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Cryptochrome-2 (Atcry2) (Blue light photoreceptor) (Protein PHR homolog 1) (AtPHH1) (Protein SUPPRESSOR OF elf3 20)

 CRY2_ARATH              Reviewed;         612 AA.
Q96524; B0LQ23; B0LQ24; B0LQ25; B0LQ29; Q42549; Q42603; Q42604;
Q56ZL8; Q696X6; Q696X8; Q696Z7; Q697A2; Q8VWL9; Q8VZY9;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
07-JUN-2017, entry version 151.
RecName: Full=Cryptochrome-2 {ECO:0000303|Ref.2};
Short=Atcry2 {ECO:0000303|Ref.2};
AltName: Full=Blue light photoreceptor {ECO:0000303|PubMed:9003312};
AltName: Full=Protein PHR homolog 1 {ECO:0000303|PubMed:9003312};
Short=AtPHH1 {ECO:0000303|PubMed:9003312};
AltName: Full=Protein SUPPRESSOR OF elf3 20 {ECO:0000303|PubMed:21296763};
Name=CRY2 {ECO:0000303|Ref.2};
Synonyms=PHH1 {ECO:0000303|PubMed:9003312},
SEL20 {ECO:0000303|PubMed:21296763};
OrderedLocusNames=At1g04400 {ECO:0000312|Araport:AT1G04400};
ORFNames=F19P19.14 {ECO:0000312|EMBL:AAB70435.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=cv. Columbia;
PubMed=9003312; DOI=10.1007/s004380050321;
Hoffman P.D., Batschauer A., Hays J.B.;
"PHH1, a novel gene from Arabidopsis thaliana that encodes a protein
similar to plant blue-light photoreceptors and microbial
photolyases.";
Mol. Gen. Genet. 253:259-265(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Lin C., Ahmad M., Chan J., Cashmore A.R.;
"CRY2: a second member of the Arabidopsis cryptochrome gene family.";
(er) Plant Gene Register PGR96-001(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=cv. Cvi-0, and cv. Landsberg erecta;
PubMed=11726930; DOI=10.1038/ng767;
El-Din El-Assal S., Alonso-Blanco C., Peeters A.J.M., Raz V.,
Koornneef M.;
"A QTL for flowering time in Arabidopsis reveals a novel allele of
CRY2.";
Nat. Genet. 29:435-440(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
STRAIN=cv. Bla-10, cv. Bsch-0, cv. Bu-0, cv. Bu-2, cv. Chi-1,
cv. Co-1, cv. Columbia, cv. Cvi-0, cv. Da(1)-12, cv. Di-G, cv. El-0,
cv. Fe-1, cv. Gr-3, cv. Hn-0, cv. Kon, cv. Kr-0, cv. Landsberg erecta,
cv. Le-0, cv. Li-3, cv. Lip-0, cv. Lz-0, cv. Mrk-0, cv. Mt-0,
cv. Mz-0, cv. Ove-0, cv. PHW-1, cv. PHW-32, cv. PHW-36, cv. Sha,
cv. Stw-0, cv. Ta-0, and cv. Wassilewskija-3;
PubMed=18273534; DOI=10.1007/s00239-007-9063-3;
Moore R.C., Stevens M.H.H.;
"Local patterns of nucleotide polymorphism are highly variable in the
selfing species Arabidopsis thaliana.";
J. Mol. Evol. 66:116-129(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[6]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-612.
STRAIN=cv. Bla-10, cv. Bsch-0, cv. Bu-0, cv. Bu-2, cv. Chi-1,
cv. Co-1, cv. Cvi-0, cv. Da(1)-12, cv. Di-G, cv. El-0, cv. Fe-1,
cv. Gr-3, cv. Hn-0, cv. Kon, cv. Kr-0, cv. Landsberg erecta, cv. Le-0,
cv. Li-3, cv. Lip-0, cv. Lz-0, cv. Mrk-0, cv. Mt-0, cv. Mz-0,
cv. Ove-0, cv. Oy-1, cv. PHW-1, cv. PHW-33, cv. PHW-36, cv. Sha,
cv. Stw-0, and cv. Ta-0;
PubMed=15280248; DOI=10.1534/genetics.103.024950;
Olsen K.M., Halldorsdottir S.S., Stinchcombe J.R., Weinig C.,
Schmitt J., Purugganan M.D.;
"Linkage disequilibrium mapping of Arabidopsis CRY2 flowering time
alleles.";
Genetics 167:1361-1369(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-612.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
FUNCTION, AND MUTAGENESIS OF GLY-337.
PubMed=9565033; DOI=10.1038/33701;
Ahmad M., Jarillo J.A., Smirnova O., Cashmore A.R.;
"Cryptochrome blue-light photoreceptors of Arabidopsis implicated in
phototropism.";
Nature 392:720-723(1998).
[11]
PHOSPHORYLATION.
PubMed=9651577; DOI=10.1016/S1097-2765(00)80094-5;
Ahmad M., Jarillo J.A., Smirnova O., Cashmore A.R.;
"The CRY1 blue light photoreceptor of Arabidopsis interacts with
phytochrome A in vitro.";
Mol. Cell 1:939-948(1998).
[12]
FUNCTION.
PubMed=9482948; DOI=10.1073/pnas.95.5.2686;
Lin C., Yang H., Guo H., Mockler T., Chen J., Cashmore A.R.;
"Enhancement of blue-light sensitivity of Arabidopsis seedlings by a
blue light receptor cryptochrome 2.";
Proc. Natl. Acad. Sci. U.S.A. 95:2686-2690(1998).
[13]
SUBCELLULAR LOCATION.
PubMed=10476076; DOI=10.1046/j.1365-313X.1999.00535.x;
Kleiner O., Kircher S., Harter K., Batschauer A.;
"Nuclear localization of the Arabidopsis blue light receptor
cryptochrome 2.";
Plant J. 19:289-296(1999).
[14]
DOMAINS.
PubMed=11114337; DOI=10.1016/S0092-8674(00)00184-7;
Yang H.-Q., Wu Y.-J., Tang R.-H., Liu D., Liu Y., Cashmore A.R.;
"The C termini of Arabidopsis cryptochromes mediate a constitutive
light response.";
Cell 103:815-827(2000).
[15]
INTERACTION WITH PHYB.
PubMed=11089975; DOI=10.1038/35041583;
Mas P., Devlin P.F., Panda S., Kay S.A.;
"Functional interaction of phytochrome B and cryptochrome 2.";
Nature 408:207-211(2000).
[16]
INDUCTION BY CIRCADIAN CLOCK AND LIGHT, AND TISSUE SPECIFICITY.
PubMed=11743105; DOI=10.1104/pp.127.4.1607;
Toth R., Kevei E., Hall A., Millar A.J., Nagy F., Kozma-Bognar L.;
"Circadian clock-regulated expression of phytochrome and cryptochrome
genes in Arabidopsis.";
Plant Physiol. 127:1607-1616(2001).
[17]
INTERACTION WITH COP1.
PubMed=11509693; DOI=10.1126/science.1063630;
Wang H., Ma L.-G., Li J.-M., Zhao H.-Y., Deng X.W.;
"Direct interaction of Arabidopsis cryptochromes with COP1 in light
control development.";
Science 294:154-158(2001).
[18]
PHOSPHORYLATION.
PubMed=12066190; DOI=10.1038/nature00815;
Shalitin D., Yang H., Mockler T.C., Maymon M., Guo H., Whitelam G.C.,
Lin C.;
"Regulation of Arabidopsis cryptochrome 2 by blue-light-dependent
phosphorylation.";
Nature 417:763-767(2002).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12857830; DOI=10.1104/pp.102.018481;
Whippo C.W., Hangarter R.P.;
"Second positive phototropism results from coordinated co-action of
the phototropins and cryptochromes.";
Plant Physiol. 132:1499-1507(2003).
[20]
FUNCTION.
PubMed=14605222; DOI=10.1104/pp.103.029819;
El-Din El-Assal S., Alonso-Blanco C., Peeters A.J., Wagemaker C.,
Weller J.L., Koornneef M.;
"The role of cryptochrome 2 in flowering in Arabidopsis.";
Plant Physiol. 133:1504-1516(2003).
[21]
INDUCTION.
PubMed=12578985; DOI=10.1073/pnas.0437826100;
Mockler T., Yang H., Yu X., Parikh D., Cheng Y.C., Dolan S., Lin C.;
"Regulation of photoperiodic flowering by Arabidopsis
photoreceptors.";
Proc. Natl. Acad. Sci. U.S.A. 100:2140-2145(2003).
[22]
FUNCTION.
PubMed=16093319; DOI=10.1073/pnas.0501011102;
Mao J., Zhang Y.C., Sang Y., Li Q.H., Yang H.Q.;
"A role for Arabidopsis cryptochromes and COP1 in the regulation of
stomatal opening.";
Proc. Natl. Acad. Sci. U.S.A. 102:12270-12275(2005).
[23]
PTM, COFACTOR, AND ATP-BINDING.
PubMed=17073458; DOI=10.1021/bi061556n;
Ozguer S., Sancar A.;
"Analysis of autophosphorylating kinase activities of Arabidopsis and
human cryptochromes.";
Biochemistry 45:13369-13374(2006).
[24]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16703358; DOI=10.1007/s00425-006-0280-6;
Canamero R.C., Bakrim N., Bouly J.-P., Garay A., Dudkin E.E.,
Habricot Y., Ahmad M.;
"Cryptochrome photoreceptors cry1 and cry2 antagonistically regulate
primary root elongation in Arabidopsis thaliana.";
Planta 224:995-1003(2006).
[25]
COFACTOR.
PubMed=17355959; DOI=10.1074/jbc.M700616200;
Banerjee R., Schleicher E., Meier S., Viana R.M., Pokorny R.,
Ahmad M., Bittl R., Batschauer A.;
"The signaling state of Arabidopsis cryptochrome 2 contains flavin
semiquinone.";
J. Biol. Chem. 282:14916-14922(2007).
[26]
FUNCTION.
PubMed=17470059; DOI=10.1111/j.1365-313X.2007.03093.x;
Tessadori F., Schulkes R.K., van Driel R., Fransz P.;
"Light-regulated large-scale reorganization of chromatin during the
floral transition in Arabidopsis.";
Plant J. 50:848-857(2007).
[27]
SUBCELLULAR LOCATION, SUBUNIT, AND PHOSPHORYLATION.
PubMed=17438275; DOI=10.1073/pnas.0701912104;
Yu X., Shalitin D., Liu X., Maymon M., Klejnot J., Yang H., Lopez J.,
Zhao X., Bendehakkalu K.T., Lin C.;
"Derepression of the NC80 motif is critical for the photoactivation of
Arabidopsis CRY2.";
Proc. Natl. Acad. Sci. U.S.A. 104:7289-7294(2007).
[28]
SUBCELLULAR LOCATION, UBIQUITINATION, AND PHOSPHORYLATION.
PubMed=17965271; DOI=10.1105/tpc.107.053017;
Yu X., Klejnot J., Zhao X., Shalitin D., Maymon M., Yang H., Lee J.,
Liu X., Lopez J., Lin C.;
"Arabidopsis cryptochrome 2 completes its posttranslational life cycle
in the nucleus.";
Plant Cell 19:3146-3156(2007).
[29]
FUNCTION.
PubMed=17259260; DOI=10.1105/tpc.106.048157;
Endo M., Mochizuki N., Suzuki T., Nagatani A.;
"CRYPTOCHROME2 in vascular bundles regulates flowering in
Arabidopsis.";
Plant Cell 19:84-93(2007).
[30]
INTERACTION WITH BHLH63/CIB1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-387.
PubMed=18988809; DOI=10.1126/science.1163927;
Liu H., Yu X., Li K., Klejnot J., Yang H., Lisiero D., Lin C.;
"Photoexcited CRY2 interacts with CIB1 to regulate transcription and
floral initiation in Arabidopsis.";
Science 322:1535-1539(2008).
[31]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=19558423; DOI=10.1111/j.1469-8137.2009.02921.x;
Millenaar F.F., van Zanten M., Cox M.C., Pierik R., Voesenek L.A.,
Peeters A.J.;
"Differential petiole growth in Arabidopsis thaliana: photocontrol and
hormonal regulation.";
New Phytol. 184:141-152(2009).
[32]
REVIEW ON CRYPTOCHROMES.
PubMed=21841916; DOI=10.1199/tab.0135;
Yu X., Liu H., Klejnot J., Lin C.;
"The cryptochrome blue light receptors.";
Arabidopsis Book 8:E0135-E0135(2010).
[33]
REVIEW ON PHOTORECEPTORS.
PubMed=20705178; DOI=10.1016/S0070-2153(10)91002-8;
Kami C., Lorrain S., Hornitschek P., Fankhauser C.;
"Light-regulated plant growth and development.";
Curr. Top. Dev. Biol. 91:29-66(2010).
[34]
BIOTECHNOLOGY.
PubMed=21037589; DOI=10.1038/nmeth.1524;
Kennedy M.J., Hughes R.M., Peteya L.A., Schwartz J.W., Ehlers M.D.,
Tucker C.L.;
"Rapid blue-light-mediated induction of protein interactions in living
cells.";
Nat. Methods 7:973-975(2010).
[35]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY LOW LIGHT.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=20935177; DOI=10.1104/pp.110.164616;
van Zanten M., Tessadori F., McLoughlin F., Smith R., Millenaar F.F.,
van Driel R., Voesenek L.A.C.J., Peeters A.J.M., Fransz P.;
"Photoreceptors CRYTOCHROME2 and phytochrome B control chromatin
compaction in Arabidopsis.";
Plant Physiol. 154:1686-1696(2010).
[36]
FUNCTION, DISRUPTION PHENOTYPE, REGULATION BY BLUE-LIGHT AND DARKNESS,
INTERACTION WITH COP1, AND SUBCELLULAR LOCATION.
PubMed=20624951; DOI=10.1073/pnas.1004529107;
Jeong R.-D., Chandra-Shekara A.C., Barman S.R., Navarre D.,
Klessig D.F., Kachroo A., Kachroo P.;
"Cryptochrome 2 and phototropin 2 regulate resistance protein-mediated
viral defense by negatively regulating an E3 ubiquitin ligase.";
Proc. Natl. Acad. Sci. U.S.A. 107:13538-13543(2010).
[37]
FUNCTION, INTERACTION WITH SPA1, AND MUTAGENESIS OF ASP-387.
PubMed=21514160; DOI=10.1016/j.cub.2011.03.048;
Zuo Z., Liu H., Liu B., Liu X., Lin C.;
"Blue light-dependent interaction of CRY2 with SPA1 regulates COP1
activity and floral initiation in Arabidopsis.";
Curr. Biol. 21:841-847(2011).
[38]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION
WITH SPA1.
STRAIN=cv. Columbia;
PubMed=21511872; DOI=10.1101/gad.2025111;
Lian H.-L., He S.-B., Zhang Y.-C., Zhu D.-M., Zhang J.-Y., Jia K.-P.,
Sun S.-X., Li L., Yang H.-Q.;
"Blue-light-dependent interaction of cryptochrome 1 with SPA1 defines
a dynamic signaling mechanism.";
Genes Dev. 25:1023-1028(2011).
[39]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21296763; DOI=10.1093/jxb/erq450;
Nefissi R., Natsui Y., Miyata K., Oda A., Hase Y., Nakagawa M.,
Ghorbel A., Mizoguchi T.;
"Double loss-of-function mutation in EARLY FLOWERING 3 and
CRYPTOCHROME 2 genes delays flowering under continuous light but
accelerates it under long days and short days: an important role for
Arabidopsis CRY2 to accelerate flowering time in continuous light.";
J. Exp. Bot. 62:2731-2744(2011).
[40]
MUTAGENESIS OF TRP-321; TRP-374 AND TRP-397, AND INTERACTION WITH SPA1
AND BHLH63/CIB1.
STRAIN=cv. Columbia;
PubMed=22139370; DOI=10.1073/pnas.1114579108;
Li X., Wang Q., Yu X., Liu H., Yang H., Zhao C., Liu X., Tan C.,
Klejnot J., Zhong D., Lin C.;
"Arabidopsis cryptochrome 2 (CRY2) functions by the photoactivation
mechanism distinct from the tryptophan (trp) triad-dependent
photoreduction.";
Proc. Natl. Acad. Sci. U.S.A. 108:20844-20849(2011).
[41]
MUTAGENESIS OF GLY-377.
PubMed=21765176; DOI=10.1093/mp/ssr052;
Gu N.-N., Zhang Y.-C., Yang H.-Q.;
"Substitution of a conserved glycine in the PHR domain of Arabidopsis
cryptochrome 1 confers a constitutive light response.";
Mol. Plant 5:85-97(2012).
[42]
SUBCELLULAR LOCATION, REGULATION BY BLUE LIGHT, AND MUTAGENESIS OF
LYS-541 AND 554-LYS-LYS-555.
STRAIN=cv. Columbia;
PubMed=22311776; DOI=10.1093/mp/sss007;
Zuo Z.-C., Meng Y.-Y., Yu X.-H., Zhang Z.-L., Feng D.-S., Sun S.-F.,
Liu B., Lin C.-T.;
"A study of the blue-light-dependent phosphorylation, degradation, and
photobody formation of Arabidopsis CRY2.";
Mol. Plant 5:726-733(2012).
[43]
INTERACTION WITH SPA1, AND SUBCELLULAR LOCATION.
PubMed=22739826; DOI=10.1105/tpc.112.098210;
Weidler G., Zur Oven-Krockhaus S., Heunemann M., Orth C.,
Schleifenbaum F., Harter K., Hoecker U., Batschauer A.;
"Degradation of Arabidopsis CRY2 is regulated by SPA proteins and
phytochrome A.";
Plant Cell 24:2610-2623(2012).
[44]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=22147516; DOI=10.1104/pp.111.187237;
Boccalandro H.E., Giordano C.V., Ploschuk E.L., Piccoli P.N.,
Bottini R., Casal J.J.;
"Phototropins but not cryptochromes mediate the blue light-specific
promotion of stomatal conductance, while both enhance photosynthesis
and transpiration under full sunlight.";
Plant Physiol. 158:1475-1484(2012).
[45]
BIOTECHNOLOGY.
PubMed=22847441; DOI=10.1073/pnas.1211305109;
Idevall-Hagren O., Dickson E.J., Hille B., Toomre D.K., De Camilli P.;
"Optogenetic control of phosphoinositide metabolism.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2316-E2323(2012).
[46]
SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
PubMed=23833191; DOI=10.1074/jbc.M113.493361;
Ozkan-Dagliyan I., Chiou Y.-Y., Ye R., Hassan B.H., Ozturk N.,
Sancar A.;
"Formation of Arabidopsis Cryptochrome 2 photobodies in mammalian
nuclei: application as an optogenetic DNA damage checkpoint switch.";
J. Biol. Chem. 288:23244-23251(2013).
[47]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY TEMPERATURE.
STRAIN=cv. Columbia;
PubMed=23511208; DOI=10.1038/msb.2013.7;
Gould P.D., Ugarte N., Domijan M., Costa M., Foreman J., Macgregor D.,
Rose K., Griffiths J., Millar A.J., Finkenstaedt B., Penfield S.,
Rand D.A., Halliday K.J., Hall A.J.W.;
"Network balance via CRY signalling controls the Arabidopsis circadian
clock over ambient temperatures.";
Mol. Syst. Biol. 9:650-650(2013).
[48]
PHOSPHORYLATION AT SER-587 AND THR-603 BY CK1.3 AND CK1.4, AND
MUTAGENESIS OF SER-587 AND THR-603.
PubMed=23897926; DOI=10.1105/tpc.113.114322;
Tan S.-T., Dai C., Liu H.-T., Xue H.-W.;
"Arabidopsis casein kinase1 proteins CK1.3 and CK1.4 phosphorylate
cryptochrome2 to regulate blue light signaling.";
Plant Cell 25:2618-2632(2013).
[49]
FUNCTION.
STRAIN=cv. Landsberg erecta;
PubMed=23398192; DOI=10.1111/tpj.12144;
Herbel V., Orth C., Wenzel R., Ahmad M., Bittl R., Batschauer A.;
"Lifetimes of Arabidopsis cryptochrome signaling states in vivo.";
Plant J. 74:583-592(2013).
[50]
FUNCTION, AND INTERACTION WITH BHLH63/CIB1; BHLH78/CIB2; BHLH74/CIB4
AND BHLH76/CIB5.
STRAIN=cv. Columbia;
PubMed=24130508; DOI=10.1371/journal.pgen.1003861;
Liu Y., Li X., Li K., Liu H., Lin C.;
"Multiple bHLH proteins form heterodimers to mediate CRY2-dependent
regulation of flowering-time in Arabidopsis.";
PLoS Genet. 9:E1003861-E1003861(2013).
[51]
INTERACTION WITH BHLH63/CIB1.
PubMed=24780222; DOI=10.1016/j.ab.2014.04.023;
Cui Y., Choudhury S.R., Irudayaraj J.;
"Quantitative real-time kinetics of optogenetic proteins CRY2 and
CIB1/N using single-molecule tools.";
Anal. Biochem. 458:58-60(2014).
[52]
BIOTECHNOLOGY.
PubMed=24718798; DOI=10.1007/978-1-4939-0470-9_8;
Idevall-Hagren O., Decamilli P.;
"Manipulation of plasma membrane phosphoinositides using photoinduced
protein-protein interactions.";
Methods Mol. Biol. 1148:109-128(2014).
[53]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=24126495; DOI=10.1093/mp/sst093;
Jia K.-P., Luo Q., He S.-B., Lu X.-D., Yang H.-Q.;
"Strigolactone-regulated hypocotyl elongation is dependent on
cryptochrome and phytochrome signaling pathways in Arabidopsis.";
Mol. Plant 7:528-540(2014).
[54]
FUNCTION, COFACTOR, AND MUTAGENESIS OF TRP-321; TRP-331; TRP-374;
TRP-376; TRP-397 AND TYR-399.
PubMed=25428980; DOI=10.1105/tpc.114.129809;
Engelhard C., Wang X., Robles D., Moldt J., Essen L.-O.,
Batschauer A., Bittl R., Ahmad M.;
"Cellular metabolites enhance the light sensitivity of Arabidopsis
cryptochrome through alternate electron transfer pathways.";
Plant Cell 26:4519-4531(2014).
[55]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26095447; DOI=10.1002/bem.21927;
Xu C., Li Y., Yu Y., Zhang Y., Wei S.;
"Suppression of Arabidopsis flowering by near-null magnetic field is
affected by light.";
Bioelectromagnetics 36:476-479(2015).
[56]
BIOTECHNOLOGY.
PubMed=25963241; DOI=10.1016/j.chembiol.2015.04.014;
Duan L., Che D., Zhang K., Ong Q., Guo S., Cui B.;
"Optogenetic control of molecular motors and organelle distributions
in cells.";
Chem. Biol. 22:671-682(2015).
[57]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-598; SER-599 AND SER-605,
MUTAGENESIS OF 570-SER--SER-575; SER-580; SER-582; SER-584; SER-587;
598-SER-SER-599 AND SER-605, IDENTIFICATION BY MASS SPECTROMETRY,
UBIQUITINATION, AND REGULATION BY BLUE LIGHT.
PubMed=25792146; DOI=10.1016/j.molp.2015.03.005;
Wang Q., Barshop W.D., Bian M., Vashisht A.A., He R., Yu X., Liu B.,
Nguyen P., Liu X., Zhao X., Wohlschlegel J.A., Lin C.;
"The blue light-dependent phosphorylation of the CCE domain determines
the photosensitivity of Arabidopsis CRY2.";
Mol. Plant 8:631-643(2015).
[58]
DOMAINS.
PubMed=25721730; DOI=10.1016/j.molp.2015.02.008;
He S.B., Wang W.X., Zhang J.Y., Xu F., Lian H.L., Li L., Yang H.Q.;
"The CNT1 domain of Arabidopsis CRY1 Alone is sufficient to mediate
blue light inhibition of hypocotyl elongation.";
Mol. Plant 8:822-825(2015).
[59]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=26179959; DOI=10.1080/15592324.2015.1042647;
Jourdan N., Martino C.F., El-Esawi M., Witczak J., Bouchet P.-E.,
d'Harlingue A., Ahmad M.;
"Blue-light dependent ROS formation by Arabidopsis cryptochrome-2 may
contribute toward its signaling role.";
Plant Signal. Behav. 10:E1042647-E1042647(2015).
[60]
FUNCTION, INDUCTION BY LOW BLUE LIGHT, INTERACTION WITH PIF4 AND PIF5,
AND SUBCELLULAR LOCATION.
PubMed=26724867; DOI=10.1016/j.cell.2015.12.018;
Pedmale U.V., Huang S.S., Zander M., Cole B.J., Hetzel J., Ljung K.,
Reis P.A., Sridevi P., Nito K., Nery J.R., Ecker J.R., Chory J.;
"Cryptochromes interact directly with PIFs to control plant growth in
limiting blue light.";
Cell 164:233-245(2016).
[61]
INTERACTION WITH BIC1, AND SUBUNIT.
PubMed=27846570; DOI=10.1126/science.aaf9030;
Wang Q., Zuo Z., Wang X., Gu L., Yoshizumi T., Yang Z., Yang L.,
Liu Q., Liu W., Han Y.J., Kim J.I., Liu B., Wohlschlegel J.A.,
Matsui M., Oka Y., Lin C.;
"Photoactivation and inactivation of Arabidopsis cryptochrome 2.";
Science 354:343-347(2016).
-!- FUNCTION: Photoreceptor that mediates primarily blue light
inhibition of hypocotyl elongation and photoperiodic control of
floral initiation, and regulates other light responses, including
circadian rhythms, tropic growth, stomata opening, guard cell
development, root development, bacterial and viral pathogen
responses, abiotic stress responses, cell cycles, programmed cell
death, apical dominance, fruit and ovule development, seed
dormancy, and magnetoreception. Photoexcited cryptochromes
interact with signaling partner proteins to alter gene expression
at both transcriptional and post-translational levels and,
consequently, regulate the corresponding metabolic and
developmental programs (PubMed:21841916). Blue-light absorbing
flavoprotein that activates reversible flavin photoreduction via
an electron transport chain comprising a tryptophan triad (W-321,
W-374 and W-397), or via an alternative electron transport that
involves small metabolites, including NADPH, NADH, and ATP. The
half-life of the activated signaling state is about 16 minutes
(PubMed:25428980, PubMed:23398192). Perceives low blue light (LBL)
and responds by directly contacting two bHLH transcription
factors, PIF4 and PIF5, at chromatin on E-box variant 5'-
CA[CT]GTG-3' to promote their activity and stimulate specific gene
expression to adapt global physiology (e.g. hypocotyl elongation
and hyponastic growth in low blue light) (PubMed:26724867,
PubMed:19558423). In response to blue light, binds to CIB proteins
(e.g. BHLH63/CIB1 and BHLH76/CIB5) to activates transcription and
floral initiation (PubMed:24130508). Mediates blue light-induced
gene expression, floral initiation and hypocotyl elongation
through the interaction with SPA1 that prevents formation of
SPA1/COP1 complex but stimulates COP1 binding, and thus inhibits
COP1-mediated degradation of transcription factors (e.g. CO and
HY5) (PubMed:21514160, PubMed:21511872, PubMed:16093319). Promotes
flowering time in continuous light (LL) (PubMed:21296763).
Involved in shortening the circadian clock period, especially at
27 degrees Celsius, in blue light (BL). Required to maintain clock
genes expression rhythm (PubMed:23511208). Triggers nuclear
accumulation of ROS in response to blue light illumination
(PubMed:26179959). Involved in blue light-dependent stomatal
opening, transpiration and inhibition of stem and root growth,
probably by regulating abscisic acid (ABA) (PubMed:22147516,
PubMed:16093319, PubMed:16703358, PubMed:9482948, PubMed:9565033).
Regulates the timing of flowering by promoting the expression of
'FLOWERING LOCUS T' (FT) in vascular bundles. Negatively regulated
by 'FLOWERING LOCUS C' (FLC) (PubMed:14605222, PubMed:17259260).
General positive regulator of reversible low light-induced
chromatin decompaction (PubMed:20935177). Involved in triggering
chromatin decondensation during floral transition
(PubMed:17470059). Together with phototropins, involved in
phototropism regulation by various blue light fluence; blue light
attenuates phototropism in high fluence rates (100 umol.m-2.s-1)
but enhances phototropism in low fluence rates (<1.0 umol.m-2.s-1)
(PubMed:12857830). The effect of near-null magnetic field on
flowering is altered by changes of blue light cycle and intensity
in a CRY1/CRY2-dependent manner (PubMed:26095447). Involved in the
strigolactone signaling that regulates hypocotyl growth in
response to blue light (PubMed:24126495).
{ECO:0000269|PubMed:12857830, ECO:0000269|PubMed:14605222,
ECO:0000269|PubMed:16093319, ECO:0000269|PubMed:16703358,
ECO:0000269|PubMed:17259260, ECO:0000269|PubMed:17470059,
ECO:0000269|PubMed:19558423, ECO:0000269|PubMed:20935177,
ECO:0000269|PubMed:21296763, ECO:0000269|PubMed:21511872,
ECO:0000269|PubMed:21514160, ECO:0000269|PubMed:22147516,
ECO:0000269|PubMed:23398192, ECO:0000269|PubMed:23511208,
ECO:0000269|PubMed:24126495, ECO:0000269|PubMed:24130508,
ECO:0000269|PubMed:25428980, ECO:0000269|PubMed:26095447,
ECO:0000269|PubMed:26179959, ECO:0000269|PubMed:26724867,
ECO:0000269|PubMed:9482948, ECO:0000269|PubMed:9565033,
ECO:0000303|PubMed:21841916}.
-!- FUNCTION: Confers resistance to turnip crinkle virus (TCV) by
preventing COP1-mediated proteasome-mediated degradation of
RPP8/HRT, thus promoting its stability in light. Exposure to
darkness or blue-light induces degradation of CRY2, and in turn of
RPP8/HRT, resulting in susceptibility to TCV.
{ECO:0000269|PubMed:20624951}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17073458,
ECO:0000269|PubMed:17355959};
Note=Binds 1 FAD per subunit. The flavin in the dark is in the
oxidized (bright yellow) redox state, whereas it becomes reduced
subsequent to light activation and formation of the neutral
radical (pale yellow). {ECO:0000269|PubMed:17073458,
ECO:0000269|PubMed:17355959, ECO:0000269|PubMed:25428980};
-!- COFACTOR:
Name=(6R)-5,10-methylenetetrahydrofolate; Xref=ChEBI:CHEBI:15636;
Evidence={ECO:0000250};
Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
{ECO:0000250};
-!- SUBUNIT: Homodimer (PubMed:11089975, PubMed:11509693,
PubMed:17438275, PubMed:27846570). Blue-light dependent
dimerization (PubMed:27846570). Interacts with COP1 and PHYB in
the nucleus (PubMed:11089975, PubMed:11509693, PubMed:17438275,
PubMed:20624951). Binds reversibly to CIBs proteins such as
BHLH63/CIB1, BHLH78/CIB2, BHLH74/CIB4 and BHLH76/CIB5 after blue
light illumination to stimulate their transcription factor
activities (PubMed:18988809, PubMed:22139370, PubMed:24130508,
PubMed:24780222). Interacts with PIF4 and PIF5 in the nucleus in
response to low blue light (LBL) (PubMed:26724867). Binds to SPA1
in response to blue light, this interaction prevents SPA1/COP1
complex formation but stimulates interaction with COP1, and thus
avoid COP1-dependent degradation of the transcription factors CO
and HY5 by the proteasome and promotes hypocotyl elongation and
floral initiation (PubMed:21514160, PubMed:22139370,
PubMed:21511872, PubMed:22739826). Binding to ATP mediates
conformational changes which facilitate flavin binding
(PubMed:17073458). Interacts with BIC1 in both darkness and light
(PubMed:27846570). {ECO:0000269|PubMed:11089975,
ECO:0000269|PubMed:11509693, ECO:0000269|PubMed:17073458,
ECO:0000269|PubMed:17438275, ECO:0000269|PubMed:18988809,
ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:21511872,
ECO:0000269|PubMed:21514160, ECO:0000269|PubMed:22139370,
ECO:0000269|PubMed:22739826, ECO:0000269|PubMed:24130508,
ECO:0000269|PubMed:24780222, ECO:0000269|PubMed:26724867,
ECO:0000269|PubMed:27846570}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-531555, EBI-531555;
P43254:COP1; NbExp=2; IntAct=EBI-531555, EBI-301649;
P14713:PHYB; NbExp=3; IntAct=EBI-531555, EBI-300727;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00768, ECO:0000269|PubMed:10476076,
ECO:0000269|PubMed:17438275, ECO:0000269|PubMed:17965271,
ECO:0000269|PubMed:18988809, ECO:0000269|PubMed:20624951,
ECO:0000269|PubMed:22311776, ECO:0000269|PubMed:22739826,
ECO:0000269|PubMed:25792146, ECO:0000269|PubMed:26179959,
ECO:0000269|PubMed:26724867}. Nucleus, PML body
{ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:23833191}.
Cytoplasm {ECO:0000269|PubMed:26179959}. Note=Present in nuclear
bodies (NBs) in blue light (e.g. photobodies) (PubMed:21511872,
PubMed:23833191, PubMed:22311776). Translocates from the cytosol
to the nucleus in response to blue light illumination
(PubMed:26179959). {ECO:0000269|PubMed:21511872,
ECO:0000269|PubMed:22311776, ECO:0000269|PubMed:23833191,
ECO:0000269|PubMed:26179959}.
-!- TISSUE SPECIFICITY: Mostly expressed in the shoot meristems and
root tips, and, to a lower extent, in the cotyledons, hypocotyls,
and roots. {ECO:0000269|PubMed:11743105}.
-!- INDUCTION: Daily oscillation of protein abundance in plants grown
in short days (SD) but not in long days (LD) (PubMed:12578985).
Expression levels display circadian oscillations under constant
conditions, with a low amplitude and a late phase, with maximal
expression around the end of the light phase. Repressed by light
(PubMed:11743105). In response to blue light and darkness,
phosphorylated, ubiquitinated, and subsequently degraded (at
protein level) in a SPA proteins-dependent manner
(PubMed:20624951, PubMed:25792146, PubMed:22739826,
PubMed:22311776). Transcripts levels oscillate weakly and
proportionally to temperature, but protein levels are stable
(PubMed:23511208). Accumulates in response to low blue light (LBL)
and in low light (PubMed:26724867, PubMed:20935177).
{ECO:0000269|PubMed:11743105, ECO:0000269|PubMed:12578985,
ECO:0000269|PubMed:20624951, ECO:0000269|PubMed:20935177,
ECO:0000269|PubMed:22311776, ECO:0000269|PubMed:22739826,
ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:25792146,
ECO:0000269|PubMed:26724867}.
-!- DOMAIN: The NC80 domain (486-565) contains a major active site
responsible for the signal transduction processes regulating both
hypocotyl inhibition and floral promotion. The C-terminal tail
(564-612) is not required for physiological activity of the
protein.
-!- PTM: Phosphorylated by CK1.3 and CK1.4; in response to blue light.
Required for degradation (PubMed:12066190, PubMed:17438275,
PubMed:17965271, PubMed:9651577, PubMed:25792146,
PubMed:23897926). Adopts an open conformation when phosphorylated
upon photoexcitation and thus interacts with signaling partner
proteins (PubMed:21841916). Not autophosphorylated, even in
complex with FAD cofactor (PubMed:17073458).
{ECO:0000269|PubMed:12066190, ECO:0000269|PubMed:17073458,
ECO:0000269|PubMed:17438275, ECO:0000269|PubMed:17965271,
ECO:0000269|PubMed:23897926, ECO:0000269|PubMed:25792146,
ECO:0000269|PubMed:9651577, ECO:0000303|PubMed:21841916}.
-!- PTM: Ubiquitinated; in response to blue light.
{ECO:0000269|PubMed:17965271, ECO:0000269|PubMed:25792146}.
-!- DISRUPTION PHENOTYPE: Plants show increased root elongation in
blue light (PubMed:16703358, PubMed:21511872). Reduced attenuating
effect of high fluence rates of blue light in the cry1 cry2 double
mutant. Slow rate of curvature at low fluence rates of blue light
in cry1 cry2 (PubMed:12857830). The double mutant cry1 cry2
exhibits a reduced impact of near-null magnetic field on flowering
in lower blue light intensity and short days (PubMed:26095447).
Little detectable phenotype on circadian clock in blue light (BL).
The double mutant cry1 cry2 is impaired in blue light signaling,
resulting in long-period, lower-amplitude oscillations at 12 and
17 degrees Celsius and completely abolishing rhythms at 27 degrees
Celsius (PubMed:23511208). Reduced hyponastic growth (differential
growth-driven upward leaf movement) in low blue light fluence
(PubMed:19558423). The double mutant cry1 cry2 is hyposensitive to
the strigolactone analog GR24 (PubMed:24126495). The mutant cry2
exposed to a background of red light show severely impaired
stomatal opening responses to blue light. The double mutant cry1
cry2 has reduced stomatal conductance, transpiration, and
photosynthesis, particularly under the high irradiance of full
sunlight at midday, associated with elevated abscisic acid levels
(PubMed:22147516). Mutation sel20 suppresses the inhibitory effect
of continuous light (LL) on the hypocotyl elongation of elf3-1.
The double mutant elf3 sel20 exhibits a late-flowering phenotype
(PubMed:21296763). Impaired chromatin decondensation during the
floral transition and in low light conditions (PubMed:20935177).
Increased sensitivity to turnip crinkle virus (TCV) and associated
with reduced HRT levels and stability, and characterized by
hypersensitive response (HR) symptoms (PubMed:20624951).
{ECO:0000269|PubMed:12857830, ECO:0000269|PubMed:16703358,
ECO:0000269|PubMed:19558423, ECO:0000269|PubMed:20624951,
ECO:0000269|PubMed:20935177, ECO:0000269|PubMed:21296763,
ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:22147516,
ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:24126495,
ECO:0000269|PubMed:26095447}.
-!- BIOTECHNOLOGY: The rapid blue light-mediated reversible
interaction between CRY2 and BHLH63/CIB1 is used to design an
optogenetic control of target proteins or organelles.
{ECO:0000269|PubMed:21037589, ECO:0000269|PubMed:22847441,
ECO:0000269|PubMed:23833191, ECO:0000269|PubMed:24718798,
ECO:0000269|PubMed:25963241}.
-!- MISCELLANEOUS: Phosphorylation of the C-terminal tail and
resulting derepression of NC80 domain may both depend on
homodimerization.
-!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a DNA photolyase.
{ECO:0000305|PubMed:9003312}.
-!- SEQUENCE CAUTION:
Sequence=AAT80593.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80594.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80595.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80596.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80597.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80598.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80599.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80600.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80601.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80602.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80603.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80604.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80605.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80606.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80607.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80608.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80609.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80610.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80611.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80612.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80613.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80614.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80615.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80616.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80617.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80618.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80619.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80620.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80621.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80622.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT80623.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD94467.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U62549; AAB04996.1; -; mRNA.
EMBL; U62550; AAB04997.1; -; mRNA.
EMBL; X99061; CAA67508.1; -; Genomic_DNA.
EMBL; U43397; AAD09837.1; -; mRNA.
EMBL; AY057440; AAL16377.1; -; mRNA.
EMBL; AY057441; AAL16378.1; -; Genomic_DNA.
EMBL; AY057442; AAL16379.1; -; Genomic_DNA.
EMBL; EU351967; ABY77601.1; -; Genomic_DNA.
EMBL; EU351968; ABY77602.1; -; Genomic_DNA.
EMBL; EU351969; ABY77603.1; -; Genomic_DNA.
EMBL; EU351970; ABY77604.1; -; Genomic_DNA.
EMBL; EU351971; ABY77605.1; -; Genomic_DNA.
EMBL; EU351972; ABY77606.1; -; Genomic_DNA.
EMBL; EU351973; ABY77607.1; -; Genomic_DNA.
EMBL; EU351974; ABY77608.1; -; Genomic_DNA.
EMBL; EU351975; ABY77609.1; -; Genomic_DNA.
EMBL; EU351976; ABY77610.1; -; Genomic_DNA.
EMBL; EU351977; ABY77611.1; -; Genomic_DNA.
EMBL; EU351978; ABY77612.1; -; Genomic_DNA.
EMBL; EU351979; ABY77613.1; -; Genomic_DNA.
EMBL; EU351980; ABY77614.1; -; Genomic_DNA.
EMBL; EU351981; ABY77615.1; -; Genomic_DNA.
EMBL; EU351982; ABY77616.1; -; Genomic_DNA.
EMBL; EU351983; ABY77617.1; -; Genomic_DNA.
EMBL; EU351984; ABY77618.1; -; Genomic_DNA.
EMBL; EU351985; ABY77619.1; -; Genomic_DNA.
EMBL; EU351986; ABY77620.1; -; Genomic_DNA.
EMBL; EU351987; ABY77621.1; -; Genomic_DNA.
EMBL; EU351988; ABY77622.1; -; Genomic_DNA.
EMBL; EU351989; ABY77623.1; -; Genomic_DNA.
EMBL; EU351990; ABY77624.1; -; Genomic_DNA.
EMBL; EU351991; ABY77625.1; -; Genomic_DNA.
EMBL; EU351993; ABY77627.1; -; Genomic_DNA.
EMBL; EU351992; ABY77626.1; -; Genomic_DNA.
EMBL; EU351994; ABY77628.1; -; Genomic_DNA.
EMBL; EU351995; ABY77629.1; -; Genomic_DNA.
EMBL; EU351996; ABY77630.1; -; Genomic_DNA.
EMBL; EU351997; ABY77631.1; -; Genomic_DNA.
EMBL; EU351998; ABY77632.1; -; Genomic_DNA.
EMBL; AC000104; AAB70435.1; -; Genomic_DNA.
EMBL; CP002684; AEE27692.1; -; Genomic_DNA.
EMBL; CP002684; AEE27693.1; -; Genomic_DNA.
EMBL; BT008576; AAP40403.1; -; mRNA.
EMBL; BT008648; AAP40463.1; -; mRNA.
EMBL; AY576241; AAT80593.1; ALT_INIT; Genomic_DNA.
EMBL; AY576242; AAT80594.1; ALT_INIT; Genomic_DNA.
EMBL; AY576243; AAT80595.1; ALT_INIT; Genomic_DNA.
EMBL; AY576244; AAT80596.1; ALT_INIT; Genomic_DNA.
EMBL; AY576245; AAT80597.1; ALT_INIT; Genomic_DNA.
EMBL; AY576246; AAT80598.1; ALT_INIT; Genomic_DNA.
EMBL; AY576247; AAT80599.1; ALT_INIT; Genomic_DNA.
EMBL; AY576248; AAT80600.1; ALT_INIT; Genomic_DNA.
EMBL; AY576249; AAT80601.1; ALT_INIT; Genomic_DNA.
EMBL; AY576250; AAT80602.1; ALT_INIT; Genomic_DNA.
EMBL; AY576251; AAT80603.1; ALT_INIT; Genomic_DNA.
EMBL; AY576252; AAT80604.1; ALT_INIT; Genomic_DNA.
EMBL; AY576253; AAT80605.1; ALT_INIT; Genomic_DNA.
EMBL; AY576254; AAT80606.1; ALT_INIT; Genomic_DNA.
EMBL; AY576255; AAT80607.1; ALT_INIT; Genomic_DNA.
EMBL; AY576256; AAT80608.1; ALT_INIT; Genomic_DNA.
EMBL; AY576257; AAT80609.1; ALT_INIT; Genomic_DNA.
EMBL; AY576258; AAT80610.1; ALT_INIT; Genomic_DNA.
EMBL; AY576259; AAT80611.1; ALT_INIT; Genomic_DNA.
EMBL; AY576260; AAT80612.1; ALT_INIT; Genomic_DNA.
EMBL; AY576261; AAT80613.1; ALT_INIT; Genomic_DNA.
EMBL; AY576262; AAT80614.1; ALT_INIT; Genomic_DNA.
EMBL; AY576263; AAT80615.1; ALT_INIT; Genomic_DNA.
EMBL; AY576264; AAT80616.1; ALT_INIT; Genomic_DNA.
EMBL; AY576265; AAT80617.1; ALT_INIT; Genomic_DNA.
EMBL; AY576266; AAT80618.1; ALT_INIT; Genomic_DNA.
EMBL; AY576267; AAT80619.1; ALT_INIT; Genomic_DNA.
EMBL; AY576268; AAT80620.1; ALT_INIT; Genomic_DNA.
EMBL; AY576269; AAT80621.1; ALT_INIT; Genomic_DNA.
EMBL; AY576270; AAT80622.1; ALT_INIT; Genomic_DNA.
EMBL; AY576271; AAT80623.1; ALT_INIT; Genomic_DNA.
EMBL; AK220946; BAD94467.1; ALT_INIT; mRNA.
PIR; A86176; A86176.
PIR; S71221; S71221.
RefSeq; NP_171935.1; NM_100320.4.
RefSeq; NP_849588.1; NM_179257.2.
UniGene; At.21976; -.
ProteinModelPortal; Q96524; -.
SMR; Q96524; -.
BioGrid; 24764; 11.
DIP; DIP-33589N; -.
IntAct; Q96524; 2.
MINT; MINT-207946; -.
STRING; 3702.AT1G04400.1; -.
iPTMnet; Q96524; -.
PaxDb; Q96524; -.
EnsemblPlants; AT1G04400.1; AT1G04400.1; AT1G04400.
EnsemblPlants; AT1G04400.2; AT1G04400.2; AT1G04400.
GeneID; 839529; -.
Gramene; AT1G04400.1; AT1G04400.1; AT1G04400.
Gramene; AT1G04400.2; AT1G04400.2; AT1G04400.
KEGG; ath:AT1G04400; -.
Araport; AT1G04400; -.
TAIR; locus:2018254; AT1G04400.
eggNOG; KOG0133; Eukaryota.
eggNOG; COG0415; LUCA.
InParanoid; Q96524; -.
KO; K12119; -.
OMA; NTQGWEP; -.
OrthoDB; EOG0936047F; -.
PhylomeDB; Q96524; -.
BioCyc; ARA:GQT-395-MONOMER; -.
PRO; PR:Q96524; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q96524; baseline and differential.
Genevisible; Q96524; AT.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0009882; F:blue light photoreceptor activity; ISS:TAIR.
GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006325; P:chromatin organization; IMP:TAIR.
GO; GO:0006338; P:chromatin remodeling; IMP:TAIR.
GO; GO:0010617; P:circadian regulation of calcium ion oscillation; IMP:TAIR.
GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
GO; GO:0072387; P:flavin adenine dinucleotide metabolic process; IMP:UniProtKB.
GO; GO:0048574; P:long-day photoperiodism, flowering; IMP:UniProtKB.
GO; GO:0009638; P:phototropism; IMP:UniProtKB.
GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0009909; P:regulation of flower development; IDA:TAIR.
GO; GO:1901371; P:regulation of leaf morphogenesis; IMP:UniProtKB.
GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
GO; GO:2000028; P:regulation of photoperiodism, flowering; IDA:UniProtKB.
GO; GO:0009646; P:response to absence of light; IEP:UniProtKB.
GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:UniProtKB.
GO; GO:1902347; P:response to strigolactone; IMP:UniProtKB.
GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
GO; GO:0010118; P:stomatal movement; IGI:TAIR.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
InterPro; IPR014134; Cryptochrome_pln.
InterPro; IPR018394; DNA_photolyase_1_CS_C.
InterPro; IPR006050; DNA_photolyase_N.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF00875; DNA_photolyase; 1.
Pfam; PF03441; FAD_binding_7; 1.
PRINTS; PR00147; DNAPHOTLYASE.
SUPFAM; SSF48173; SSF48173; 1.
SUPFAM; SSF52425; SSF52425; 1.
TIGRFAMs; TIGR02766; crypt_chrom_pln; 1.
PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
1: Evidence at protein level;
ATP-binding; Chromatin regulator; Chromophore; Complete proteome;
Cytoplasm; FAD; Flavoprotein; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Photoreceptor protein;
Plant defense; Receptor; Reference proteome; Sensory transduction;
Ubl conjugation.
CHAIN 1 612 Cryptochrome-2.
/FTId=PRO_0000085122.
DOMAIN 5 134 Photolyase/cryptochrome alpha/beta.
{ECO:0000255}.
NP_BIND 244 248 FAD. {ECO:0000250|UniProtKB:Q43125}.
NP_BIND 356 357 ATP. {ECO:0000250|UniProtKB:Q43125}.
NP_BIND 387 389 FAD. {ECO:0000250|UniProtKB:Q43125}.
REGION 1 485 CNT2, binds chromophores to sense blue
light and mediate CRY dimerization.
{ECO:0000303|PubMed:25721730}.
REGION 486 612 CCT2/CCE2, mediates blue light signaling.
{ECO:0000269|PubMed:11114337,
ECO:0000303|PubMed:25721730}.
MOTIF 541 555 Nuclear localization signal.
{ECO:0000255|PROSITE-ProRule:PRU00768}.
COMPBIAS 22 27 Poly-Ala. {ECO:0000255}.
COMPBIAS 546 550 Poly-Glu. {ECO:0000255}.
COMPBIAS 566 587 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
METAL 235 235 Magnesium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q43125}.
METAL 243 243 Magnesium 1.
{ECO:0000250|UniProtKB:Q43125}.
METAL 355 355 Magnesium 1; via tele nitrogen.
{ECO:0000250|UniProtKB:Q43125}.
BINDING 232 232 FAD. {ECO:0000250|UniProtKB:Q43125}.
BINDING 356 356 FAD. {ECO:0000250|UniProtKB:Q43125}.
BINDING 406 406 ATP. {ECO:0000250|UniProtKB:Q43125}.
SITE 321 321 Involved in electron transfer from the
protein surface to the FAD cofactor.
{ECO:0000269|PubMed:25428980}.
SITE 374 374 Involved in electron transfer from the
protein surface to the FAD cofactor.
{ECO:0000269|PubMed:25428980}.
SITE 397 397 Involved in electron transfer from the
protein surface to the FAD cofactor.
{ECO:0000269|PubMed:25428980}.
MOD_RES 587 587 Phosphoserine; by CK1.
{ECO:0000269|PubMed:23897926}.
MOD_RES 598 598 Phosphoserine.
{ECO:0000269|PubMed:25792146}.
MOD_RES 599 599 Phosphoserine.
{ECO:0000269|PubMed:25792146}.
MOD_RES 603 603 Phosphothreonine; by CK1.
{ECO:0000269|PubMed:23897926}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000269|PubMed:25792146}.
VARIANT 83 83 I -> V (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 127 127 Q -> S (in strain: cv. Bu-0, cv. Da(1)-
12, cv. Di-G, cv. Landsberg erecta, cv.
Le-0, cv. Lip-0, cv. Mrk-0, cv. Stw-0 and
cv. Ta-0). {ECO:0000305|PubMed:18273534}.
VARIANT 326 326 D -> E (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 367 367 V -> M (in strain: cv. Cvi-0).
{ECO:0000305|PubMed:18273534}.
VARIANT 476 476 T -> I (in strain: cv. Cvi-0).
{ECO:0000305|PubMed:18273534}.
VARIANT 482 482 A -> G (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 498 498 A -> S (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 507 507 F -> L (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 511 511 G -> E (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 543 543 V -> L (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
VARIANT 611 611 C -> Y (in strain: cv. Chi-1, cv. Co-1,
cv. Kon, cv. PHW-1 and cv. Sha).
{ECO:0000305|PubMed:18273534}.
MUTAGEN 321 321 W->A,F: Photochemically inactive in
vitro. Undergo robust light-dependent
photoreduction in an in vivo context via
an alternative electron transport
involving small molecule activators
including ATP, NADH, and NADPH.
{ECO:0000269|PubMed:22139370,
ECO:0000269|PubMed:25428980}.
MUTAGEN 331 331 W->A: Decreased light sensitivity.
Enhanced photoreduction in the presence
of added ATP.
{ECO:0000269|PubMed:25428980}.
MUTAGEN 337 337 G->E: Loss of activity.
{ECO:0000269|PubMed:9565033}.
MUTAGEN 374 374 W->A: Photochemically inactive in vitro.
Undergo robust light-dependent
photoreduction in an in vivo context via
an alternative electron transport
involving small molecule activators
including ATP, NADH, and NADPH. Enhanced
photoreduction in the presence of added
ATP. Constitutive interaction with SPA1
and BHLH63/CIB1.
{ECO:0000269|PubMed:22139370,
ECO:0000269|PubMed:25428980}.
MUTAGEN 374 374 W->F: Photochemically inactive in vitro.
Undergo robust light-dependent
photoreduction in an in vivo context via
an alternative electron transport
involving small molecule activators
including ATP, NADH, and NADPH. Enhanced
photoreduction in the presence of added
ATP. {ECO:0000269|PubMed:22139370,
ECO:0000269|PubMed:25428980}.
MUTAGEN 376 376 W->A: Decreased light sensitivity.
Enhanced photoreduction in the presence
of added ATP.
{ECO:0000269|PubMed:25428980}.
MUTAGEN 377 377 G->R: Constitutive light response.
{ECO:0000269|PubMed:21765176}.
MUTAGEN 387 387 D->A: Impaired FAD-binding leading to
impaired blue light-mediated inhibition
of hypocotyl elongation and loss of blue
light-induced degradation. Disturbed
BHLH63/CIB1 and SPA1 interactions.
{ECO:0000269|PubMed:18988809,
ECO:0000269|PubMed:21514160}.
MUTAGEN 397 397 W->A: Photochemically inactive in vitro.
Undergo robust light-dependent
photoreduction in an in vivo context via
an alternative electron transport
involving small molecule activators
including ATP, NADH, and NADPH.
{ECO:0000269|PubMed:22139370,
ECO:0000269|PubMed:25428980}.
MUTAGEN 397 397 W->F: Photochemically inactive both in
vitro and in vivo.
{ECO:0000269|PubMed:22139370,
ECO:0000269|PubMed:25428980}.
MUTAGEN 399 399 Y->A,F: Impaired ATP-mediated enhanced
photoreduction and decreased affinity for
ATP. {ECO:0000269|PubMed:25428980}.
MUTAGEN 541 541 K->R: Impaired nuclear importation
leading to reduced phosphorylation,
physiological activities, and degradation
in response to blue light. Forms protein
bodies (photobodies) in both the nucleus
and cytosol in response to blue light.
{ECO:0000269|PubMed:22311776}.
MUTAGEN 554 555 KK->RR: Impaired nuclear importation
leading to reduced phosphorylation,
physiological activities, and degradation
in response to blue light. Forms protein
bodies (photobodies) in both the nucleus
and cytosol in response to blue light.
{ECO:0000269|PubMed:22311776}.
MUTAGEN 570 575 SSSSSS->AAAAAA: Reduced blue light-
mediated phosphorylation and impaired
blue light-dependent proteolysis and
hypocotyl inhibition response; when
associated with A-580, A-582, A-584, A-
587, 598-A-A-599 and A-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 570 575 SSSSSS->DDDDDD: Reduced blue light-
mediated phosphorylation and impaired
blue light-dependent proteolysis and
hypocotyl inhibition response; when
associated with D-580, D-582, D-584, D-
587, 598-D-D-599 and D-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 580 580 S->A: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-A--A-573, A-582, A-584, A-587, 598-A-
A-599 and A-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 580 580 S->D: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-D--D-573, D-582, D-584, D-587, 598-D-
D-599 and D-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 582 582 S->A: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-A--A-573, A-580, A-584, A-587, 598-A-
A-599 and A-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 582 582 S->D: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-D--D-573, D-580, D-584, D-587, 598-D-
D-599 and D-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 584 584 S->A: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-A--A-573, A-580, A-582, A-587, 598-A-
A-599 and A-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 584 584 S->D: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-D--D-573, D-580, D-582, D-587, 598-D-
D-599 and D-605.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 587 587 S->A: Impaired regulation of hypocotyl
growth in blue light. Phosphorylated by
CK1 proteins CK1.3 and CK1.4. Reduced
phosphorylation by CK1 proteins CK1.3 and
CK1.4; when associated with A-603.
Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-A--A-573, A-580, A-582, A-584, 598-A-
A-599 and A-605.
{ECO:0000269|PubMed:23897926,
ECO:0000269|PubMed:25792146}.
MUTAGEN 587 587 S->D: Constitutive regulation of
hypocotyl growth in blue light. Reduced
blue light-mediated phosphorylation and
impaired blue light-dependent proteolysis
and hypocotyl inhibition response; when
associated with 570-D--D-573, D-580, D-
582, D-584, 598-D-D-599 and D-605.
{ECO:0000269|PubMed:23897926,
ECO:0000269|PubMed:25792146}.
MUTAGEN 598 599 SS->AA: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-A--A-573, A-580, A-582, A-584, A-587
and A-605. {ECO:0000269|PubMed:25792146}.
MUTAGEN 598 599 SS->DD: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-D--D-573, D-580, D-582, D-584, D-587
and D-605. {ECO:0000269|PubMed:25792146}.
MUTAGEN 603 603 T->A: Impaired regulation of hypocotyl
growth in blue light. Phosphorylated by
CK1 proteins CK1.3 and CK1.4. Reduced
phosphorylation by CK1 proteins CK1.3 and
CK1.4; when associated with A-587.
{ECO:0000269|PubMed:23897926}.
MUTAGEN 603 603 T->D: Constitutive regulation of
hypocotyl growth in blue light.
{ECO:0000269|PubMed:23897926}.
MUTAGEN 605 605 S->A: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-A--A-573, A-580, A-582, A-584, A-587
and 598-A-A-599.
{ECO:0000269|PubMed:25792146}.
MUTAGEN 605 605 S->D: Reduced blue light-mediated
phosphorylation and impaired blue light-
dependent proteolysis and hypocotyl
inhibition response; when associated with
570-D--D-573, D-580, D-582, D-584, D-587
and 598-D-D-599.
{ECO:0000269|PubMed:25792146}.
CONFLICT 78 78 K -> Q (in Ref. 1; AAB04996/AAB04997).
{ECO:0000305}.
CONFLICT 95 95 A -> P (in Ref. 1; AAB04996/AAB04997).
{ECO:0000305}.
CONFLICT 188 188 S -> L (in Ref. 3; AAL16379).
{ECO:0000305}.
CONFLICT 366 366 A -> G (in Ref. 1; AAB04996).
{ECO:0000305}.
CONFLICT 534 534 A -> V (in Ref. 1; AAB04996/AAB04997).
{ECO:0000305}.
CONFLICT 590 590 K -> E (in Ref. 1; CAA67508).
{ECO:0000305}.
CONFLICT 612 612 K -> Q (in Ref. 1; CAA67508).
{ECO:0000305}.
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


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EIAAB38884 Brain-enriched WD repeat-containing protein,Bwd,Rat,Rattus norvegicus,Smu1,Smu-1 suppressor of mec-8 and unc-52 protein homolog,WD40 repeat-containing protein SMU1
EIAAB28903 BCP,Blue cone photoreceptor pigment,Blue-sensitive opsin,BOP,Homo sapiens,Human,OPN1SW,Short-wave-sensitive opsin 1
EIAAB28902 BCP,Blue cone photoreceptor pigment,Blue-sensitive opsin,BOP,Bos taurus,Bovine,OPN1SW,Short-wave-sensitive opsin 1


 

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