Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 167 (12 Aug 2020)
Sequence version 1 (01 May 1997)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Cryptochrome-1

Gene

Cry1

Organism
Mus musculus (Mouse)
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

Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-ARNTL/BMAL1 independently of PER proteins and is found at CLOCK-ARNTL/BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-ARNTL/BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1, ATF4, MTA1, KLF10 and NAMPT. May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that downregulates gluconeogenic gene expression. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity (PubMed:28683290). Plays an essential role in the generation of circadian rhythms in the retina (PubMed:29561690). Represses the transcriptional activity of NR1I2 (PubMed:28751364).28 Publications

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

KL001 (N-[3-(9H-carbazol-9-yl)-2-hydroxypropyl]-N-(2-furanylmethyl)-methanesulfonamide) binds to CRY1 and stabilizes it by inhibiting FBXL3- and ubiquitin-dependent degradation of CRY1 resulting in lengthening of the circadian periods. KL001-mediated CRY1 stabilization can inhibit glucagon-induced gluconeogenesis in primary hepatocytes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei252FAD; via amide nitrogen1 Publication1
Binding sitei289FAD1 Publication1
Binding sitei355FAD1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi387 – 389FAD1 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, Repressor
Biological processBiological rhythms, Sensory transduction, Transcription, Transcription regulation
LigandChromophore, FAD, Flavoprotein, 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%5Fand%5Ftaxonomy%5Fsection">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-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Cry1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 10

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1270841, Cry1

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics 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

Mice show an advanced phase shift (around 4 hours) in the expression of DBP, NR1D1 and PER1 genes in the liver. Double knockouts of CRY1 and CRY2 show slightly decrease body weight and lose the cycling rhythmicity of feeding behavior, energy expenditure and glucocorticoids expression. Glucose homeostasis is severely disrupted and animals exhibit elevated blood glucose in response to acute feeding after an overnight fast as well as severely impaired glucose clearance in a glucose tolerance test. When challenged with high-fat diet, animals rapidly gain weight and surpass that of wild-type mice, despite displaying hypophagia. They exhibit hyperinsulinemia and selective insulin resistance in the liver and muscle but show high insulin sensitivity in adipose tissue and consequent increased lipid uptake. Mice display enlarged gonadal, subcutaneous and perirenal fat deposits with adipocyte hypertrophy and increased lipied accumulation in liver. Mice show loss of circadian rhythms in photopic ERG b-wave amplitudes, visual contrast sensitivity and pupillary light responses, with reduced robustness and stability of bioluminescent rhythms (PubMed:29561690). Both single CRY1 knockout and double CRY1 and CRY2 knockout mice show increased exercise performance and increased mitochondrial reserve capacity in primary myotubes (PubMed:28683290).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi71S → A: Phosphomimetic mutant that leads to stabilization of the protein; when associated with A-280. 1 Publication1
Mutagenesisi71S → D: Phosphomimetic mutant that leads to destabilization of the protein and abolishes ability to bind PER2; when associated with D-280. 1 Publication1
Mutagenesisi107K → R: Sensitive to FBXL3-ediated degradation but noz affected by expression of FBXL21. 1 Publication1
Mutagenesisi224H → E: Reduces affinity for FBXL3. 1 Publication1
Mutagenesisi247S → A: Reduced MAPK-catalyzed in vitro phosphorylation. No effect on inhibition of CLOCK-ARNTL/BMAL1-mediated transcriptional activity. 2 Publications1
Mutagenesisi247S → D: Reduced inhibition of CLOCK-ARNTL/BMAL1-mediated transcriptional activity. 2 Publications1
Mutagenesisi273Y → A: Reduced interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-276. 1 Publication1
Mutagenesisi276V → A: Reduced interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-273. 1 Publication1
Mutagenesisi280S → A: Phosphomimetic mutant that leads to stabilization of the protein; when associated with A-71. 1 Publication1
Mutagenesisi280S → D: Phosphomimetic mutant that leads to destabilization of the protein and abolishes ability to bind PER2; when associated with D-71. 1 Publication1
Mutagenesisi287Y → A: No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-290. 1 Publication1
Mutagenesisi290L → A: No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-287. 1 Publication1
Mutagenesisi336G → D: Abolishes transcriptional repression of target genes. Abolishes interaction with PER2. 1
Mutagenesisi382 – 383EE → RR: Decreases transcriptional repression of target genes. Decreases FBXL3 binding. Increases PER2 binding. 1 Publication2
Mutagenesisi405F → A: Decreases affinity for FBXL3. Slightly increases affinity for PER2. 1 Publication1
Mutagenesisi485K → D or E: Strongly reduces FBXL3 binding. Reduces PER2 binding. 1 Publication1
Mutagenesisi488Y → A: No efect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-491. 1 Publication1
Mutagenesisi491L → A: No effect on its interaction with MAP1LC3B and moderate decrease in its autophagy-mediated degradation; when associated with A-488. 1 Publication1
Mutagenesisi494Y → A: Loss of interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-497. 1 Publication1
Mutagenesisi497L → A: Loss of interaction with MAP1LC3B and significant decrease in its autophagy-mediated degradation; when associated with A-494. 1 Publication1
Mutagenesisi551S → A: No effect on circadian period length and protein stability. 1 Publication1
Mutagenesisi551S → D: No effect on circadian period length and protein stability. 1 Publication1
Mutagenesisi564S → A: No effect on circadian period length and protein stability. 1 Publication1
Mutagenesisi564S → D: No effect on circadian period length and protein stability. 1 Publication1
Mutagenesisi585K → A: Loss of ubiquitination. No loss of interaction with DDB1-CUL4A complex. 1 Publication1
Mutagenesisi588S → A: No effect on circadian period length and protein stability. 1 Publication1
Mutagenesisi588S → D: Lengthen circadian period. No effect on repressive activity. Increases protein stability. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002611421 – 606Cryptochrome-1Add BLAST606

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 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 residuei71Phosphoserine; by AMPK1 Publication1
Cross-linki107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei247Phosphoserine; by MAPK1 Publication1
Modified residuei280Phosphoserine; by AMPK1 Publication1
Cross-linki329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki485Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki585Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei588Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylation on Ser-247 by MAPK is important for the inhibition of CLOCK-ARNTL/BMAL1-mediated transcriptional activity. Phosphorylation by CSNK1E requires interaction with PER1 or PER2. Phosphorylation at Ser-71 and Ser-280 by AMPK decreases protein stability. Phosphorylation at Ser-588 exhibits a robust circadian rhythm with a peak at CT8, increases protein stability, prevents SCF(FBXL3)-mediated degradation and is antagonized by interaction with PRKDC.4 Publications
Ubiquitinated by the SCF(FBXL3) and SCF(FBXL21) complexes, regulating the balance between degradation and stabilization. The SCF(FBXL3) complex is mainly nuclear and mediates ubiquitination and subsequent degradation of CRY1. In contrast, cytoplasmic SCF(FBXL21) complex-mediated ubiquitination leads to stabilize CRY1 and counteract the activity of the SCF(FBXL3) complex. The SCF(FBXL3) and SCF(FBXL21) complexes probably mediate ubiquitination at different Lys residues. Ubiquitination at Lys-11 and Lys-107 are specifically ubiquitinated by the SCF(FBXL21) complex but not by the SCF(FBXL3) complex. Ubiquitination may be inhibited by PER2. Deubiquitinated by USP7 (PubMed:27123980).7 Publications
Undergoes autophagy-mediated degradation in the liver in a time-dependent manner. Autophagic degradation of CRY1 (an inhibitor of gluconeogenesis) occurs during periods of reduced feeding allowing induction of gluconeogenesis and maintenance of blood glucose levels.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P97784

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P97784

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

More...
PaxDbi
P97784

PeptideAtlas

More...
PeptideAtlasi
P97784

PRoteomics IDEntifications database

More...
PRIDEi
P97784

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P97784

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P97784

<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

Expressed in cones, amacrine cells, and retinal ganglion cells of the retina (at protein level) (PubMed:29561690). Expressed in all tissues examined including heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Higher levels in brain, liver and testis. In the retina, highly expressed in the ganglion cell layer (GCL) and in the inner nuclear layer (INL). Evenly distributed in central and peripheral retina. In the brain, highly expressed in the suprachiasmatic nucleus (SCN). High levels in cerebral cortical layers particularly in the pyramidial cell layer of the hippocampus, the granular cell layer of the dentate gyrus (DG) and the pyramidal cell layer of the piriform cortex (PFC).7 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

Oscillates diurnally, rhythmic expression in the early night is critical for clock function (at protein level). In SCN, exhibits circadian rhythm expression with highest levels during the light phase at CT10. No detectable expression after 8 hours in the dark. Circadian oscillations also observed in liver, skeletal muscle and cerebellum, but not in testis.8 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020038, Expressed in secondary oocyte and 297 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P97784, MM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins (PubMed:11779462).

Interacts directly with TIMELESS (PubMed:10428031, PubMed:24489120, PubMed:23418588).

Interacts directly with PER1 and PER2; interaction with PER2 inhibits its ubiquitination and vice versa (PubMed:10428031, PubMed:11889036, PubMed:11875063, PubMed:14701732, PubMed:16478995, PubMed:23746849, PubMed:23418588, PubMed:21613214, PubMed:20159955).

Interacts with PER3 (PubMed:10428031, PubMed:14701732).

Interacts with FBXL21 (PubMed:18953409, PubMed:23452855, PubMed:23452856).

Interacts with FBXL3 (PubMed:17462724, PubMed:23746849, PubMed:23452855, PubMed:23452856, PubMed:30500822).

Interacts with PPP5C (via TPR repeats) (By similarity).

Interacts with CLOCK-ARNTL/BMAL1 independently of PER2 and DNA (PubMed:21613214).

Interacts with HDAC1, HDAC2 and SIN3B (PubMed:15226430).

Interacts with nuclear receptors AR, NR1D1, NR3C1/GR, RORA and RORC; the interaction with at least NR3C1/GR is ligand dependent (PubMed:22170608, PubMed:28751364).

Interacts with PRKDC (PubMed:24158435).

Interacts with the G protein subunit alpha GNAS; the interaction may block GPCR-mediated regulation of cAMP concentrations (By similarity).

Interacts with PRMT5 (PubMed:23133559).

Interacts with EZH2 (PubMed:16717091).

Interacts with MYBBP1A, DOCK7, HNRNPU, RPL7A, RPL8 and RPS3 (PubMed:19129230).

Interacts with MAP1LC3B (PubMed:29937374).

Interacts with CLOCK (PubMed:16717091, PubMed:19917250).

Interacts with ARNTL/BMAL1 (PubMed:26776516, PubMed:16717091, PubMed:19917250, PubMed:23746849).

Interacts weakly with HDAC3; this interaction is enhanced in the presence of FBXL3 (PubMed:26776516).

Interacts with TRIM28, KCTD5 and DDB1 (PubMed:27123980).

Interacts with DTL (By similarity).

Interacts with DDB1-CUL4A complex (PubMed:26431207).

Interacts with FOXO1 (PubMed:28790135).

Interacts with PSMD2 in a KDM8-dependent manner (PubMed:30500822).

Interacts with KDM8 in a FBXL3-dependent manner (PubMed:30500822).

Interacts with PPARA (PubMed:28683290).

Interacts with PPARG in a ligand-dependent manner (PubMed:28683290).

Interacts with PPARD (via domain NR LBD) in a ligand-dependent manner (PubMed:28683290, PubMed:28751364).

Interacts with NR1I2 (via domain NR LBD) in a ligand-dependent manner (PubMed:28751364).

Interacts with NR1I3, VDR and HNF4A (PubMed:28751364).

By similarity30 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
198906, 35 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3209, Cry1-Per2 complex
CPX-3216, Cry1-Per1 complex
CPX-3217, Cry1-Per3 complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P97784

Database of interacting proteins

More...
DIPi
DIP-38515N

Protein interaction database and analysis system

More...
IntActi
P97784, 49 interactors

Molecular INTeraction database

More...
MINTi
P97784

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000020227

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P97784, protein

<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

1606
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P97784

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini3 – 132Photolyase/cryptochrome alpha/betaAdd 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>Regioni371 – 470Required for inhibition of CLOCK-ARNTL/BMAL1-mediated transcription1 PublicationAdd BLAST100
Regioni471 – 493Interaction with TIMELESS1 PublicationAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi50 – 54LIR 11 Publication5
Motifi82 – 87LIR 21 Publication6
Motifi151 – 156LIR 31 Publication6
Motifi255 – 260LIR 41 Publication6
Motifi271 – 276LIR 51 Publication6
Motifi285 – 290LIR 61 Publication6
Motifi335 – 339LIR 71 Publication5
Motifi379 – 384LIR 81 Publication6
Motifi395 – 400LIR 91 Publication6
Motifi411 – 416LIR 101 Publication6
Motifi430 – 435LIR 111 Publication6
Motifi486 – 491LIR 121 Publication6
Motifi492 – 497LIR 131 Publication6

<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 LIR motifs (LC3-interacting region) 3 and 5 are required for its interaction with MAP1LC3B and for its autophagy-mediated degradation.1 Publication

<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

More...
eggNOGi
KOG0133, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155455

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010348_3_4_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P97784

KEGG Orthology (KO)

More...
KOi
K02295

Identification of Orthologs from Complete Genome Data

More...
OMAi
WQWSASS

Database of Orthologous Groups

More...
OrthoDBi
378952at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P97784

TreeFam database of animal gene trees

More...
TreeFami
TF323191

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.620, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID50287

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036134, Crypto/Photolyase_FAD-like_sf
IPR036155, Crypto/Photolyase_N_sf
IPR005101, Cryptochr/Photolyase_FAD-bd
IPR006050, DNA_photolyase_N
IPR014729, Rossmann-like_a/b/a_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00875, DNA_photolyase, 1 hit
PF03441, FAD_binding_7, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48173, SSF48173, 1 hit
SSF52425, SSF52425, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P97784-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGVNAVHWFR KGLRLHDNPA LKECIQGADT IRCVYILDPW FAGSSNVGIN
60 70 80 90 100
RWRFLLQCLE DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WNITKLSIEY
110 120 130 140 150
DSEPFGKERD AAIKKLATEA GVEVIVRISH TLYDLDKIIE LNGGQPPLTY
160 170 180 190 200
KRFQTLVSKM EPLEMPADTI TSDVIGKCMT PLSDDHDEKY GVPSLEELGF
210 220 230 240 250
DTDGLSSAVW PGGETEALTR LERHLERKAW VANFERPRMN ANSLLASPTG
260 270 280 290 300
LSPYLRFGCL SCRLFYFKLT DLYKKVKKNS SPPLSLYGQL LWREFFYTAA
310 320 330 340 350
TNNPRFDKME GNPICVQIPW DKNPEALAKW AEGRTGFPWI DAIMTQLRQE
360 370 380 390 400
GWIHHLARHA VACFLTRGDL WISWEEGMKV FEELLLDADW SINAGSWMWL
410 420 430 440 450
SCSSFFQQFF HCYCPVGFGR RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA
460 470 480 490 500
PEGIQKVAKC LIGVNYPKPM VNHAEASRLN IERMKQIYQQ LSRYRGLGLL
510 520 530 540 550
ASVPSNSNGN GGLMGYAPGE NVPSCSSSGN GGLMGYAPGE NVPSCSGGNC
560 570 580 590 600
SQGSGILHYA HGDSQQTHSL KQGRSSAGTG LSSGKRPSQE EDAQSVGPKV

QRQSSN
Length:606
Mass (Da):68,001
Last modified:May 1, 1997 - v1
<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:i2F2B8DD53F0A9AF9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1L1SUT8A0A1L1SUT8_MOUSE
Cryptochrome-1
Cry1
59Annotation score:

Annotation score:1 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB000777 mRNA Translation: BAA19175.1
AF156986 mRNA Translation: AAD39548.1
AK162460 mRNA Translation: BAE36931.1
BC022174 mRNA Translation: AAH22174.1
BC085499 mRNA Translation: AAH85499.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS24089.1

NCBI Reference Sequences

More...
RefSeqi
NP_031797.1, NM_007771.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000020227; ENSMUSP00000020227; ENSMUSG00000020038

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
12952

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12952

UCSC genome browser

More...
UCSCi
uc007gle.1, mouse

<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
AB000777 mRNA Translation: BAA19175.1
AF156986 mRNA Translation: AAD39548.1
AK162460 mRNA Translation: BAE36931.1
BC022174 mRNA Translation: AAH22174.1
BC085499 mRNA Translation: AAH85499.1
CCDSiCCDS24089.1
RefSeqiNP_031797.1, NM_007771.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CT0X-ray2.45A1-496[»]
4K0RX-ray2.65A1-606[»]
5T5XX-ray1.84A1-491[»]
6KX4X-ray2.00A1-496[»]
6KX5X-ray2.00A1-496[»]
6KX6X-ray2.00A/B1-496[»]
6KX7X-ray2.10A1-496[»]
6OF7X-ray3.11A1-491[»]
SMRiP97784
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi198906, 35 interactors
ComplexPortaliCPX-3209, Cry1-Per2 complex
CPX-3216, Cry1-Per1 complex
CPX-3217, Cry1-Per3 complex
CORUMiP97784
DIPiDIP-38515N
IntActiP97784, 49 interactors
MINTiP97784
STRINGi10090.ENSMUSP00000020227

PTM databases

iPTMnetiP97784
PhosphoSitePlusiP97784

Proteomic databases

EPDiP97784
MaxQBiP97784
PaxDbiP97784
PeptideAtlasiP97784
PRIDEiP97784

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3122, 278 antibodies

Genome annotation databases

EnsembliENSMUST00000020227; ENSMUSP00000020227; ENSMUSG00000020038
GeneIDi12952
KEGGimmu:12952
UCSCiuc007gle.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1407
MGIiMGI:1270841, Cry1

Phylogenomic databases

eggNOGiKOG0133, Eukaryota
GeneTreeiENSGT00940000155455
HOGENOMiCLU_010348_3_4_1
InParanoidiP97784
KOiK02295
OMAiWQWSASS
OrthoDBi378952at2759
PhylomeDBiP97784
TreeFamiTF323191

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
12952, 1 hit in 18 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Cry1, mouse

Protein Ontology

More...
PROi
PR:P97784
RNActiP97784, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020038, Expressed in secondary oocyte and 297 other tissues
GenevisibleiP97784, MM

Family and domain databases

Gene3Di3.40.50.620, 1 hit
IDEALiIID50287
InterProiView protein in InterPro
IPR036134, Crypto/Photolyase_FAD-like_sf
IPR036155, Crypto/Photolyase_N_sf
IPR005101, Cryptochr/Photolyase_FAD-bd
IPR006050, DNA_photolyase_N
IPR014729, Rossmann-like_a/b/a_fold
PfamiView protein in Pfam
PF00875, DNA_photolyase, 1 hit
PF03441, FAD_binding_7, 1 hit
SUPFAMiSSF48173, SSF48173, 1 hit
SSF52425, SSF52425, 1 hit
PROSITEiView protein in PROSITE
PS51645, PHR_CRY_ALPHA_BETA, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_MOUSE
<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: P97784
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 1997
Last modified: August 12, 2020
This is version 167 of the entry and version 1 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 programChordata 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again