CRY1_CULQU
ID CRY1_CULQU Reviewed; 499 AA.
AC B0WRR9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Cryptochrome-1;
GN Name=cry {ECO:0000250|UniProtKB:O77059}; ORFNames=CPIJ009455;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000312|EMBL:EDS33478.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000312|EMBL:EDS33478.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 Functions, together with per, as a transcriptional repressor required
CC for the 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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- DOMAIN: DNA photolyase domain is sufficient for light detection and
CC phototransduction. {ECO:0000250|UniProtKB:O77059}.
CC -!- DOMAIN: FAD-binding region regulates cry stability, cry-tim
CC interaction, and circadian photosensitivity.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000255}.
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DR EMBL; DS232059; EDS33478.1; -; Genomic_DNA.
DR RefSeq; XP_001851403.1; XM_001851351.1.
DR AlphaFoldDB; B0WRR9; -.
DR SMR; B0WRR9; -.
DR STRING; 7176.CPIJ009455-PA; -.
DR EnsemblMetazoa; XM_038265885.1; XP_038121813.1; LOC6042266.
DR GeneID; 6042266; -.
DR KEGG; cqu:CpipJ_CPIJ009455; -.
DR VEuPathDB; VectorBase:CPIJ009455; -.
DR VEuPathDB; VectorBase:CQUJHB009977; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_546603_0_0_1; -.
DR InParanoid; B0WRR9; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; B0WRR9; -.
DR Proteomes; UP000002320; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR PANTHER; PTHR11455; PTHR11455; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 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..499
FT /note="Cryptochrome-1"
FT /id="PRO_0000348596"
FT BINDING 190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 360..362
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 56272 MW; A847E3EC46CC7280 CRC64;
MTDKVRNRVQ CWPALAQESS CVDFIPARQG ATCGSTVVFI PCCGLTRGRR VLCQWFPCLS
GGCCSQESSC VDFIPARQGA TCGSTVVFIP CCGLTRGRRV LCQWFPCLSG GCCSQHTVNI
IGEPPRPVGA PSFEFVEFGR LPSILSTELK LFQRAPVPED FGIYYEGNAD IARQRWTGGE
AKALELLGRR LKQEEEAFRE GYYLPTQARP DFLAPPSSMS AALRFGCLSV RMFYWCVHDL
FARVQANNQL KHPGGHHITG QLIWREYFYT MSVHNPHYAV MELNPICLNI PWYEAKDDSL
DRWKEGRTGF PLIDAAMRQL MAEGWLHHIL RNITATFLTR GGLWISWEAG VQHFLKYLLD
ADWSVCAGNW MWVSSSAFEK LLDSSSCTSP VALARRLDPK GEYVKRYLPE LEKFPALYVH
EPWKAPPELQ EQYGCVIGKD YPAPMVNLAE VNKCNANKMN AIRQKLLDQG GSTPAHCRPS
DMDEVRQFFW LPEDVAAES
