CRY1_CHICK
ID CRY1_CHICK Reviewed; 621 AA.
AC Q8QG61;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Cryptochrome-1;
GN Name=CRY1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Pineal gland;
RX PubMed=11684328; DOI=10.1016/s0304-3940(01)02227-3;
RA Yamamoto K., Okano T., Fukada Y.;
RT "Chicken pineal Cry genes: light-dependent up-regulation of cCry1 and cCry2
RT transcripts.";
RL Neurosci. Lett. 313:13-16(2001).
CC -!- FUNCTION: Transcriptional repressor which forms a core component of the
CC circadian clock. The circadian clock, an internal time-keeping system,
CC regulates various physiological processes through the generation of
CC approximately 24 hour circadian rhythms in gene expression, which are
CC translated into rhythms in metabolism and behavior. It is derived from
CC the Latin roots 'circa' (about) and 'diem' (day) and acts as an
CC important regulator of a wide array of physiological functions
CC including metabolism, sleep, body temperature, blood pressure,
CC endocrine, immune, cardiovascular, and renal function. Consists of two
CC major components: the central clock, residing in the suprachiasmatic
CC nucleus (SCN) of the brain, and the peripheral clocks that are present
CC in nearly every tissue and organ system. Both the central and
CC peripheral clocks can be reset by environmental cues, also known as
CC Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the
CC central clock is light, which is sensed by retina and signals directly
CC to the SCN. The central clock entrains the peripheral clocks through
CC neuronal and hormonal signals, body temperature and feeding-related
CC cues, aligning all clocks with the external light/dark cycle. Circadian
CC rhythms allow an organism to achieve temporal homeostasis with its
CC environment at the molecular level by regulating gene expression to
CC create a peak of protein expression once every 24 hours to control when
CC a particular physiological process is most active with respect to the
CC solar day. Transcription and translation of core clock components
CC (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and
CC CRY2) plays a critical role in rhythm generation, whereas delays
CC imposed by post-translational modifications (PTMs) are important for
CC determining the period (tau) of the rhythms (tau refers to the period
CC of a rhythm and is the length, in time, of one complete cycle). A
CC diurnal rhythm is synchronized with the day/night cycle, while the
CC ultradian and infradian rhythms have a period shorter and longer than
CC 24 hours, respectively. Disruptions in the circadian rhythms contribute
CC to the pathology of cardiovascular diseases, cancer, metabolic
CC syndromes and aging. A transcription/translation feedback loop (TTFL)
CC forms the core of the molecular circadian clock mechanism.
CC Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2,
CC form the positive limb of the feedback loop, act in the form of a
CC heterodimer and activate the transcription of core clock genes and
CC clock-controlled genes (involved in key metabolic processes), harboring
CC E-box elements (5'-CACGTG-3') within their promoters. The core clock
CC genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form
CC the negative limb of the feedback loop and interact with the
CC CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its
CC activity and thereby negatively regulating their own expression. This
CC heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G,
CC which form a second feedback loop and which activate and repress
CC ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant
CC functions but also differential and selective contributions at least in
CC defining the pace of the SCN circadian clock and its circadian
CC transcriptional outputs. More potent transcriptional repressor in
CC cerebellum and liver than CRY2, though more effective in lengthening
CC the period of the SCN oscillator. On its side, CRY2 seems to play a
CC critical role in tuning SCN circadian period by opposing the action of
CC CRY1. With CRY2, is dispensable for circadian rhythm generation but
CC necessary for the development of intercellular networks for rhythm
CC synchrony. Capable of translocating circadian clock core proteins such
CC as PER proteins to the nucleus (By similarity). Interacts with CLOCK-
CC ARNTL/BMAL1 independently of PER proteins and is found at CLOCK-
CC ARNTL/BMAL1-bound sites, suggesting that CRY may act as a molecular
CC gatekeeper to maintain CLOCK-ARNTL/BMAL1 in a poised and repressed
CC state until the proper time for transcriptional activation (By
CC similarity). Represses CLOCK-ARNTL/BMAL1-mediated transcriptional
CC activation (PubMed:11684328). {ECO:0000250|UniProtKB:P97784,
CC ECO:0000250|UniProtKB:Q16526, ECO:0000269|PubMed:11684328}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P97784};
CC Note=Binds 1 FAD per subunit. Only a minority of the protein molecules
CC contain bound FAD. Contrary to the situation in photolyases, the FAD is
CC bound in a shallow, surface-exposed pocket.
CC {ECO:0000250|UniProtKB:P97784};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per
CC subunit. {ECO:0000250};
CC -!- SUBUNIT: Component of the circadian core oscillator, which includes the
CC CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1E, and
CC the PER proteins. {ECO:0000250|UniProtKB:P97784}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P97784}. Nucleus
CC {ECO:0000250|UniProtKB:P97784}. Note=Translocated to the nucleus
CC through interaction with other Clock proteins such as PER2 or ARNTL.
CC {ECO:0000250|UniProtKB:P97784}.
CC -!- TISSUE SPECIFICITY: Expressed in the pineal gland.
CC {ECO:0000269|PubMed:11684328}.
CC -!- INDUCTION: Up-regulated by light. Higher levels in light/dark cycle
CC than in total darkness. {ECO:0000269|PubMed:11684328}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
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DR EMBL; AY034432; AAK61385.1; -; mRNA.
DR RefSeq; NP_989576.1; NM_204245.1.
DR AlphaFoldDB; Q8QG61; -.
DR SMR; Q8QG61; -.
DR STRING; 9031.ENSGALP00000020598; -.
DR PaxDb; Q8QG61; -.
DR GeneID; 374093; -.
DR KEGG; gga:374093; -.
DR CTD; 1407; -.
DR VEuPathDB; HostDB:geneid_374093; -.
DR eggNOG; KOG0133; Eukaryota.
DR InParanoid; Q8QG61; -.
DR OrthoDB; 378952at2759; -.
DR PhylomeDB; Q8QG61; -.
DR PRO; PR:Q8QG61; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; IDA:AgBase.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:AgBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR GO; GO:0032922; P:circadian regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IBA:GO_Central.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; ISS:UniProtKB.
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 SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 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..621
FT /note="Cryptochrome-1"
FT /id="PRO_0000261145"
FT DOMAIN 3..132
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 581..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..54
FT /note="LIR 1"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 82..87
FT /note="LIR 2"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 151..156
FT /note="LIR 3"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 255..260
FT /note="LIR 4"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 271..276
FT /note="LIR 5"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 285..290
FT /note="LIR 6"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 335..339
FT /note="LIR 7"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 379..384
FT /note="LIR 8"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 395..400
FT /note="LIR 9"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 411..416
FT /note="LIR 10"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 430..435
FT /note="LIR 11"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 486..491
FT /note="LIR 12"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT MOTIF 492..497
FT /note="LIR 13"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT BINDING 252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT BINDING 355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97784"
FT BINDING 387..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97784"
SQ SEQUENCE 621 AA; 69672 MW; 5E549707689664E3 CRC64;
MGVNAVHWFR KGLRLHDNPA LRECIRGADT VRCVYILDPW FAGSSNVGIN RWRFLLQCLE
DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WSIAKLSIEY DSEPFGKERD AAIKKLASEA
GVEVIVRISH TLYDLDKIIE LNGGQPPLTY KRFQTLISRM EPLEMPVETI TPEVMQKCTT
PVSDDHDEKY GVPSLEELGF DTDGLPSAVW PGGETEALTR LERHLERKAW VANFERPRMN
ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYKKVKKNS SPPLSLYGQL LWREFFYTAA
TNNPRFDKME GNPICVQIPW DKNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA
VACFLTRGDL WISWEEGMKV FEELLLDADW SVNAGSWMWL SCSSFFQQFF HCYCPVGFGR
RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA PESVQKAAKC VIGVNYPKPM VNHAEASRLN
IERMKQIYQQ LSRYRGLGLL ATVPSNPNGN GNGGLMSFSP GESISGCSSA GGAQLGTGDG
QTVGVQTCAL GDSHTGGSGV QQQGYCQASS ILRYAHGDNQ QSHLMQPGRA SLGTGISAGK
RPNPEEETQS VGPKVQRQST N
