CRY1_ARATH
ID CRY1_ARATH Reviewed; 681 AA.
AC Q43125; Q43126; Q8L7Y1; Q9ASZ2; Q9M0S9; Q9ZPF0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Cryptochrome-1 {ECO:0000303|PubMed:8953250};
DE Short=AtCry {ECO:0000303|PubMed:22421133};
DE Short=Atcry1 {ECO:0000303|PubMed:8953250};
DE AltName: Full=Blue light photoreceptor {ECO:0000303|PubMed:7756321};
DE AltName: Full=Protein BLUE LIGHT UNINHIBITED 1 {ECO:0000303|PubMed:12324610};
DE AltName: Full=Protein ELONGATED HYPOCOTYL 4 {ECO:0000303|PubMed:8232555};
DE AltName: Full=Protein OUT OF PHASE 2;
DE Short=OOP2;
GN Name=CRY1 {ECO:0000303|PubMed:8953250};
GN Synonyms=BLU1 {ECO:0000303|PubMed:12324610},
GN HY4 {ECO:0000303|PubMed:8232555};
GN OrderedLocusNames=At4g08920 {ECO:0000312|Araport:AT4G08920};
GN ORFNames=T3H13.14 {ECO:0000312|EMBL:AAD17364.1},
GN T3H13.5 {ECO:0000312|EMBL:AAD17364.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8232555; DOI=10.1038/366162a0;
RA Ahmad M., Cashmore A.R.;
RT "HY4 gene of A. thaliana encodes a protein with characteristics of a blue-
RT light photoreceptor.";
RL Nature 366:162-166(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12324610; DOI=10.2307/3869250;
RA Liscum E., Hangarter R.P.;
RT "Arabidopsis mutants lacking blue light-dependent inhibition of hypocotyl
RT elongation.";
RL Plant Cell 3:685-694(1991).
RN [6]
RP FUNCTION, AND COFACTOR.
RX PubMed=7756321; DOI=10.1021/bi00020a037;
RA Malhotra K., Kim S.-T., Batschauer A., Dawut L., Sancar A.;
RT "Putative blue-light photoreceptors from Arabidopsis thaliana and Sinapis
RT alba with a high degree of sequence homology to DNA photolyase contain the
RT two photolyase cofactors but lack DNA repair activity.";
RL Biochemistry 34:6892-6899(1995).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-220; GLY-283;
RP GLY-340; GLY-347; GLU-515; GLU-531; PRO-549; GLU-559; ARG-576; ARG-581 AND
RP ARG-611.
RX PubMed=8528277; DOI=10.1046/j.1365-313x.1995.08050653.x;
RA Ahmad M., Lin C., Cashmore A.R.;
RT "Mutations throughout an Arabidopsis blue-light photoreceptor impair blue-
RT light-responsive anthocyanin accumulation and inhibition of hypocotyl
RT elongation.";
RL Plant J. 8:653-658(1995).
RN [8]
RP CHARACTERIZATION.
RX PubMed=8953250; DOI=10.1046/j.1365-313x.1996.10050893.x;
RA Lin C., Ahmad M., Cashmore A.R.;
RT "Arabidopsis cryptochrome 1 is a soluble protein mediating blue light-
RT dependent regulation of plant growth and development.";
RL Plant J. 10:893-902(1996).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLY-340.
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 [10]
RP INTERACTION WITH PHYA, AND 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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9733523; DOI=10.1104/pp.118.1.27;
RA Neff M.M., Chory J.;
RT "Genetic interactions between phytochrome A, phytochrome B, and
RT cryptochrome 1 during Arabidopsis development.";
RL Plant Physiol. 118:27-35(1998).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9765547; DOI=10.1104/pp.118.2.609;
RA Parks B.M., Cho M.H., Spalding E.P.;
RT "Two genetically separable phases of growth inhibition induced by blue
RT light in Arabidopsis seedlings.";
RL Plant Physiol. 118:609-615(1998).
RN [13]
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 [14]
RP INTERACTION WITH ADO1.
RX PubMed=11260718; DOI=10.1038/35068589;
RA Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M., Ecker J.R.,
RA Cashmore A.R.;
RT "An Arabidopsis circadian clock component interacts with both CRY1 and
RT phyB.";
RL Nature 410:487-490(2001).
RN [15]
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 [16]
RP INTERACTION WITH COP1.
RX PubMed=11752373; DOI=10.2307/3871520;
RA Yang H.-Q., Tang R.-H., Cashmore A.R.;
RT "The signaling mechanism of Arabidopsis CRY1 involves direct interaction
RT with COP1.";
RL Plant Cell 13:2573-2587(2001).
RN [17]
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 [18]
RP PHOSPHORYLATION.
RX PubMed=12846824; DOI=10.1046/j.1432-1033.2003.03691.x;
RA Bouly J.-P., Giovani B., Djamei A., Mueller M., Zeugner A., Dudkin E.A.,
RA Batschauer A., Ahmad M.;
RT "Novel ATP-binding and autophosphorylation activity associated with
RT Arabidopsis and human cryptochrome-1.";
RL Eur. J. Biochem. 270:2921-2928(2003).
RN [19]
RP PHOSPHORYLATION.
RX PubMed=14523249; DOI=10.1105/tpc013011;
RA Shalitin D., Yu X., Maymon M., Mockler T., Lin C.;
RT "Blue light-dependent in vivo and in vitro phosphorylation of Arabidopsis
RT cryptochrome 1.";
RL Plant Cell 15:2421-2429(2003).
RN [20]
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 [21]
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 [22]
RP ACTIVITY REGULATION.
RX PubMed=15751956; DOI=10.1021/bi047545g;
RA Partch C.L., Clarkson M.W., Ozgur S., Lee A.L., Sancar A.;
RT "Role of structural plasticity in signal transduction by the cryptochrome
RT blue-light photoreceptor.";
RL Biochemistry 44:3795-3805(2005).
RN [23]
RP SUBUNIT, AND MUTAGENESIS OF SER-66; GLY-347 AND ALA-462.
RX PubMed=15805487; DOI=10.1105/tpc.104.029645;
RA Sang Y., Li Q.-H., Rubio V., Zhang Y.-C., Mao J., Deng X.-W., Yang H.-Q.;
RT "N-terminal domain-mediated homodimerization is required for photoreceptor
RT activity of Arabidopsis CRYPTOCHROME 1.";
RL Plant Cell 17:1569-1584(2005).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=15610358; DOI=10.1111/j.1365-313x.2004.02281.x;
RA Koroleva O.A., Tomlinson M.L., Leader D., Shaw P., Doonan J.H.;
RT "High-throughput protein localization in Arabidopsis using Agrobacterium-
RT mediated transient expression of GFP-ORF fusions.";
RL Plant J. 41:162-174(2005).
RN [25]
RP AUTOPHOSPHORYLATION, 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 [26]
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 [27]
RP FUNCTION IN PCD, AND DISRUPTION PHENOTYPE.
RX PubMed=17075038; DOI=10.1073/pnas.0608139103;
RA Danon A., Coll N.S., Apel K.;
RT "Cryptochrome-1-dependent execution of programmed cell death induced by
RT singlet oxygen in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17036-17041(2006).
RN [28]
RP MUTAGENESIS OF ASP-21; SER-286; GLY-340 AND GLU-623.
RC STRAIN=cv. Columbia;
RX PubMed=18065688; DOI=10.1105/tpc.107.054312;
RA Ruckle M.E., DeMarco S.M., Larkin R.M.;
RT "Plastid signals remodel light signaling networks and are essential for
RT efficient chloroplast biogenesis in Arabidopsis.";
RL Plant Cell 19:3944-3960(2007).
RN [29]
RP SUBCELLULAR LOCATION.
RX PubMed=18003924; DOI=10.1073/pnas.0705082104;
RA Wu G., Spalding E.P.;
RT "Separate functions for nuclear and cytoplasmic cryptochrome 1 during
RT photomorphogenesis of Arabidopsis seedlings.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18813-18818(2007).
RN [30]
RP FUNCTION.
RX PubMed=18397371; DOI=10.1111/j.1365-313x.2008.03508.x;
RA Hong S.H., Kim H.J., Ryu J.S., Choi H., Jeong S., Shin J., Choi G.,
RA Nam H.G.;
RT "CRY1 inhibits COP1-mediated degradation of BIT1, a MYB transcription
RT factor, to activate blue light-dependent gene expression in Arabidopsis.";
RL Plant J. 55:361-371(2008).
RN [31]
RP ATP BINDING.
RX PubMed=19327354; DOI=10.1016/j.febslet.2009.03.040;
RA Burney S., Hoang N., Caruso M., Dudkin E.A., Ahmad M., Bouly J.-P.;
RT "Conformational change induced by ATP binding correlates with enhanced
RT biological function of Arabidopsis cryptochrome.";
RL FEBS Lett. 583:1427-1433(2009).
RN [32]
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 [33]
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 [34]
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 [35]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20133010; DOI=10.1016/j.jplph.2009.12.003;
RA Zeng J., Wang Q., Lin J., Deng K., Zhao X., Tang D., Liu X.;
RT "Arabidopsis cryptochrome-1 restrains lateral roots growth by inhibiting
RT auxin transport.";
RL J. Plant Physiol. 167:670-673(2010).
RN [36]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=20053798; DOI=10.1093/mp/ssp107;
RA Wu L., Yang H.-Q.;
RT "CRYPTOCHROME 1 is implicated in promoting R protein-mediated plant
RT resistance to Pseudomonas syringae in Arabidopsis.";
RL Mol. Plant 3:539-548(2010).
RN [37]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=20668058; DOI=10.1104/pp.110.160820;
RA Sellaro R., Crepy M., Trupkin S.A., Karayekov E., Buchovsky A.S., Rossi C.,
RA Casal J.J.;
RT "Cryptochrome as a sensor of the blue/green ratio of natural radiation in
RT Arabidopsis.";
RL Plant Physiol. 154:401-409(2010).
RN [38]
RP MUTAGENESIS OF LEU-407.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=20926618; DOI=10.1104/pp.110.160895;
RA Exner V., Alexandre C., Rosenfeldt G., Alfarano P., Nater M., Caflisch A.,
RA Gruissem W., Batschauer A., Hennig L.;
RT "A gain-of-function mutation of Arabidopsis cryptochrome1 promotes
RT flowering.";
RL Plant Physiol. 154:1633-1645(2010).
RN [39]
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 [40]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH SPA1 AND SPA4.
RX PubMed=21511871; DOI=10.1101/gad.2025011;
RA Liu B., Zuo Z., Liu H., Liu X., Lin C.;
RT "Arabidopsis cryptochrome 1 interacts with SPA1 to suppress COP1 activity
RT in response to blue light.";
RL Genes Dev. 25:1029-1034(2011).
RN [41]
RP FUNCTION.
RX PubMed=21467031; DOI=10.1074/jbc.m111.228940;
RA Mueller P., Ahmad M.;
RT "Light-activated cryptochrome reacts with molecular oxygen to form a
RT flavin-superoxide radical pair consistent with magnetoreception.";
RL J. Biol. Chem. 286:21033-21040(2011).
RN [42]
RP FUNCTION, AND MUTAGENESIS OF TRP-324.
RX PubMed=21875594; DOI=10.1016/j.jmb.2011.08.031;
RA Kondoh M., Shiraishi C., Mueller P., Ahmad M., Hitomi K., Getzoff E.D.,
RA Terazima M.;
RT "Light-induced conformational changes in full-length Arabidopsis thaliana
RT cryptochrome.";
RL J. Mol. Biol. 413:128-137(2011).
RN [43]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21265897; DOI=10.1111/j.1365-313x.2010.04434.x;
RA Foreman J., Johansson H., Hornitschek P., Josse E.-M., Fankhauser C.,
RA Halliday K.J.;
RT "Light receptor action is critical for maintaining plant biomass at warm
RT ambient temperatures.";
RL Plant J. 65:441-452(2011).
RN [44]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21457375; DOI=10.1111/j.1365-313x.2011.04598.x;
RA Keller M.M., Jaillais Y., Pedmale U.V., Moreno J.E., Chory J.,
RA Ballare C.L.;
RT "Cryptochrome 1 and phytochrome B control shade-avoidance responses in
RT Arabidopsis via partially independent hormonal cascades.";
RL Plant J. 67:195-207(2011).
RN [45]
RP MUTAGENESIS OF ASP-396.
RX PubMed=22890584; DOI=10.1002/anie.201203476;
RA Burney S., Wenzel R., Kottke T., Roussel T., Hoang N., Bouly J.P.,
RA Bittl R., Heberle J., Ahmad M.;
RT "Single amino acid substitution reveals latent photolyase activity in
RT Arabidopsis cry1.";
RL Angew. Chem. Int. Ed. 51:9356-9360(2012).
RN [46]
RP INTERACTION WITH PHYB, AND MUTAGENESIS OF LEU-407.
RX PubMed=22577138; DOI=10.1074/jbc.m112.360545;
RA Hughes R.M., Vrana J.D., Song J., Tucker C.L.;
RT "Light-dependent, dark-promoted interaction between Arabidopsis
RT cryptochrome 1 and phytochrome B proteins.";
RL J. Biol. Chem. 287:22165-22172(2012).
RN [47]
RP MUTAGENESIS OF GLY-380, AND SUBCELLULAR LOCATION.
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 [48]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22786870; DOI=10.1105/tpc.112.100099;
RA Shaikhali J., de Dios Barajas-Lopez J., Oetvoes K., Kremnev D.,
RA Garcia A.S., Srivastava V., Wingsle G., Bako L., Strand A.;
RT "The CRYPTOCHROME1-dependent response to excess light is mediated through
RT the transcriptional activators ZINC FINGER PROTEIN EXPRESSED IN
RT INFLORESCENCE MERISTEM LIKE1 and ZML2 in Arabidopsis.";
RL Plant Cell 24:3009-3025(2012).
RN [49]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=22855128; DOI=10.1007/s11103-012-9950-x;
RA Fox A.R., Soto G.C., Jones A.M., Casal J.J., Muschietti J.P.,
RA Mazzella M.A.;
RT "cry1 and GPA1 signaling genetically interact in hook opening and
RT anthocyanin synthesis in Arabidopsis.";
RL Plant Mol. Biol. 80:315-324(2012).
RN [50]
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 [51]
RP FUNCTION.
RX PubMed=22421133; DOI=10.1073/pnas.1118959109;
RA Maeda K., Robinson A.J., Henbest K.B., Hogben H.J., Biskup T., Ahmad M.,
RA Schleicher E., Weber S., Timmel C.R., Hore P.J.;
RT "Magnetically sensitive light-induced reactions in cryptochrome are
RT consistent with its proposed role as a magnetoreceptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:4774-4779(2012).
RN [52]
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 [53]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22681544; DOI=10.1111/j.1365-3040.2012.02554.x;
RA Nameth B., Dinka S.J., Chatfield S.P., Morris A., English J., Lewis D.,
RA Oro R., Raizada M.N.;
RT "The shoot regeneration capacity of excised Arabidopsis cotyledons is
RT established during the initial hours after injury and is modulated by a
RT complex genetic network of light signalling.";
RL Plant Cell Environ. 36:68-86(2013).
RN [54]
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 [55]
RP FUNCTION.
RX PubMed=25157750; DOI=10.1021/ja506084f;
RA Cailliez F., Mueller P., Gallois M., de la Lande A.;
RT "ATP binding and aspartate protonation enhance photoinduced electron
RT transfer in plant cryptochrome.";
RL J. Am. Chem. Soc. 136:12974-12986(2014).
RN [56]
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 [57]
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 [58]
RP INTERACTION WITH TCP2.
RX PubMed=26596765; DOI=10.1093/jxb/erv495;
RA He Z., Zhao X., Kong F., Zuo Z., Liu X.;
RT "TCP2 positively regulates HY5/HYH and photomorphogenesis in Arabidopsis.";
RL J. Exp. Bot. 67:775-785(2015).
RN [59]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-66; GLY-220; GLY-283;
RP GLY-337; GLY-340; GLY-347 AND ALA-462, AND 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 [60]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=25728686; DOI=10.1111/nph.13341;
RA Consentino L., Lambert S., Martino C., Jourdan N., Bouchet P.-E.,
RA Witczak J., Castello P., El-Esawi M., Corbineau F., d'Harlingue A.,
RA Ahmad M.;
RT "Blue-light dependent reactive oxygen species formation by Arabidopsis
RT cryptochrome may define a novel evolutionarily conserved signaling
RT mechanism.";
RL New Phytol. 206:1450-1462(2015).
RN [61]
RP FUNCTION, AND MUTAGENESIS OF TRP-324 AND TRP-400.
RX PubMed=26313597; DOI=10.1080/15592324.2015.1063758;
RA El-Esawi M., Glascoe A., Engle D., Ritz T., Link J., Ahmad M.;
RT "Cellular metabolites modulate in vivo signaling of Arabidopsis
RT cryptochrome-1.";
RL Plant Signal. Behav. 10:E1063758-E1063758(2015).
RN [62]
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 [63]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-509 IN COMPLEX WITH ATP; FAD
RP AND MAGNESIUM, DISULFIDE BONDS, AND BINDING SITES.
RX PubMed=15299148; DOI=10.1073/pnas.0404851101;
RA Brautigam C.A., Smith B.S., Ma Z., Palnitkar M., Tomchick D.R., Machius M.,
RA Deisenhofer J.;
RT "Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12142-12147(2004).
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-324, W-377
CC and W-400), accompanied by a large conformational change upon
CC photoexcitation, 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 5 minutes (PubMed:26313597,
CC PubMed:25157750, PubMed:23398192, PubMed:21875594, PubMed:21467031).
CC Also involved in the detection of blue/green ratio in light (shade
CC under leaf canopies) and subsequent adaptations on plant growth and
CC development (PubMed:20668058). In darkness, the dark reoxidation of
CC flavin occurs and leads to inactivated state (PubMed:21467031,
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). When activated by high-intensity
CC blue light, catalyzes direct enzymatic conversion of molecular oxygen
CC O(2) to reactive oxygen species (ROS) and hydrogen peroxide H(2)O(2) in
CC vitro. ROS accumulation upon activation by blue light leads to cell
CC death in protoplasts (PubMed:25728686). Seems essential for blue-light-
CC triggered and singlet oxygen-mediated programmed cell death (PCD)
CC (PubMed:17075038). Required for the induction of nuclear genes encoding
CC photoprotective components by GATA24 and GATA28 in extreme light
CC intensities that exceed the electron utilization capacity of the
CC chloroplast (PubMed:22786870). Involved in shortening the circadian
CC clock period, especially at 27 degrees Celsius, in blue light (BL) and
CC required to maintain clock genes expression rhythm (PubMed:23511208).
CC Mediates blue light-induced gene expression and hypocotyl elongation
CC through the inhibition of COP1-mediated degradation of the
CC transcription factors BIT1 and HY5 and via the activation of anion
CC channels at the plasma membrane, probably via auxin signaling
CC (PubMed:21511872, PubMed:21511871, PubMed:16093319, PubMed:18397371,
CC PubMed:12324610, PubMed:8528277, PubMed:9765547, PubMed:25721730).
CC Required for the hypocotyl hook formation in darkness
CC (PubMed:22855128). Involved in blue light-dependent stomatal opening,
CC CHS gene expression, transpiration, inhibition of stem growth and
CC increase of root growth, probably by regulating abscisic acid (ABA)
CC (PubMed:22147516, PubMed:16093319, PubMed:16703358, PubMed:7756321,
CC PubMed:9565033). Prevents lateral roots growth by inhibiting auxin
CC transport (PubMed:20133010). Necessary for shade avoidance syndrome
CC (SAS), characterized by leaf hyponasty and reduced lamina/petiole
CC ratio, when exposed to blue light attenuation (PubMed:21457375).
CC Together with phototropins, involved in phototropism regulation by
CC various blue light fluence; blue light attenuates phototropism in high
CC fluence rates (100 umol.m-2.s-1) but enhances phototropism in low
CC fluence rates (<1.0 umol.m-2.s-1) (PubMed:12857830). Required for
CC blue/UV-A wavelengths-mediated inhibition of explants shoot
CC regeneration in vitro (e.g. new shoot apical meristems regeneration
CC from excised cotyledons) (PubMed:22681544). Modulates anthocyanin
CC accumulation in a PHYA-dependent manner in far-red-light. Acts as a
CC PHYA/PHYB-dependent modulator of chlorophyll accumulation in red light.
CC Contributes to most blue light deetiolation responses (PubMed:9733523,
CC PubMed:8528277). May act as a chemical magnetoreceptor, via
CC magnetically sensitive kinetics and quantum yields of photo-induced
CC flavin / tryptophan radical pairs (PubMed:22421133). The effect of
CC near-null magnetic field on flowering is altered by changes of blue
CC light cycle and intensity in a CRY1/CRY2-dependent manner
CC (PubMed:26095447). Involved in the strigolactone signaling that
CC regulates hypocotyl growth in response to blue light (PubMed:24126495).
CC Modulates temperature-dependent growth and physiology maintenance,
CC especially at warm ambient temperatures, via HFR1-dependent activity
CC (PubMed:21265897). {ECO:0000269|PubMed:12324610,
CC ECO:0000269|PubMed:12857830, ECO:0000269|PubMed:16093319,
CC ECO:0000269|PubMed:16703358, ECO:0000269|PubMed:17075038,
CC ECO:0000269|PubMed:18397371, ECO:0000269|PubMed:19558423,
CC ECO:0000269|PubMed:20133010, ECO:0000269|PubMed:20668058,
CC ECO:0000269|PubMed:21265897, ECO:0000269|PubMed:21457375,
CC ECO:0000269|PubMed:21467031, ECO:0000269|PubMed:21511871,
CC ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:21875594,
CC ECO:0000269|PubMed:22147516, ECO:0000269|PubMed:22421133,
CC ECO:0000269|PubMed:22681544, ECO:0000269|PubMed:22786870,
CC ECO:0000269|PubMed:22855128, ECO:0000269|PubMed:23398192,
CC ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:24126495,
CC ECO:0000269|PubMed:25157750, ECO:0000269|PubMed:25721730,
CC ECO:0000269|PubMed:25728686, ECO:0000269|PubMed:26095447,
CC ECO:0000269|PubMed:26313597, ECO:0000269|PubMed:26724867,
CC ECO:0000269|PubMed:7756321, ECO:0000269|PubMed:8528277,
CC ECO:0000269|PubMed:9565033, ECO:0000269|PubMed:9733523,
CC ECO:0000269|PubMed:9765547, ECO:0000303|PubMed:21841916}.
CC -!- FUNCTION: Implicated in promoting R protein-mediated resistance to
CC Pseudomonas syringae pv. tomato (Pst.) DC3000 under continuous light
CC conditions. Promotes systemic acquired resistance (SAR) and PR gene
CC expression triggered by P. syringae. {ECO:0000269|PubMed:20053798}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17073458, ECO:0000269|PubMed:7756321};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17073458,
CC ECO:0000269|PubMed:7756321};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000269|PubMed:7756321};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000269|PubMed:7756321};
CC -!- ACTIVITY REGULATION: Light exposure induces a conformational change in
CC the C-terminal domain CCT1 required for activity.
CC {ECO:0000269|PubMed:15751956}.
CC -!- SUBUNIT: Homodimer. Interacts with ADO1, COP1 and PHYA. Interacts
CC specifically with the dark/far-red (Pr) state of PHYB, but not with the
CC red light-activated (Pfr) (PubMed:22577138). Interacts with PIF4 and
CC PIF5 in the nucleus in response to low blue light (LBL)
CC (PubMed:26724867). Binds to SPA1 and SPA4 in response to blue light,
CC this interaction prevents SPA1/COP1 complex formation and thus avoid
CC COP1-dependent degradation of the transcription factor HY5 by the
CC proteasome and promotes hypocotyl elongation (PubMed:21511872,
CC PubMed:21511871). Interacts with TCP2 (PubMed:26596765). Binding to ATP
CC mediates conformational changes which facilitate flavin binding
CC (PubMed:19327354, PubMed:17073458). {ECO:0000269|PubMed:11260718,
CC ECO:0000269|PubMed:11509693, ECO:0000269|PubMed:11752373,
CC ECO:0000269|PubMed:15299148, ECO:0000269|PubMed:15805487,
CC ECO:0000269|PubMed:17073458, ECO:0000269|PubMed:19327354,
CC ECO:0000269|PubMed:21511871, ECO:0000269|PubMed:21511872,
CC ECO:0000269|PubMed:22577138, ECO:0000269|PubMed:26596765,
CC ECO:0000269|PubMed:26724867, ECO:0000269|PubMed:9651577}.
CC -!- INTERACTION:
CC Q43125; P43254: COP1; NbExp=4; IntAct=EBI-300703, EBI-301649;
CC Q43125; Q43125: CRY1; NbExp=6; IntAct=EBI-300703, EBI-300703;
CC Q43125; P06593: PHYA3; Xeno; NbExp=2; IntAct=EBI-300703, EBI-630413;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18003924}. Nucleus
CC {ECO:0000269|PubMed:15610358, ECO:0000269|PubMed:18003924,
CC ECO:0000269|PubMed:26724867}. Nucleus, PML body
CC {ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:21765176}. Note=The
CC nuclear pool is involved in hypocotyl and petiole growth inhibition and
CC anthocyanin production, while the cytoplasmic pool is involved in root
CC growth and cotyledon expansion (PubMed:18003924). Present in nuclear
CC bodies (NBs) (PubMed:21511872, PubMed:21765176).
CC {ECO:0000269|PubMed:18003924, ECO:0000269|PubMed:21511872,
CC ECO:0000269|PubMed:21765176}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:8953250). Expressed in the
CC aerial tissues (e.g. cotyledons and leaf primordia), but not detected
CC in the roots (PubMed:11743105). {ECO:0000269|PubMed:11743105,
CC ECO:0000269|PubMed:8953250}.
CC -!- INDUCTION: Expression levels display circadian oscillations under
CC constant conditions, with a high amplitude and an early phase, with
CC maximal expression around 4-6 hours of the light phase. Induced by
CC light (PubMed:11743105). Transcripts levels oscillate weakly and
CC proportionally to temperature, but protein levels are stable, with
CC higher levels at low temperature (12 degrees Celsius)
CC (PubMed:23511208). Accumulates in response to low blue light (LBL)
CC (PubMed:26724867). {ECO:0000269|PubMed:11743105,
CC ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:26724867}.
CC -!- DOMAIN: The N-terminal domain CNT1 (1-489) is sufficient for
CC autophosphorylation and is required for dimerization. The C-terminal
CC domain CCT1 (490-681) of the homodimer binds to COP1.
CC -!- PTM: Autophosphorylated; in response to blue light and when in complex
CC with FAD cofactor (PubMed:12846824, PubMed:14523249, PubMed:9651577,
CC PubMed:17073458). Kinase activity is optimal in the presence of
CC magnesium ions, about 30 percent of the optimal activity in the
CC presence of manganese ions, but inactive with calcium ions
CC (PubMed:17073458). Adopts an open conformation when phosphorylated upon
CC photoexcitation and thus interacts with signaling partner proteins
CC (PubMed:21841916). {ECO:0000269|PubMed:12846824,
CC ECO:0000269|PubMed:14523249, ECO:0000269|PubMed:17073458,
CC ECO:0000269|PubMed:9651577, ECO:0000303|PubMed:21841916}.
CC -!- DISRUPTION PHENOTYPE: Prevents the shortening of period at 27 degrees
CC Celsius, resulting in a long period phenotype. The double mutant cry1
CC cry2 is impaired in blue light signaling, resulting in long-period,
CC lower-amplitude oscillations at 12 and 17 degrees Celsius and
CC completely abolishing rhythms at 27 degrees Celsius (PubMed:23511208).
CC Plants show reduced root and hypocotyl elongation in an anion channels
CC activation-dependent manner at the plasma membrane, as well a reduced
CC anthocyanin accumulation in blue light (PubMed:8528277,
CC PubMed:12324610, PubMed:16703358, PubMed:21511871, PubMed:21511872,
CC PubMed:9765547). Impaired blue/UV-A wavelengths-mediated inhibition of
CC shoot regeneration (PubMed:22681544). Impaired detection of blue/green
CC ratio in light leading to abnormal inhibition of hypocotyl growth
CC (PubMed:20668058). Reduced attenuating effect of high fluence rates of
CC blue light. This phenotype is stronger in the cry1 cry2 double mutant.
CC Slow rate of curvature at low fluence rates of blue light in cry1 cry2
CC (PubMed:12857830). Lower anthocyanin accumulation in the phyB cry1
CC double mutant exposed to far-red light. Reduced chlorophyll levels in
CC the phyB cry1 double mutant exposed to red light. In blue light,
CC impaired cotyledon unfolding and smaller cotyledons, longer hypocotyls
CC and less chlorophyll (PubMed:9733523). Impaired accumulation of
CC reactive oxygen species (ROS) in double mutant cry1 cry2 exposed to
CC high-intensity blue light (PubMed:25728686). Altered blue-light-
CC triggered and singlet oxygen-mediated programmed cell death (PCD)
CC (PubMed:17075038). 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). Reduced hyponastic growth
CC (differential growth-driven upward leaf movement) in low blue light
CC fluence (PubMed:19558423). The double mutant cry1 cry2 is hyposensitive
CC to the strigolactone analog GR24 (PubMed:24126495). The mutant cry1
CC exposed to a background of red light show severely impaired stomatal
CC opening responses to blue light. The double mutant cry1 cry2 has
CC reduced stomatal conductance, transpiration, and photosynthesis,
CC particularly under the high irradiance of full sunlight at midday,
CC associated with elevated abscisic acid levels (PubMed:22147516). The
CC cry1 mutants grown in complete darkness have premature opening of the
CC hypocotyl hook (PubMed:22855128). Reduced expression of nuclear genes
CC encoding photoprotective components in response to extreme high light
CC (PubMed:22786870). Reduced shade avoidance syndrome (SAS) when exposed
CC to blue light attenuation (PubMed:21457375). Reduced growth at warm
CC ambient temperatures (PubMed:21265897). Down-regulated local resistance
CC and systemic acquired resistance (SAR) to Pseudomonas syringae pv.
CC tomato (Pst.) DC3000 under continuous light conditions, leading to
CC pathogen proliferation (PubMed:20053798). When grown in blue light,
CC increased growth of lateral roots and reduced sensitivity to auxin
CC (IAA) on this phenotype (PubMed:20133010).
CC {ECO:0000269|PubMed:12324610, ECO:0000269|PubMed:12857830,
CC ECO:0000269|PubMed:16703358, ECO:0000269|PubMed:17075038,
CC ECO:0000269|PubMed:19558423, ECO:0000269|PubMed:20053798,
CC ECO:0000269|PubMed:20133010, ECO:0000269|PubMed:20668058,
CC ECO:0000269|PubMed:21265897, ECO:0000269|PubMed:21457375,
CC ECO:0000269|PubMed:21511871, ECO:0000269|PubMed:21511872,
CC ECO:0000269|PubMed:22147516, ECO:0000269|PubMed:22681544,
CC ECO:0000269|PubMed:22786870, ECO:0000269|PubMed:22855128,
CC ECO:0000269|PubMed:23511208, ECO:0000269|PubMed:24126495,
CC ECO:0000269|PubMed:25728686, ECO:0000269|PubMed:26095447,
CC ECO:0000269|PubMed:8528277, ECO:0000269|PubMed:9733523,
CC ECO:0000269|PubMed:9765547}.
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:8232555}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB28725.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD17364.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78016.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; S66907; AAB28724.1; -; mRNA.
DR EMBL; S66909; AAB28725.2; ALT_FRAME; mRNA.
DR EMBL; AF128396; AAD17364.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161513; CAB78016.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82696.1; -; Genomic_DNA.
DR EMBL; AF361588; AAK32756.1; -; mRNA.
DR EMBL; AY124863; AAM70572.1; -; mRNA.
DR PIR; H85089; H85089.
DR PIR; S39058; S39058.
DR RefSeq; NP_567341.1; NM_116961.5.
DR PDB; 1U3C; X-ray; 2.60 A; A=1-509.
DR PDB; 1U3D; X-ray; 2.45 A; A=1-509.
DR PDB; 6QTW; X-ray; 1.39 A; B=544-553.
DR PDBsum; 1U3C; -.
DR PDBsum; 1U3D; -.
DR PDBsum; 6QTW; -.
DR AlphaFoldDB; Q43125; -.
DR SMR; Q43125; -.
DR BioGRID; 11769; 7.
DR IntAct; Q43125; 3.
DR MINT; Q43125; -.
DR STRING; 3702.AT4G08920.1; -.
DR iPTMnet; Q43125; -.
DR PaxDb; Q43125; -.
DR PRIDE; Q43125; -.
DR ProteomicsDB; 224510; -.
DR EnsemblPlants; AT4G08920.1; AT4G08920.1; AT4G08920.
DR GeneID; 826470; -.
DR Gramene; AT4G08920.1; AT4G08920.1; AT4G08920.
DR KEGG; ath:AT4G08920; -.
DR Araport; AT4G08920; -.
DR TAIR; locus:2138728; AT4G08920.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_5_0_1; -.
DR InParanoid; Q43125; -.
DR OMA; YIWAPEE; -.
DR OrthoDB; 378952at2759; -.
DR EvolutionaryTrace; Q43125; -.
DR PRO; PR:Q43125; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q43125; baseline and differential.
DR Genevisible; Q43125; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA: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:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0046283; P:anthocyanin-containing compound metabolic process; IMP:UniProtKB.
DR GO; GO:0060918; P:auxin transport; IMP:UniProtKB.
DR GO; GO:0009785; P:blue light signaling pathway; TAS: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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009583; P:detection of light stimulus; IMP:TAIR.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0072387; P:flavin adenine dinucleotide metabolic process; IDA:UniProtKB.
DR GO; GO:1901332; P:negative regulation of lateral root development; IMP:UniProtKB.
DR GO; GO:0009640; P:photomorphogenesis; IMP:TAIR.
DR GO; GO:0010117; P:photoprotection; IMP:UniProtKB.
DR GO; GO:0009638; P:phototropism; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:1901529; P:positive regulation of anion channel activity; IMP:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1902448; P:positive regulation of shade avoidance; IMP:UniProtKB.
DR GO; GO:1901672; P:positive regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IDA:UniProtKB.
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:2000377; P:regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:2000652; P:regulation of secondary cell wall biogenesis; IDA:TAIR.
DR GO; GO:0051510; P:regulation of unidimensional cell growth; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IMP:UniProtKB.
DR GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
DR GO; GO:0010218; P:response to far red light; IMP:UniProtKB.
DR GO; GO:0009644; P:response to high light intensity; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR GO; GO:0010244; P:response to low fluence blue light stimulus by blue low-fluence system; IMP:UniProtKB.
DR GO; GO:0071000; P:response to magnetism; IDA:UniProtKB.
DR GO; GO:0010114; P:response to red light; 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:0010343; P:singlet oxygen-mediated programmed cell death; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:UniProtKB.
DR DisProt; DP00474; -.
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; IPR020978; Cryptochrome_C.
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; PF12546; Cryptochrome_C; 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; Apoptosis; ATP-binding; Chromophore; Cytoplasm;
KW Disulfide bond; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Photoreceptor protein;
KW Plant defense; Receptor; Reference proteome; Sensory transduction.
FT CHAIN 1..681
FT /note="Cryptochrome-1"
FT /id="PRO_0000085121"
FT DOMAIN 12..141
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000255"
FT REGION 1..489
FT /note="CNT1, binds chromophores to sense blue light and
FT mediate CRY dimerization"
FT /evidence="ECO:0000303|PubMed:25721730"
FT REGION 490..681
FT /note="CCT1/CCE1, mediates blue light signaling"
FT /evidence="ECO:0000269|PubMed:11114337,
FT ECO:0000303|PubMed:25721730"
FT REGION 525..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3D"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT BINDING 247..251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT BINDING 293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3D"
FT BINDING 358
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C"
FT BINDING 359..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3D"
FT BINDING 359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT BINDING 390..392
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3D"
FT SITE 324
FT /note="Involved in electron transfer from the protein
FT surface to the FAD cofactor"
FT /evidence="ECO:0000269|PubMed:26313597,
FT ECO:0000303|PubMed:22421133"
FT SITE 377
FT /note="Involved in electron transfer from the protein
FT surface to the FAD cofactor"
FT /evidence="ECO:0000303|PubMed:22421133"
FT SITE 400
FT /note="Involved in electron transfer from the protein
FT surface to the FAD cofactor"
FT /evidence="ECO:0000269|PubMed:26313597,
FT ECO:0000303|PubMed:22421133"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96524"
FT MOD_RES 621
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96524"
FT DISULFID 80..190
FT /evidence="ECO:0000269|PubMed:15299148,
FT ECO:0007744|PDB:1U3C, ECO:0007744|PDB:1U3D"
FT MUTAGEN 21
FT /note="D->N: In cry1-401; genomes uncoupled mutant (gun)
FT with defects in plastid-to-nucleus signaling."
FT /evidence="ECO:0000269|PubMed:18065688"
FT MUTAGEN 66
FT /note="S->N: Loss of dimerization and activity. Abnormal
FT hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:15805487,
FT ECO:0000269|PubMed:25721730"
FT MUTAGEN 220
FT /note="G->D: In hy4-6; reduced anthocyanin accumulation and
FT abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:25721730,
FT ECO:0000269|PubMed:8528277"
FT MUTAGEN 283
FT /note="G->E: In hy4-5; reduced anthocyanin accumulation and
FT abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:25721730,
FT ECO:0000269|PubMed:8528277"
FT MUTAGEN 286
FT /note="S->N: In cry1-402; genomes uncoupled mutant (gun)
FT with defects in plastid-to-nucleus signaling."
FT /evidence="ECO:0000269|PubMed:18065688"
FT MUTAGEN 324
FT /note="W->F: Impaired photoreduction in vitro, but not in
FT vivo or in whole cell extracts, due to an alternative
FT electron transport that involves small metabolites.
FT Abolished intra-protein electron transfer cascade and
FT impaired conformational change upon photoexcitation."
FT /evidence="ECO:0000269|PubMed:21875594,
FT ECO:0000269|PubMed:26313597"
FT MUTAGEN 337
FT /note="G->D: Abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:25721730"
FT MUTAGEN 340
FT /note="G->E: In cry1-404 and hy4-1; reduced anthocyanin
FT accumulation and abnormal hypocotyl elongation in blue
FT light. Loss of activity. Genomes uncoupled mutant (gun)
FT with defects in plastid-to-nucleus signaling."
FT /evidence="ECO:0000269|PubMed:18065688,
FT ECO:0000269|PubMed:25721730, ECO:0000269|PubMed:8528277,
FT ECO:0000269|PubMed:9565033"
FT MUTAGEN 347
FT /note="G->E: In hy4-16; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:25721730,
FT ECO:0000269|PubMed:8528277"
FT MUTAGEN 347
FT /note="G->R: In hy4-15; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light. Loss of
FT dimerization and activity."
FT /evidence="ECO:0000269|PubMed:15805487,
FT ECO:0000269|PubMed:25721730, ECO:0000269|PubMed:8528277"
FT MUTAGEN 380
FT /note="G->R: Constitutive light response."
FT /evidence="ECO:0000269|PubMed:21765176"
FT MUTAGEN 396
FT /note="D->N: Upon illumination, formation of the reduced
FT anionic flavin (RED) flavin, useful for DNA repair, rather
FT than the semi-reduced radical form (SR) flavin, which is
FT correlated with cryptochrome activity."
FT /evidence="ECO:0000269|PubMed:22890584"
FT MUTAGEN 400
FT /note="W->F: Impaired photoreduction in vitro, but not in
FT vivo or whole cell extracts, due to an alternative electron
FT transport that involves small metabolites."
FT /evidence="ECO:0000269|PubMed:26313597"
FT MUTAGEN 407
FT /note="L->F: Gain of function mutant. Hypersensitive toward
FT blue, red, and far-red light in hypocotyl growth
FT inhibition. Very early flowering in short-day conditions,
FT associated with enhanced expression of CO and FT. Impaired
FT interaction with PHYB."
FT /evidence="ECO:0000269|PubMed:20926618,
FT ECO:0000269|PubMed:22577138"
FT MUTAGEN 462
FT /note="A->V: Loss of dimerization and activity. Abnormal
FT hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:15805487,
FT ECO:0000269|PubMed:25721730"
FT MUTAGEN 515
FT /note="E->K: In hy4-19; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 531
FT /note="E->K: In hy4-20; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 549
FT /note="P->L: In hy4-9; reduced anthocyanin accumulation and
FT abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 559
FT /note="E->K: In hy4-22; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 576
FT /note="R->K: In hy4-10; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 581
FT /note="R->K: In hy4-23; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 611
FT /note="R->K: In hy4-24; reduced anthocyanin accumulation
FT and abnormal hypocotyl elongation in blue light."
FT /evidence="ECO:0000269|PubMed:8528277"
FT MUTAGEN 623
FT /note="E->K: In cry1-403; genomes uncoupled mutant (gun)
FT with defects in plastid-to-nucleus signaling."
FT /evidence="ECO:0000269|PubMed:18065688"
FT CONFLICT 40
FT /note="I -> N (in Ref. 4; AAK32756)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="G -> R (in Ref. 1; AAB28724)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1U3C"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 57..76
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:1U3D"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1U3D"
FT TURN 235..240
FT /evidence="ECO:0007829|PDB:1U3D"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 261..278
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 281..305
FT /evidence="ECO:0007829|PDB:1U3D"
FT TURN 308..312
FT /evidence="ECO:0007829|PDB:1U3D"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 328..336
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 377..387
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 393..404
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:1U3D"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:1U3D"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:1U3D"
FT HELIX 477..495
FT /evidence="ECO:0007829|PDB:1U3D"
SQ SEQUENCE 681 AA; 76695 MW; 372A7E6DDC2AC076 CRC64;
MSGSVSGCGS GGCSIVWFRR DLRVEDNPAL AAAVRAGPVI ALFVWAPEEE GHYHPGRVSR
WWLKNSLAQL DSSLRSLGTC LITKRSTDSV ASLLDVVKST GASQIFFNHL YDPLSLVRDH
RAKDVLTAQG IAVRSFNADL LYEPWEVTDE LGRPFSMFAA FWERCLSMPY DPESPLLPPK
KIISGDVSKC VADPLVFEDD SEKGSNALLA RAWSPGWSNG DKALTTFING PLLEYSKNRR
KADSATTSFL SPHLHFGEVS VRKVFHLVRI KQVAWANEGN EAGEESVNLF LKSIGLREYS
RYISFNHPYS HERPLLGHLK FFPWAVDENY FKAWRQGRTG YPLVDAGMRE LWATGWLHDR
IRVVVSSFFV KVLQLPWRWG MKYFWDTLLD ADLESDALGW QYITGTLPDS REFDRIDNPQ
FEGYKFDPNG EYVRRWLPEL SRLPTDWIHH PWNAPESVLQ AAGIELGSNY PLPIVGLDEA
KARLHEALSQ MWQLEAASRA AIENGSEEGL GDSAEVEEAP IEFPRDITME ETEPTRLNPN
RRYEDQMVPS ITSSLIRPEE DEESSLNLRN SVGDSRAEVP RNMVNTNQAQ QRRAEPASNQ
VTAMIPEFNI RIVAESTEDS TAESSSSGRR ERSGGIVPEW SPGYSEQFPS EENGIGGGST
TSSYLQNHHE ILNWRRLSQT G
