ID A0A6P3TA66_SHEEP Unreviewed; 587 AA. AC A0A6P3TA66; B3F206; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 29-MAY-2024, entry version 17. DE RecName: Full=Cryptochrome-1 {ECO:0000256|ARBA:ARBA00021159}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|EMBL:ABS44879.1}; RN [1] {ECO:0000313|EMBL:ABS44879.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18953409; DOI=10.1371/journal.pone.0003530; RA Dardente H., Mendoza J., Fustin J.M., Challet E., Hazlerigg D.G.; RT "Implication of the F-Box Protein FBXL21 in circadian pacemaker function in RT mammals."; RL PLoS ONE 3:E3530-E3530(2008). RN [2] {ECO:0000313|EMBL:ABS44879.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19341811; DOI=10.1016/j.cbpa.2009.03.016; RA Dardente H., Fustin J.M., Hazlerigg D.G.; RT "Transcriptional feedback loops in the ovine circadian clock."; RL Comp. Biochem. Physiol. 153:391-398(2009). CC -!- COFACTOR: CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate; CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family. CC {ECO:0000256|ARBA:ARBA00005862}. 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; EF494243; ABS44879.1; -; mRNA. DR RefSeq; NP_001123207.1; NM_001129735.1. DR RefSeq; XP_012014825.1; XM_012159435.2. DR AlphaFoldDB; A0A6P3TA66; -. DR SMR; A0A6P3TA66; -. DR GeneID; 443263; -. DR KEGG; oas:443263; -. DR CTD; 1407; -. DR OrthoDB; 124765at2759; -. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0070888; F:E-box binding; IEA:Ensembl. DR GO; GO:0071949; F:FAD binding; IEA:TreeGrafter. DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl. DR GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl. DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl. DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl. DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl. DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl. DR GO; GO:0019915; P:lipid storage; IEA:Ensembl. DR GO; GO:0042754; P:negative regulation of circadian rhythm; IEA:Ensembl. DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:2000323; P:negative regulation of glucocorticoid receptor signaling pathway; IEA:Ensembl. DR GO; GO:2000850; P:negative regulation of glucocorticoid secretion; IEA:Ensembl. DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl. DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl. DR GO; GO:0032868; P:response to insulin; IEA:Ensembl. DR GO; GO:0042770; P:signal transduction in response to DNA damage; IEA:Ensembl. DR Gene3D; 1.25.40.80; -; 2. DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1. DR Gene3D; 3.40.50.620; HUPs; 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; CRYPTOCHROME; 1. DR PANTHER; PTHR11455:SF16; CRYPTOCHROME-1; 1. DR Pfam; PF00875; DNA_photolyase; 1. DR Pfam; PF03441; FAD_binding_7; 1. DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1. DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1. DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1. PE 2: Evidence at transcript level; KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081- KW 1}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Photoreceptor protein {ECO:0000256|ARBA:ARBA00022543}; KW Receptor {ECO:0000256|ARBA:ARBA00023170}; KW Repressor {ECO:0000256|ARBA:ARBA00022491}; KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606}; KW Transcription {ECO:0000256|ARBA:ARBA00023163}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}. FT DOMAIN 3..132 FT /note="Photolyase/cryptochrome alpha/beta" FT /evidence="ECO:0000259|PROSITE:PS51645" FT BINDING 289..296 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT BINDING 387..389 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1" FT SITE 320 FT /note="Electron transfer via tryptophanyl radical" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2" FT SITE 374 FT /note="Electron transfer via tryptophanyl radical" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2" FT SITE 397 FT /note="Electron transfer via tryptophanyl radical" FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2" SQ SEQUENCE 587 AA; 66454 MW; 4EEA4025338CE66D CRC64; MGVNAVHWFR KGLRLHDNPA LKECIQGADT IRCVYILDPW FAGSSNVGIN RWRFLLQCLE DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WNITKLSIEY DSEPFGKERD AAIKKLATEA GVEVIIRISH TLYDLDKIIE LNGGQPPLTY KRFQTLISKM EPLEIPVETI TSEVMEKCTT PLSDDHDEKY GVPSLEELGF DTDGLPSAVW PGGETEALTR LERHLERKAW VANFERPRMN ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYKKVKKNS SPPLSLYGQL LWREFFYTAA TNNPRFDKME GNPICVQIPW DKNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA VACFLTRGDL WISWEEGMKV FEELLLDADW SINAGSWMWL SCSSFFQQFF HCYCPVGFGR RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA PEGIQKVAKC LIGVNYPKPM VNHAEASRLN IERMKQIYQQ LSRYRGLGLL ASVPSNPNGN GGLMGYSPGE NIPGCSSSAS CTQGSGILHY AHGDSQQTHL LKQGRSSTAA GLGSGKRPSQ EEDTQSVGPK VQRQSTN //