CRY1_ANOGA
ID CRY1_ANOGA Reviewed; 545 AA.
AC Q7PYI7; Q0QW08;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cryptochrome-1;
DE Short=agCRY1 {ECO:0000303|PubMed:16332522};
GN Name=Cry1 {ECO:0000312|EMBL:ABB29886.1}; ORFNames=AGAP001958;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000312|EMBL:ABB29886.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16332522; DOI=10.1016/j.cub.2005.11.030;
RA Zhu H., Yuan Q., Briscoe A.D., Froy O., Casselman A., Reppert S.M.;
RT "The two CRYs of the butterfly.";
RL Curr. Biol. 15:R953-R954(2005).
RN [2] {ECO:0000312|EMBL:EAA01270.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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; DQ219482; ABB29886.1; -; mRNA.
DR EMBL; AAAB01008987; EAA01270.4; -; Genomic_DNA.
DR RefSeq; XP_321104.4; XM_321104.5.
DR AlphaFoldDB; Q7PYI7; -.
DR SMR; Q7PYI7; -.
DR STRING; 7165.AGAP001958-PA; -.
DR PaxDb; Q7PYI7; -.
DR GeneID; 1281165; -.
DR KEGG; aga:AgaP_AGAP001958; -.
DR CTD; 1281165; -.
DR VEuPathDB; VectorBase:AGAP001958; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_3_4_1; -.
DR InParanoid; Q7PYI7; -.
DR OMA; IWFRHGL; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; Q7PYI7; -.
DR Proteomes; UP000007062; Chromosome 2R.
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:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
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 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 2: Evidence at transcript level;
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_0000348594"
FT DOMAIN 3..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 308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 407..409
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 413
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 545 AA; 62497 MW; 88814BF4D3945D2E CRC64;
MTINNILWFR HGLRLHDNPS LLEALKSDCV NQSSEAVKLF PIFIFDGESA GTRIVGYNRM
KFLLESLADL DRQFRDLGGQ LLVFRGDSVT VLRRLFEELN IKKLCYEQDC EPIWKERDDA
VAKLCRTMDV RCVENVSHTL WNPIEVIQTN GDIPPLTYQM FLHTVNIIGD PPRPVGAPNF
EYVEFGRVPA LLASELKLCQ QMPAPDDFGI HYDGNARIAF QKWIGGETRA LEALGARLKQ
EEEAFREGYY LPTQAKPEIL GPATSMSAAL RFGCLSVRMF YWCVHDLFAK VQSNSQFKYP
GGHHITGQLI WREYFYTMSV QNPHYGEMER NPICLNIPWY KPEDDSLTRW KEGRTGFPMI
DAAMRQLLAE GWLHHILRNI TATFLTRGGL WLSWEEGLQH FLKYLLDADW SVCAGNWMWV
SSSAFERLLD SSKCTCPIAL ARRLDPKGDY VKRYLPELAN YPAQFVHEPW KASREQQIEY
GCVIGEKYPA PMVDLAIVSK RNAHTMASLR EKLVDGGSTP PHCRPSDIEE IRQFFWLADD
AATEA
