CRY1_AEDAE
ID CRY1_AEDAE Reviewed; 545 AA.
AC Q17DK5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cryptochrome-1;
GN Name=cry {ECO:0000250|UniProtKB:O77059}; ORFNames=AAEL004146;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT44496.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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: FAD-binding region regulates cry stability, cry-tim
CC interaction, and circadian photosensitivity.
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}.
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DR EMBL; CH477293; EAT44496.1; -; Genomic_DNA.
DR RefSeq; XP_001648498.1; XM_001648448.1.
DR AlphaFoldDB; Q17DK5; -.
DR SMR; Q17DK5; -.
DR STRING; 7159.AAEL004146-PA; -.
DR GeneID; 5564182; -.
DR KEGG; aag:5564182; -.
DR CTD; 42305; -.
DR VEuPathDB; VectorBase:AAEL004146; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_3_4_1; -.
DR InParanoid; Q17DK5; -.
DR OMA; IWFRHGL; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; Q17DK5; -.
DR Proteomes; UP000008820; Unassembled 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 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; IPR018394; DNA_photolyase_1_CS_C.
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; PS00394; DNA_PHOTOLYASES_1_1; 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..545
FT /note="Cryptochrome-1"
FT /id="PRO_0000348595"
FT DOMAIN 3..138
FT /note="Photolyase/cryptochrome alpha/beta"
FT BINDING 236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 406..408
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 545 AA; 62541 MW; ECE08ED76B6136AE CRC64;
MTVNNILWFR HGLRLHDNPS LLEALRNDGT GSESVRLYPI FIFDGESAGT KLVGFNRMKF
LLESLADLDR QLREIGGQLY VFKGNAVNVM RRLFEELNIR KLCFEQDCEP IWKARDDAIQ
NLCRMMDVKC VEKVSHTLWD PQQIIRTNGG IPPLTYQMFL HTVDIIGKPP RPVAAPSFEF
VEFGSIPSIL AQEVKLQQVR NLSPEDFGIY YEGNPDISHQ QWMGGETKAL ECLGHRLKQE
EEAFLGGYFL PTQAKPEFLV PPTSMSAALR FGCLSVRMFY WCVHDLYEKV QANNQYRNPG
GQHITGQLIW REYFYTMSVH NPHYAEMEAN PICLNIPWYE PKDDSLDRWK EGRTGFPMID
AAMRQLLAEG WLHHILRNIT ATFLTRGALW ISWEAGVQHF LKYLLDADWS VCAGNWMWVS
SSAFEKLLDS SSCTSPIALA RRLDPKGEYV RRYLPELKNL PTLYVHEPWK APLDVQKECG
CIVGRDYPAP MIDLAAASRA NANTMNSIRQ KLMERGGSTP PHCRPSDVEE IRNFFWLPED
VVADC
