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Entry version 171 (13 Feb 2019)
Sequence version 2 (03 May 2011)
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Protein

Cryptochrome-1

Gene

CRY1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Photoreceptor that mediates primarily blue light inhibition of hypocotyl elongation and photoperiodic control of floral initiation, and regulates other light responses, including circadian rhythms, tropic growth, stomata opening, guard cell development, root development, bacterial and viral pathogen responses, abiotic stress responses, cell cycles, programmed cell death, apical dominance, fruit and ovule development, seed dormancy, and magnetoreception. Photoexcited cryptochromes interact with signaling partner proteins to alter gene expression at both transcriptional and post-translational levels and, consequently, regulate the corresponding metabolic and developmental programs (PubMed:21841916). Blue-light absorbing flavoprotein that activates reversible flavin photoreduction via an electron transport chain comprising a tryptophan triad (W-324, W-377 and W-400), accompanied by a large conformational change upon photoexcitation, or via an alternative electron transport that involves small metabolites, including NADPH, NADH, and ATP. The half-life of the activated signaling state is about 5 minutes (PubMed:26313597, PubMed:25157750, PubMed:23398192, PubMed:21875594, PubMed:21467031). Also involved in the detection of blue/green ratio in light (shade under leaf canopies) and subsequent adaptations on plant growth and development (PubMed:20668058). In darkness, the dark reoxidation of flavin occurs and leads to inactivated state (PubMed:21467031, PubMed:23398192). Perceives low blue light (LBL) and responds by directly contacting two bHLH transcription factors, PIF4 and PIF5, at chromatin on E-box variant 5'-CA[CT]GTG-3' to promote their activity and stimulate specific gene expression to adapt global physiology (e.g. hypocotyl elongation and hyponastic growth in low blue light) (PubMed:26724867, PubMed:19558423). When activated by high-intensity blue light, catalyzes direct enzymatic conversion of molecular oxygen O2 to reactive oxygen species (ROS) and hydrogen peroxide H2O2 in vitro. ROS accumulation upon activation by blue light leads to cell death in protoplasts (PubMed:25728686). Seems essential for blue-light-triggered and singlet oxygen-mediated programmed cell death (PCD) (PubMed:17075038). Required for the induction of nuclear genes encoding photoprotective components by GATA24 and GATA28 in extreme light intensities that exceed the electron utilization capacity of the chloroplast (PubMed:22786870). Involved in shortening the circadian clock period, especially at 27 degrees Celsius, in blue light (BL) and required to maintain clock genes expression rhythm (PubMed:23511208). Mediates blue light-induced gene expression and hypocotyl elongation through the inhibition of COP1-mediated degradation of the transcription factors BIT1 and HY5 and via the activation of anion channels at the plasma membrane, probably via auxin signaling (PubMed:21511872, PubMed:21511871, PubMed:16093319, PubMed:18397371, PubMed:12324610, PubMed:8528277, PubMed:9765547, PubMed:25721730). Required for the hypocotyl hook formation in darkness (PubMed:22855128). Involved in blue light-dependent stomatal opening, CHS gene expression, transpiration, inhibition of stem growth and increase of root growth, probably by regulating abscisic acid (ABA) (PubMed:22147516, PubMed:16093319, PubMed:16703358, PubMed:7756321, PubMed:9565033). Prevents lateral roots growth by inhibiting auxin transport (PubMed:20133010). Necessary for shade avoidance syndrome (SAS), characterized by leaf hyponasty and reduced lamina/petiole ratio, when exposed to blue light attenuation (PubMed:21457375). Together with phototropins, involved in phototropism regulation by various blue light fluence; blue light attenuates phototropism in high fluence rates (100 µmol.m-2.s-1) but enhances phototropism in low fluence rates (<1.0 µmol.m-2.s-1) (PubMed:12857830). Required for blue/UV-A wavelengths-mediated inhibition of explants shoot regeneration in vitro (e.g. new shoot apical meristems regeneration from excised cotyledons) (PubMed:22681544). Modulates anthocyanin accumulation in a PHYA-dependent manner in far-red-light. Acts as a PHYA/PHYB-dependent modulator of chlorophyll accumulation in red light. Contributes to most blue light deetiolation responses (PubMed:9733523, PubMed:8528277). May act as a chemical magnetoreceptor, via magnetically sensitive kinetics and quantum yields of photo-induced flavin / tryptophan radical pairs (PubMed:22421133). The effect of near-null magnetic field on flowering is altered by changes of blue light cycle and intensity in a CRY1/CRY2-dependent manner (PubMed:26095447). Involved in the strigolactone signaling that regulates hypocotyl growth in response to blue light (PubMed:24126495). Modulates temperature-dependent growth and physiology maintenance, especially at warm ambient temperatures, via HFR1-dependent activity (PubMed:21265897).1 Publication34 Publications
Implicated in promoting R protein-mediated resistance to Pseudomonas syringae pv. tomato (Pst.) DC3000 under continuous light conditions. Promotes systemic acquired resistance (SAR) and PR gene expression triggered by P. syringae.1 Publication

Caution

Was originally thought to be a DNA photolyase.1 Publication

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Light exposure induces a conformational change in the C-terminal domain CCT1 required for activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei235FADCombined sources1 Publication1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi238Magnesium 1; via carbonyl oxygenCombined sources1 Publication1
Binding sitei239ATPCombined sources1 Publication1
Metal bindingi241Magnesium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi244Magnesium 2Combined sources1 Publication1
Metal bindingi246Magnesium 1Combined sources1 Publication1
Metal bindingi246Magnesium 2Combined sources1 Publication1
Binding sitei293FAD; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei324Involved in electron transfer from the protein surface to the FAD cofactor1 Publication1 Publication1
Metal bindingi358Magnesium 1; via tele nitrogenCombined sources1 Publication1
Binding sitei359FADCombined sources1 Publication1
Sitei377Involved in electron transfer from the protein surface to the FAD cofactor1 Publication1
Sitei400Involved in electron transfer from the protein surface to the FAD cofactor1 Publication1 Publication1
Binding sitei409ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi247 – 251FADCombined sources1 Publication5
Nucleotide bindingi359 – 360ATPCombined sources1 Publication2
Nucleotide bindingi390 – 392FADCombined sources1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPhotoreceptor protein, Receptor
Biological processApoptosis, Plant defense, Sensory transduction
LigandATP-binding, Chromophore, FAD, Flavoprotein, Magnesium, Metal-binding, Nucleotide-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cryptochrome-11 Publication
Short name:
AtCry1 Publication
Short name:
Atcry11 Publication
Alternative name(s):
Blue light photoreceptor1 Publication
Protein BLUE LIGHT UNINHIBITED 11 Publication
Protein ELONGATED HYPOCOTYL 41 Publication
Protein OUT OF PHASE 2
Short name:
OOP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CRY11 Publication
Synonyms:BLU11 Publication, HY41 Publication
Ordered Locus Names:At4g08920Imported
ORF Names:T3H13.14Imported, T3H13.5Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G08920

The Arabidopsis Information Resource

More...
TAIRi
locus:2138728 AT4G08920

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Prevents the shortening of period at 27 degrees Celsius, resulting in a long period phenotype. The double mutant cry1 cry2 is impaired in blue light signaling, resulting in long-period, lower-amplitude oscillations at 12 and 17 degrees Celsius and completely abolishing rhythms at 27 degrees Celsius (PubMed:23511208). Plants show reduced root and hypocotyl elongation in an anion channels activation-dependent manner at the plasma membrane, as well a reduced anthocyanin accumulation in blue light (PubMed:8528277, PubMed:12324610, PubMed:16703358, PubMed:21511871, PubMed:21511872, PubMed:9765547). Impaired blue/UV-A wavelengths-mediated inhibition of shoot regeneration (PubMed:22681544). Impaired detection of blue/green ratio in light leading to abnormal inhibition of hypocotyl growth (PubMed:20668058). Reduced attenuating effect of high fluence rates of blue light. This phenotype is stronger in the cry1 cry2 double mutant. Slow rate of curvature at low fluence rates of blue light in cry1 cry2 (PubMed:12857830). Lower anthocyanin accumulation in the phyB cry1 double mutant exposed to far-red light. Reduced chlorophyll levels in the phyB cry1 double mutant exposed to red light. In blue light, impaired cotyledon unfolding and smaller cotyledons, longer hypocotyls and less chlorophyll (PubMed:9733523). Impaired accumulation of reactive oxygen species (ROS) in double mutant cry1 cry2 exposed to high-intensity blue light (PubMed:25728686). Altered blue-light-triggered and singlet oxygen-mediated programmed cell death (PCD) (PubMed:17075038). The double mutant cry1 cry2 exhibits a reduced impact of near-null magnetic field on flowering in lower blue light intensity and short days (PubMed:26095447). Reduced hyponastic growth (differential growth-driven upward leaf movement) in low blue light fluence (PubMed:19558423). The double mutant cry1 cry2 is hyposensitive to the strigolactone analog GR24 (PubMed:24126495). The mutant cry1 exposed to a background of red light show severely impaired stomatal opening responses to blue light. The double mutant cry1 cry2 has reduced stomatal conductance, transpiration, and photosynthesis, particularly under the high irradiance of full sunlight at midday, associated with elevated abscisic acid levels (PubMed:22147516). The cry1 mutants grown in complete darkness have premature opening of the hypocotyl hook (PubMed:22855128). Reduced expression of nuclear genes encoding photoprotective components in response to extreme high light (PubMed:22786870). Reduced shade avoidance syndrome (SAS) when exposed to blue light attenuation (PubMed:21457375). Reduced growth at warm ambient temperatures (PubMed:21265897). Down-regulated local resistance and systemic acquired resistance (SAR) to Pseudomonas syringae pv. tomato (Pst.) DC3000 under continuous light conditions, leading to pathogen proliferation (PubMed:20053798). When grown in blue light, increased growth of lateral roots and reduced sensitivity to auxin (IAA) on this phenotype (PubMed:20133010).23 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi21D → N in cry1-401; genomes uncoupled mutant (gun) with defects in plastid-to-nucleus signaling. 1 Publication1
Mutagenesisi66S → N: Loss of dimerization and activity. Abnormal hypocotyl elongation in blue light. 2 Publications1
Mutagenesisi220G → D in hy4-6; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 2 Publications1
Mutagenesisi283G → E in hy4-5; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 2 Publications1
Mutagenesisi286S → N in cry1-402; genomes uncoupled mutant (gun) with defects in plastid-to-nucleus signaling. 1 Publication1
Mutagenesisi324W → F: Impaired photoreduction in vitro, but not in vivo or in whole cell extracts, due to an alternative electron transport that involves small metabolites. Abolished intra-protein electron transfer cascade and impaired conformational change upon photoexcitation. 2 Publications1
Mutagenesisi337G → D: Abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi340G → E in cry1-404 and hy4-1; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. Loss of activity. Genomes uncoupled mutant (gun) with defects in plastid-to-nucleus signaling. 4 Publications1
Mutagenesisi347G → E in hy4-16; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 2 Publications1
Mutagenesisi347G → R in hy4-15; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. Loss of dimerization and activity. 3 Publications1
Mutagenesisi380G → R: Constitutive light response. 1 Publication1
Mutagenesisi396D → N: Upon illumination, formation of the reduced anionic flavin (RED) flavin, useful for DNA repair, rather than the semi-reduced radical form (SR) flavin, which is correlated with cryptochrome activity. 1 Publication1
Mutagenesisi400W → F: Impaired photoreduction in vitro, but not in vivo or whole cell extracts, due to an alternative electron transport that involves small metabolites. 1 Publication1
Mutagenesisi407L → F: Gain of function mutant. Hypersensitive toward blue, red, and far-red light in hypocotyl growth inhibition. Very early flowering in short-day conditions, associated with enhanced expression of CO and FT. Impaired interaction with PHYB. 2 Publications1
Mutagenesisi462A → V: Loss of dimerization and activity. Abnormal hypocotyl elongation in blue light. 2 Publications1
Mutagenesisi515E → K in hy4-19; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi531E → K in hy4-20; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi549P → L in hy4-9; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi559E → K in hy4-22; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi576R → K in hy4-10; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi581R → K in hy4-23; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi611R → K in hy4-24; reduced anthocyanin accumulation and abnormal hypocotyl elongation in blue light. 1 Publication1
Mutagenesisi623E → K in cry1-403; genomes uncoupled mutant (gun) with defects in plastid-to-nucleus signaling. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000851211 – 681Cryptochrome-1Add BLAST681

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi80 ↔ 190Combined sources1 Publication
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei616PhosphoserineBy similarity1
Modified residuei621PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated; in response to blue light and when in complex with FAD cofactor (PubMed:12846824, PubMed:14523249, PubMed:9651577, PubMed:17073458). Kinase activity is optimal in the presence of magnesium ions, about 30 percent of the optimal activity in the presence of manganese ions, but inactive with calcium ions (PubMed:17073458). Adopts an open conformation when phosphorylated upon photoexcitation and thus interacts with signaling partner proteins (PubMed:21841916).1 Publication4 Publications

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q43125

PRoteomics IDEntifications database

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PRIDEi
Q43125

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q43125

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed (PubMed:8953250). Expressed in the aerial tissues (e.g. cotyledons and leaf primordia), but not detected in the roots (PubMed:11743105).2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression levels display circadian oscillations under constant conditions, with a high amplitude and an early phase, with maximal expression around 4-6 hours of the light phase. Induced by light (PubMed:11743105). Transcripts levels oscillate weakly and proportionally to temperature, but protein levels are stable, with higher levels at low temperature (12 degrees Celsius) (PubMed:23511208). Accumulates in response to low blue light (LBL) (PubMed:26724867).3 Publications

Gene expression databases

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q43125 AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Interacts with ADO1, COP1 and PHYA. Interacts specifically with the dark/far-red (Pr) state of PHYB, but not with the red light-activated (Pfr) (PubMed:22577138). Interacts with PIF4 and PIF5 in the nucleus in response to low blue light (LBL) (PubMed:26724867). Binds to SPA1 and SPA4 in response to blue light, this interaction prevents SPA1/COP1 complex formation and thus avoid COP1-dependent degradation of the transcription factor HY5 by the proteasome and promotes hypocotyl elongation (PubMed:21511872, PubMed:21511871). Interacts with TCP2 (PubMed:26596765). Binding to ATP mediates conformational changes which facilitate flavin binding (PubMed:19327354, PubMed:17073458).13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
11769, 7 interactors

Protein interaction database and analysis system

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IntActi
Q43125, 3 interactors

Molecular INTeraction database

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MINTi
Q43125

STRING: functional protein association networks

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STRINGi
3702.AT4G08920.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1681
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U3CX-ray2.60A1-509[»]
1U3DX-ray2.45A1-509[»]

Database of protein disorder

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DisProti
DP00474

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q43125

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q43125

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q43125

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini12 – 141Photolyase/cryptochrome alpha/betaSequence analysisAdd BLAST130

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 489CNT1, binds chromophores to sense blue light and mediate CRY dimerization1 PublicationAdd BLAST489
Regioni490 – 681CCT1/CCE1, mediates blue light signaling1 Publication1 PublicationAdd BLAST192

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal domain CNT1 (1-489) is sufficient for autophosphorylation and is required for dimerization. The C-terminal domain CCT1 (490-681) of the homodimer binds to COP1.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DNA photolyase class-1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0133 Eukaryota
COG0415 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000245621

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q43125

KEGG Orthology (KO)

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KOi
K12118

Identification of Orthologs from Complete Genome Data

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OMAi
AINAYMW

Database of Orthologous Groups

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OrthoDBi
378952at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.620, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR036134 Crypto/Photolyase_FAD-like_sf
IPR036155 Crypto/Photolyase_N_sf
IPR005101 Cryptochr/Photolyase_FAD-bd
IPR002081 Cryptochrome/DNA_photolyase_1
IPR020978 Cryptochrome_C
IPR014134 Cryptochrome_pln
IPR018394 DNA_photolyase_1_CS_C
IPR006050 DNA_photolyase_N
IPR014729 Rossmann-like_a/b/a_fold

Pfam protein domain database

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Pfami
View protein in Pfam
PF12546 Cryptochrome_C, 1 hit
PF00875 DNA_photolyase, 1 hit
PF03441 FAD_binding_7, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00147 DNAPHOTLYASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48173 SSF48173, 1 hit
SSF52425 SSF52425, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR02766 crypt_chrom_pln, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00394 DNA_PHOTOLYASES_1_1, 1 hit
PS00691 DNA_PHOTOLYASES_1_2, 1 hit
PS51645 PHR_CRY_ALPHA_BETA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q43125-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGSVSGCGS GGCSIVWFRR DLRVEDNPAL AAAVRAGPVI ALFVWAPEEE
60 70 80 90 100
GHYHPGRVSR WWLKNSLAQL DSSLRSLGTC LITKRSTDSV ASLLDVVKST
110 120 130 140 150
GASQIFFNHL YDPLSLVRDH RAKDVLTAQG IAVRSFNADL LYEPWEVTDE
160 170 180 190 200
LGRPFSMFAA FWERCLSMPY DPESPLLPPK KIISGDVSKC VADPLVFEDD
210 220 230 240 250
SEKGSNALLA RAWSPGWSNG DKALTTFING PLLEYSKNRR KADSATTSFL
260 270 280 290 300
SPHLHFGEVS VRKVFHLVRI KQVAWANEGN EAGEESVNLF LKSIGLREYS
310 320 330 340 350
RYISFNHPYS HERPLLGHLK FFPWAVDENY FKAWRQGRTG YPLVDAGMRE
360 370 380 390 400
LWATGWLHDR IRVVVSSFFV KVLQLPWRWG MKYFWDTLLD ADLESDALGW
410 420 430 440 450
QYITGTLPDS REFDRIDNPQ FEGYKFDPNG EYVRRWLPEL SRLPTDWIHH
460 470 480 490 500
PWNAPESVLQ AAGIELGSNY PLPIVGLDEA KARLHEALSQ MWQLEAASRA
510 520 530 540 550
AIENGSEEGL GDSAEVEEAP IEFPRDITME ETEPTRLNPN RRYEDQMVPS
560 570 580 590 600
ITSSLIRPEE DEESSLNLRN SVGDSRAEVP RNMVNTNQAQ QRRAEPASNQ
610 620 630 640 650
VTAMIPEFNI RIVAESTEDS TAESSSSGRR ERSGGIVPEW SPGYSEQFPS
660 670 680
EENGIGGGST TSSYLQNHHE ILNWRRLSQT G
Length:681
Mass (Da):76,695
Last modified:May 3, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i372A7E6DDC2AC076
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB28725 differs from that shown. Reason: Frameshift at position 546.Curated
The sequence AAD17364 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAB78016 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti40I → N in AAK32756 (PubMed:14593172).Curated1
Sequence conflicti654G → R in AAB28724 (PubMed:8232555).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
S66907 mRNA Translation: AAB28724.1
S66909 mRNA Translation: AAB28725.2 Frameshift.
AF128396 Genomic DNA Translation: AAD17364.1 Sequence problems.
AL161513 Genomic DNA Translation: CAB78016.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE82696.1
AF361588 mRNA Translation: AAK32756.1
AY124863 mRNA Translation: AAM70572.1

Protein sequence database of the Protein Information Resource

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PIRi
H85089
S39058

NCBI Reference Sequences

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RefSeqi
NP_567341.1, NM_116961.5

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
At.27730

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT4G08920.1; AT4G08920.1; AT4G08920

Database of genes from NCBI RefSeq genomes

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GeneIDi
826470

Gramene; a comparative resource for plants

More...
Gramenei
AT4G08920.1; AT4G08920.1; AT4G08920

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT4G08920

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S66907 mRNA Translation: AAB28724.1
S66909 mRNA Translation: AAB28725.2 Frameshift.
AF128396 Genomic DNA Translation: AAD17364.1 Sequence problems.
AL161513 Genomic DNA Translation: CAB78016.1 Sequence problems.
CP002687 Genomic DNA Translation: AEE82696.1
AF361588 mRNA Translation: AAK32756.1
AY124863 mRNA Translation: AAM70572.1
PIRiH85089
S39058
RefSeqiNP_567341.1, NM_116961.5
UniGeneiAt.27730

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U3CX-ray2.60A1-509[»]
1U3DX-ray2.45A1-509[»]
DisProtiDP00474
ProteinModelPortaliQ43125
SMRiQ43125
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11769, 7 interactors
IntActiQ43125, 3 interactors
MINTiQ43125
STRINGi3702.AT4G08920.1

PTM databases

iPTMnetiQ43125

Proteomic databases

PaxDbiQ43125
PRIDEiQ43125

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G08920.1; AT4G08920.1; AT4G08920
GeneIDi826470
GrameneiAT4G08920.1; AT4G08920.1; AT4G08920
KEGGiath:AT4G08920

Organism-specific databases

AraportiAT4G08920
TAIRilocus:2138728 AT4G08920

Phylogenomic databases

eggNOGiKOG0133 Eukaryota
COG0415 LUCA
HOGENOMiHOG000245621
InParanoidiQ43125
KOiK12118
OMAiAINAYMW
OrthoDBi378952at2759

Miscellaneous databases

EvolutionaryTraceiQ43125

Protein Ontology

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PROi
PR:Q43125

Gene expression databases

GenevisibleiQ43125 AT

Family and domain databases

Gene3Di3.40.50.620, 1 hit
InterProiView protein in InterPro
IPR036134 Crypto/Photolyase_FAD-like_sf
IPR036155 Crypto/Photolyase_N_sf
IPR005101 Cryptochr/Photolyase_FAD-bd
IPR002081 Cryptochrome/DNA_photolyase_1
IPR020978 Cryptochrome_C
IPR014134 Cryptochrome_pln
IPR018394 DNA_photolyase_1_CS_C
IPR006050 DNA_photolyase_N
IPR014729 Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF12546 Cryptochrome_C, 1 hit
PF00875 DNA_photolyase, 1 hit
PF03441 FAD_binding_7, 1 hit
PRINTSiPR00147 DNAPHOTLYASE
SUPFAMiSSF48173 SSF48173, 1 hit
SSF52425 SSF52425, 1 hit
TIGRFAMsiTIGR02766 crypt_chrom_pln, 1 hit
PROSITEiView protein in PROSITE
PS00394 DNA_PHOTOLYASES_1_1, 1 hit
PS00691 DNA_PHOTOLYASES_1_2, 1 hit
PS51645 PHR_CRY_ALPHA_BETA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCRY1_ARATH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q43125
Secondary accession number(s): Q43126
, Q8L7Y1, Q9ASZ2, Q9M0S9, Q9ZPF0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 3, 2011
Last modified: February 13, 2019
This is version 171 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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