CRY1_DROPS
ID CRY1_DROPS Reviewed; 540 AA.
AC Q293P8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Cryptochrome-1;
GN Name=cry {ECO:0000250|UniProtKB:O77059}; ORFNames=GA17677;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Blue light-dependent regulator that is the input of the
CC circadian feedback loop. Has no photolyase activity for cyclobutane
CC pyrimidine dimers or 6-4 photoproducts. Regulation of expression by
CC light suggests a role in photoreception for locomotor activity rhythms.
CC Light induces the degradation of cry, likely due to conformational
CC change in the photoreceptor leading to targeting to the proteasome.
CC Under circadian regulation, expression is influenced by the clock
CC pacemaker genes period, timeless, Clock and cycle. Binding to tim
CC irreversibly commits tim to proteasomal degradation. Functions,
CC together with per, as a transcriptional repressor required for the
CC oscillation of peripheral circadian clocks and for the correct
CC specification of clock cells. Genes directly activated by the
CC transcription factors Clock (Clk) and cycle (cyc) are repressed by cry.
CC Necessary for light-dependent magnetosensitivity, an intact circadian
CC system is not required for the magnetoreception mechanism to operate.
CC Required for both the naive and trained responses to magnetic field,
CC consistent with the notion that Cry is in the input pathway of magnetic
CC sensing (By similarity). {ECO:0000250|UniProtKB:O77059}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O77059};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O77059};
CC -!- SUBUNIT: Interacts with tim and per; promoted by light conditions.
CC {ECO:0000250|UniProtKB:O77059}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O77059}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O77059}. Nucleus
CC {ECO:0000250|UniProtKB:O77059}. Note=Nuclear translocation initiates
CC after the perception of a light signal. Accumulates in the perinuclear
CC region about one hour before translocation into the nucleus.
CC Translocation occurs through interaction with other Clock proteins such
CC as tim and per (By similarity). {ECO:0000250|UniProtKB:O77059}.
CC -!- DOMAIN: FAD-binding region regulates cry stability, cry-tim
CC interaction, and circadian photosensitivity.
CC {ECO:0000250|UniProtKB:O77059}.
CC -!- DOMAIN: Photolyase/cryptochrome alpha/beta domain is sufficient for
CC light detection and phototransduction. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000070; EAL29166.2; -; Genomic_DNA.
DR RefSeq; XP_001360014.2; XM_001359977.3.
DR AlphaFoldDB; Q293P8; -.
DR SMR; Q293P8; -.
DR STRING; 7237.FBpp0284934; -.
DR EnsemblMetazoa; FBtr0286496; FBpp0284934; FBgn0077687.
DR GeneID; 4803241; -.
DR KEGG; dpo:Dpse_GA17677; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_3_4_1; -.
DR InParanoid; Q293P8; -.
DR OMA; IWFRHGL; -.
DR ChiTaRS; cry; fly.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0077687; Expressed in insect adult head and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009882; F:blue light photoreceptor activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:EnsemblMetazoa.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0050980; P:detection of light stimulus involved in magnetoreception; IEA:EnsemblMetazoa.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IEA:EnsemblMetazoa.
DR GO; GO:0042332; P:gravitaxis; IEA:EnsemblMetazoa.
DR GO; GO:0045475; P:locomotor rhythm; IEA:EnsemblMetazoa.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IEA:EnsemblMetazoa.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR GO; GO:0071000; P:response to magnetism; IEA:EnsemblMetazoa.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR11455; PTHR11455; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Biological rhythms; Chromophore; Cytoplasm; FAD; Flavoprotein;
KW Nucleotide-binding; Nucleus; Photoreceptor protein; Receptor;
KW Reference proteome; Repressor; Sensory transduction; Transcription;
KW Transcription regulation.
FT CHAIN 1..540
FT /note="Cryptochrome-1"
FT /id="PRO_0000348598"
FT DOMAIN 5..140
FT /note="Photolyase/cryptochrome alpha/beta"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 410..412
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 416
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 540 AA; 62337 MW; 122BC57A039A1435 CRC64;
MVPRGANVLW FRHGLRLHDN PALLAALEEK DQGIPLIPVF IFDGESAGTK SVGYNRMRFL
LDSLQDLDEQ LQSATEGRGR LFVFEGEPTL IFRRLHEQVR LHKICAELDC EPIWNERDES
ARLLCRELGI EYVEKVSHTL WDPRLVIETN GGIPPLTYQM FLHTVQIIGV PPRPAIDAHI
NDATFIQLAP ELRQHLGCFD QVPNPEHFNI YSDNMGFLAK INWRGGETQA LALLEERLKV
ERNAFERGYY LPNQANPNIQ EAPKSMSAHL RFGCLSVRRF YWSVHDLFEN VQLAACVRGV
QIEGGAHITG QLIWREYFYT MSVNNPNYDR MEGNEICLTI PWAKPDENLL QRWRLGQTGF
PLIDGAMRQL LAEGWLHHTL RNTVATFLTR GGLWQSWEPG LKHFLKYLLD ADWSVCAGNW
MWVSSSAFER LLDSSLVTCP VALAKRLDPE GVYIRRYVPE LKNLPKEYIH EPWRLSAEQQ
VKFECLIGVH YPERIIDLSK AVKRNMMAMT ALRNSLITPP PHCRPSNEEE VRQFFWLANY
