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Database: UniProt
Entry: A0A2R8ZDU0_PANPA
LinkDB: A0A2R8ZDU0_PANPA
Original site: A0A2R8ZDU0_PANPA 
ID   A0A2R8ZDU0_PANPA        Unreviewed;       586 AA.
AC   A0A2R8ZDU0;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Cryptochrome-1 {ECO:0000256|ARBA:ARBA00021159};
GN   Name=CRY1 {ECO:0000313|Ensembl:ENSPPAP00000003201.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000003201.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000003201.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000003201.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   EMBL; AJFE02116999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02117007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003832588.1; XM_003832540.2.
DR   AlphaFoldDB; A0A2R8ZDU0; -.
DR   STRING; 9597.ENSPPAP00000003201; -.
DR   Ensembl; ENSPPAT00000014816.1; ENSPPAP00000003201.1; ENSPPAG00000013513.1.
DR   GeneID; 100968247; -.
DR   KEGG; pps:100968247; -.
DR   CTD; 1407; -.
DR   GeneTree; ENSGT00940000155455; -.
DR   OMA; TPYKNAW; -.
DR   OrthoDB; 124765at2759; -.
DR   Proteomes; UP000240080; Chromosome 12.
DR   Bgee; ENSPPAG00000013513; Expressed in testis and 6 other cell types or tissues.
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:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR   GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000240080};
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   REGION          545..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   586 AA;  66363 MW;  96A5B09A637E6212 CRC64;
     MGVNAVHWFR KGLRLHDNPA LKECIQGADT IRCVYILDPW FAGSSNVGIN RWRFLLQCLE
     DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WNITKLSIEY DSEPFGKERD AAIKKLATEA
     GVEVIVRISH TLYDLDKIIE LNGGQPPLTY KRFQTLISKM EPLEIPVETI TSEVIEKCTT
     PLSDDHDEKY GVPSLEELGF DTDGLSSAVW 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 GGFMGYSAEN IPGCSSSGSC SQGSGILHYA
     HGDSQQTHLL KQGRSSVGTG LSGGKRPSQE EDTQSIGPKV QRQSTN
//
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