ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q43125


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CRY1_ARATH
Primary accession number Q43125
Secondary accession numbers Q43126 Q8L7Y1 Q9ASZ2 Q9M0S9 Q9ZPF0
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1997 (Sequence version 1)
Annotations were last modified on    May 20, 2008 (Entry version 77)
Name and origin of the protein
Protein name Cryptochrome-1
Synonym Blue light photoreceptor
Gene name
Name: CRY1
Synonyms: HY4
OrderedLocusNames: At4g08920
ORFNames: T3H13.5, T3H13.14
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1038/366162a0; PubMed=8232555 [NCBI, ExPASy, EBI, Israel, Japan]
Ahmad M., Cashmore A.R.;
"HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor.";
Nature 366:162-166(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
CHARACTERIZATION.
PubMed=8953250 [NCBI, ExPASy, EBI, Israel, Japan]
Lin C., Ahmad M., Cashmore A.R.;
"Arabidopsis cryptochrome 1 is a soluble protein mediating blue light-dependent regulation of plant growth and development.";
Plant J. 10:893-902(1996).
[5]
INTERACTION WITH ADO1.
DOI=10.1038/35068589; PubMed=11260718 [NCBI, ExPASy, EBI, Israel, Japan]
Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M., Ecker J.R., Cashmore A.R.;
"An Arabidopsis circadian clock component interacts with both CRY1 and phyB.";
Nature 410:487-490(2001).
[6]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-509 IN COMPLEX WITH FAD AND ATP, AND BINDING SITES.
DOI=10.1073/pnas.0404851101; PubMed=15299148 [NCBI, ExPASy, EBI, Israel, Japan]
Brautigam C.A., Smith B.S., Ma Z., Palnitkar M., Tomchick D.R., Machius M., Deisenhofer J.;
"Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 101:12142-12147(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
S66907; AAB28724.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S66909; AAB28725.2; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF128396; AAD17364.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161513; CAB78016.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF361588; AAK32756.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY124863; AAM70572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR H85089; H85089.
S39058; S39058.
UniGene At.27730
3D structure databases
PDB
1U3C; X-ray; 2.60 A; A=1-509.[ExPASy / RCSB / EBI]
1U3D; X-ray; 2.45 A; A=1-509.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1U3C; -.
1U3D; -.
DisProt DP00474; -.
ModBase Q43125.
Protein-protein interaction databases
IntAct Q43125; -.
Organism-specific databases
TAIR At4g08920; -.
Gene expression databases
ArrayExpress Q43125; -.
GermOnline AT4G08920; Arabidopsis thaliana.
Ontologies
GO
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR002081; Cryptochrome/DNA_photolyase_1.
IPR014134; Cryptochrome_pln.
IPR006050; DNA_photolyase_N.
IPR005101; Photolyase_FAD-bd/Cryptochr_C.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF00875; DNA_photolyase; 1.
PF03441; FAD_binding_7; 1.
Pfam graphical view of domain structure.
PRINTS PR00147; DNAPHOTLYASE.
ProDom PD004390; FAD_binding_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR02766; crypt_chrom_pln; 1.
PROSITE PS00394; DNA_PHOTOLYASES_1_1; 1.
PS00691; DNA_PHOTOLYASES_1_2; 1.
BLOCKS Q43125.
Genome annotation databases
GenomeReviews CT486007_GR; AT4G08920.
Other
ProtoNet Q43125.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Chromophore; Complete proteome; FAD; Flavoprotein; Nucleotide-binding; Photoreceptor protein; Receptor; Sensory transduction.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   681  681     Cryptochrome-1. PRO_0000085121
NP_BIND   247   251  5     FAD. 
BINDING   235   235        FAD. 
BINDING   359   359        ATP. 
BINDING   359   359        FAD. 
BINDING   360   360        ATP. 
BINDING   390   390        FAD; via carbonyl oxygen. 
BINDING   392   392        FAD; via amide nitrogen. 
BINDING   409   409        ATP. 
DISULFID   80   190         
CONFLICT   40    40        I -> N (in Ref. 3; AAK32756). 
CONFLICT   654   654        R -> G (in Ref. 3; AAM70572). 
STRAND   14    20  7      
HELIX   28    36  9      
STRAND   39    45  7      
HELIX   47    50  4      
HELIX   57    76  20      
STRAND   81    85  5      
HELIX   89   100  12      
STRAND   104   108  5      
HELIX   113   127  15      
TURN   128   130  3      
STRAND   132   136  5      
HELIX   144   146  3      
STRAND   150   152  3      
HELIX   158   166  9      
HELIX   187   189  3      
HELIX   200   206  7      
HELIX   209   212  4      
HELIX   217   228  12      
HELIX   231   234  4      
TURN   235   240  6      
STRAND   242   244  3      
HELIX   251   255  5      
HELIX   261   278  18      
HELIX   281   305  25      
TURN   308   312  5      
TURN   318   321  4      
HELIX   328   336  9      
HELIX   342   354  13      
HELIX   359   371  13      
HELIX   377   387  11      
HELIX   393   404  12      
HELIX   419   426  8      
HELIX   431   436  6      
HELIX   438   440  3      
HELIX   445   448  4      
TURN   451   453  3      
HELIX   456   462  7      
TURN   467   469  3      
HELIX   477   495  19      
Sequence information
Length: 681 AA [This is the length of the unprocessed precursor] Molecular weight: 76794 Da [This is the MW of the unprocessed precursor] CRC64: 372A7E798D6FC076 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGSVSGCGS GGCSIVWFRR DLRVEDNPAL AAAVRAGPVI ALFVWAPEEE GHYHPGRVSR 

        70         80         90        100        110        120 
WWLKNSLAQL DSSLRSLGTC LITKRSTDSV ASLLDVVKST GASQIFFNHL YDPLSLVRDH 

       130        140        150        160        170        180 
RAKDVLTAQG IAVRSFNADL LYEPWEVTDE LGRPFSMFAA FWERCLSMPY DPESPLLPPK 

       190        200        210        220        230        240 
KIISGDVSKC VADPLVFEDD SEKGSNALLA RAWSPGWSNG DKALTTFING PLLEYSKNRR 

       250        260        270        280        290        300 
KADSATTSFL SPHLHFGEVS VRKVFHLVRI KQVAWANEGN EAGEESVNLF LKSIGLREYS 

       310        320        330        340        350        360 
RYISFNHPYS HERPLLGHLK FFPWAVDENY FKAWRQGRTG YPLVDAGMRE LWATGWLHDR 

       370        380        390        400        410        420 
IRVVVSSFFV KVLQLPWRWG MKYFWDTLLD ADLESDALGW QYITGTLPDS REFDRIDNPQ 

       430        440        450        460        470        480 
FEGYKFDPNG EYVRRWLPEL SRLPTDWIHH PWNAPESVLQ AAGIELGSNY PLPIVGLDEA 

       490        500        510        520        530        540 
KARLHEALSQ MWQLEAASRA AIENGSEEGL GDSAEVEEAP IEFPRDITME ETEPTRLNPN 

       550        560        570        580        590        600 
RRYEDQMVPS ITSSLIRPEE DEESSLNLRN SVGDSRAEVP RNMVNTNQAQ QRRAEPASNQ 

       610        620        630        640        650        660 
VTAMIPEFNI RIVAESTEDS TAESSSSGRR ERSGGIVPEW SPGYSEQFPS EENRIGGGST 

       670        680 
TSSYLQNHHE ILNWRRLSQT G 

Q43125 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!