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 24-JAN-2024, entry version 195. 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}, HY4 GN {ECO:0000303|PubMed:8232555}; GN OrderedLocusNames=At4g08920 {ECO:0000312|Araport:AT4G08920}; GN ORFNames=T3H13.14 {ECO:0000312|EMBL:AAD17364.1}, T3H13.5 GN {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=10.1105/tpc.3.7.685; 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=10.1105/tpc.010367; 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/tpc.013011; 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 FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia; RX PubMed=30635559; DOI=10.1038/s41467-018-08059-z; RA Qiu Y., Li M., Kim R.J.-A., Moore C.M., Chen M.; RT "Daytime temperature is sensed by phytochrome B in Arabidopsis through a RT transcriptional activator HEMERA."; RL Nat. Commun. 10:140-140(2019). RN [64] 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 (e.g. 27 degrees Celsius) and CC in white light and low-light conditions, via HFR1-dependent activity; CC this process requires PTAC12/HMR/PAP5 (transcriptional transactivator) CC (PubMed:21265897, PubMed:30635559). {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:30635559, ECO:0000269|PubMed:7756321, CC ECO:0000269|PubMed:8528277, ECO:0000269|PubMed:9565033, CC ECO:0000269|PubMed:9733523, ECO:0000269|PubMed:9765547, CC 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). Altered warm-temperature (e.g. 27 degrees Celsius) CC responses leading to abnormal hypocotyl elongation depending on light CC conditions and seedling stages (PubMed:30635559). Reduced attenuating CC effect of high fluence rates of blue light. This phenotype is stronger CC in the cry1 cry2 double mutant. Slow rate of curvature at low fluence CC rates of blue light in cry1 cry2 (PubMed:12857830). Lower anthocyanin CC accumulation in the phyB cry1 double mutant exposed to far-red light. CC Reduced chlorophyll levels in the phyB cry1 double mutant exposed to CC red light. In blue light, impaired cotyledon unfolding and smaller CC cotyledons, longer hypocotyls and less chlorophyll (PubMed:9733523). CC Impaired accumulation of reactive oxygen species (ROS) in double mutant CC cry1 cry2 exposed to high-intensity blue light (PubMed:25728686). CC Altered blue-light-triggered and singlet oxygen-mediated programmed CC cell death (PCD) (PubMed:17075038). The double mutant cry1 cry2 CC exhibits a reduced impact of near-null magnetic field on flowering in CC lower blue light intensity and short days (PubMed:26095447). Reduced CC hyponastic growth (differential growth-driven upward leaf movement) in CC low blue light fluence (PubMed:19558423). The double mutant cry1 cry2 CC is hyposensitive to the strigolactone analog GR24 (PubMed:24126495). CC The mutant cry1 exposed to a background of red light show severely CC impaired stomatal opening responses to blue light. The double mutant CC cry1 cry2 has reduced stomatal conductance, transpiration, and CC photosynthesis, particularly under the high irradiance of full sunlight CC at midday, associated with elevated abscisic acid levels CC (PubMed:22147516). The cry1 mutants grown in complete darkness have CC premature opening of the hypocotyl hook (PubMed:22855128). Reduced CC expression of nuclear genes encoding photoprotective components in CC response to extreme high light (PubMed:22786870). Reduced shade CC avoidance syndrome (SAS) when exposed to blue light attenuation CC (PubMed:21457375). Reduced growth at warm ambient temperatures CC (PubMed:21265897). Down-regulated local resistance and systemic CC acquired resistance (SAR) to Pseudomonas syringae pv. tomato (Pst.) CC DC3000 under continuous light conditions, leading to pathogen CC proliferation (PubMed:20053798). When grown in blue light, increased CC growth of lateral roots and reduced sensitivity to auxin (IAA) on this CC phenotype (PubMed:20133010). {ECO:0000269|PubMed:12324610, CC ECO:0000269|PubMed:12857830, ECO:0000269|PubMed:16703358, CC ECO:0000269|PubMed:17075038, ECO:0000269|PubMed:19558423, CC ECO:0000269|PubMed:20053798, ECO:0000269|PubMed:20133010, CC ECO:0000269|PubMed:20668058, ECO:0000269|PubMed:21265897, CC ECO:0000269|PubMed:21457375, ECO:0000269|PubMed:21511871, CC ECO:0000269|PubMed:21511872, ECO:0000269|PubMed:22147516, CC ECO:0000269|PubMed:22681544, ECO:0000269|PubMed:22786870, CC ECO:0000269|PubMed:22855128, ECO:0000269|PubMed:23511208, CC ECO:0000269|PubMed:24126495, ECO:0000269|PubMed:25728686, CC ECO:0000269|PubMed:26095447, ECO:0000269|PubMed:30635559, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 14. DR IntAct; Q43125; 3. DR MINT; Q43125; -. DR STRING; 3702.Q43125; -. DR iPTMnet; Q43125; -. DR PaxDb; 3702-AT4G08920-1; -. 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; AT4G08920; CRY1. DR eggNOG; KOG0133; Eukaryota. DR HOGENOM; CLU_010348_5_0_1; -. DR InParanoid; Q43125; -. DR OMA; KYFPWVV; -. DR OrthoDB; 124765at2759; -. DR EvolutionaryTrace; Q43125; -. DR PRO; PR:Q43125; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q43125; baseline and differential. 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: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: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: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:0009266; P:response to temperature stimulus; 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; 1.25.40.80; -; 1. DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1. DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR02766; crypt_chrom_pln; 1. DR PANTHER; PTHR11455; CRYPTOCHROME; 1. DR PANTHER; PTHR11455:SF50; CRYPTOCHROME-1; 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; Cryptochrome/photolyase FAD-binding domain; 1. DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 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. DR Genevisible; Q43125; AT. 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 //