocotyl growth in
FT blue light. Reduced blue light-mediated phosphorylation and
FT impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-D--D-573, D-
FT 580, D-582, D-584, 598-D-D-599 and D-605."
FT /evidence="ECO:0000269|PubMed:23897926,
FT ECO:0000269|PubMed:25792146"
FT MUTAGEN 598..599
FT /note="SS->AA: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-A--A-573, A-
FT 580, A-582, A-584, A-587 and A-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 598..599
FT /note="SS->DD: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-D--D-573, D-
FT 580, D-582, D-584, D-587 and D-605."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 603
FT /note="T->A: Impaired regulation of hypocotyl growth in
FT blue light. Phosphorylated by CK1 proteins CK1.3 and CK1.4.
FT Reduced phosphorylation by CK1 proteins CK1.3 and CK1.4;
FT when associated with A-587."
FT /evidence="ECO:0000269|PubMed:23897926"
FT MUTAGEN 603
FT /note="T->D: Constitutive regulation of hypocotyl growth in
FT blue light."
FT /evidence="ECO:0000269|PubMed:23897926"
FT MUTAGEN 605
FT /note="S->A: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-A--A-573, A-
FT 580, A-582, A-584, A-587 and 598-A-A-599."
FT /evidence="ECO:0000269|PubMed:25792146"
FT MUTAGEN 605
FT /note="S->D: Reduced blue light-mediated phosphorylation
FT and impaired blue light-dependent proteolysis and hypocotyl
FT inhibition response; when associated with 570-D--D-573, D-
FT 580, D-582, D-584, D-587 and 598-D-D-599."
FT /evidence="ECO:0000269|PubMed:25792146"
FT CONFLICT 78
FT /note="K -> Q (in Ref. 1; AAB04996/AAB04997)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="A -> P (in Ref. 1; AAB04996/AAB04997)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> L (in Ref. 3; AAL16379)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> G (in Ref. 1; AAB04996)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="A -> V (in Ref. 1; AAB04996/AAB04997)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="K -> E (in Ref. 1; CAA67508)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="K -> Q (in Ref. 1; CAA67508)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:6K8K"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 50..69
FT /evidence="ECO:0007829|PDB:6K8K"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 82..93
FT /evidence="ECO:0007829|PDB:6K8K"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:6K8K"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6X24"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:6K8K"
FT TURN 181..185
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:6K8K"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 258..274
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 278..303
FT /evidence="ECO:0007829|PDB:6K8K"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 390..400
FT /evidence="ECO:0007829|PDB:6K8K"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:6M79"
FT HELIX 416..423
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:6X24"
FT HELIX 428..433
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:6K8K"
FT TURN 442..446
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 453..458
FT /evidence="ECO:0007829|PDB:6K8K"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:6K8K"
FT HELIX 474..494
FT /evidence="ECO:0007829|PDB:6K8K"
SQ SEQUENCE 612 AA; 69457 MW; 082E311301465904 CRC64;
MKMDKKTIVW FRRDLRIEDN PALAAAAHEG SVFPVFIWCP EEEGQFYPGR ASRWWMKQSL
AHLSQSLKAL GSDLTLIKTH NTISAILDCI RVTGATKVVF NHLYDPVSLV RDHTVKEKLV
ERGISVQSYN GDLLYEPWEI YCEKGKPFTS FNSYWKKCLD MSIESVMLPP PWRLMPITAA
AEAIWACSIE ELGLENEAEK PSNALLTRAW SPGWSNADKL LNEFIEKQLI DYAKNSKKVV
GNSTSLLSPY LHFGEISVRH VFQCARMKQI IWARDKNSEG EESADLFLRG IGLREYSRYI
CFNFPFTHEQ SLLSHLRFFP WDADVDKFKA WRQGRTGYPL VDAGMRELWA TGWMHNRIRV
IVSSFAVKFL LLPWKWGMKY FWDTLLDADL ECDILGWQYI SGSIPDGHEL DRLDNPALQG
AKYDPEGEYI RQWLPELARL PTEWIHHPWD APLTVLKASG VELGTNYAKP IVDIDTAREL
LAKAISRTRE AQIMIGAAPD EIVADSFEAL GANTIKEPGL CPSVSSNDQQ VPSAVRYNGS
KRVKPEEEEE RDMKKSRGFD ERELFSTAES SSSSSVFFVS QSCSLASEGK NLEGIQDSSD
QITTSLGKNG CK
