General information | DisProt: | DP00474 | Name: | Cryptochrome-1 | Synonym(s): | CRY1_ARATH
CRY1
Blue light photoreceptor
Protein OUT OF PHASE 2
OOP2
Protein BLUE LIGHT UNINHIBITED 1
Protein ELONGATED HYPOCOTYL 4
HY4
| First appeared in release: | Release 3.1 (03/31/2006) | UniProt: | Q43125 | UniGene: | At.27730 | SwissProt: | CRY1_ARATH | TrEMBL: | | NCBI (GI): | 2499553 | Source organism: | Arabidopsis thaliana (Mouse-ear cress) | Sequence length: | 681 | Percent disordered: | 26% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MSGSVSGCGS GGCSIVWFRR DLRVEDNPAL AAAVRAGPVI ALFVWAPEEE GHYHPGRVSR - 60 WWLKNSLAQL DSSLRSLGTC LITKRSTDSV ASLLDVVKST GASQIFFNHL YDPLSLVRDH - 120 RAKDVLTAQG IAVRSFNADL LYEPWEVTDE LGRPFSMFAA FWERCLSMPY DPESPLLPPK - 180 KIISGDVSKC VADPLVFEDD SEKGSNALLA RAWSPGWSNG DKALTTFING PLLEYSKNRR - 240 KADSATTSFL SPHLHFGEVS VRKVFHLVRI KQVAWANEGN EAGEESVNLF LKSIGLREYS - 300 RYISFNHPYS HERPLLGHLK FFPWAVDENY FKAWRQGRTG YPLVDAGMRE LWATGWLHDR - 360 IRVVVSSFFV KVLQLPWRWG MKYFWDTLLD ADLESDALGW QYITGTLPDS REFDRIDNPQ - 420 FEGYKFDPNG EYVRRWLPEL SRLPTDWIHH PWNAPESVLQ AAGIELGSNY PLPIVGLDEA - 480 KARLHEALSQ MWQLEAASRA AIENGSEEGL GDSAEVEEAP IEFPRDITME ETEPTRLNPN - 540 RRYEDQMVPS ITSSLIRPEE DEESSLNLRN SVGDSRAEVP RNMVNTNQAQ QRRAEPASNQ - 600 VTAMIPEFNI RIVAESTEDS TAESSSSGRR ERSGGIVPEW SPGYSEQFPS EENRIGGGST - 660 TSSYLQNHHE ILNWRRLSQT G
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Functional narrative |
Blue light has played a particularly important role as a driving force in evolution since it is the only component of the sunlight spectrum to penetrate to significant depths in aquatic environments, such as those in which life began on earth. Five classes of blue-light photoreceptors have been identified in bacteria, fungi, plants, and animals. These include the BLUF-domain proteins (AppA, PAC), PAS-domain proteins (PYP, wc-1), phototropins, UV/blue opsins, and photolyase/cryptochrome family. Of these blue-light photoreceptors, only the latter is shared by all of these diverse organisms. Cryptochromes were initially identified as putative photoreceptors because of their high degree of homology to the blue-light-activated DNA repair enzyme photolyase and the observation that, like photolyase, they contain two chromophores, a photoantenna pigment, folate, and the catalytic chromophore FAD. Photolyases catalyze the lightdependent repair of UV-induced cyclobutane pyrimidine dimers or pyrimidine-pyrimidone photoproducts in DNA, whereas cryptochromes lack DNA repair activity and act as photoreceptors for a variety of growth and adaptive responses, such as circadian rhythms and light-dependent transcriptional regulation. The photocycle of photolyase is well characterized. Photolyase binds UV-damaged DNA independently of light; absorption of a photon by the photoantenna MTHF is followed by resonance energy transfer to the catalytic chromophore FADH-, which splits the photoproduct by nonreductive electron transfer. Mediates blue light-induced gene expression through the inhibition of COP1-mediated degradation of the transcription factor BIT1. Involved in blue light-dependent stomatal opening, CHS gene expression, inhibition of stem growth and increase of root growth.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | C-terminal domain | Location: | 506 - 681 | Length: | 176 | Region sequence: |
SEEGLGDSAEVEEAPIEFPRDITMEETEPTRLNPNRRYEDQMVPSITSSLIRPEEDEESS LNLRNSVGDSRAEVPRNMVNTNQAQQRRAEPASNQVTAMIPEFNIRIVAESTEDSTAESS SSGRRERSGGIVPEWSPGYSEQFPSEENRIGGGSTTSSYLQNHHEILNWRRLSQTG | Modification type: | Fragment
Native
| PDB: | | Structural/functional type: | Function arises via a disorder to order transition | Functional classes: | | Functional subclasses: | Intraprotein interaction
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (295 K; pH: 7; 0.1 cm path length; 10 mM sodium phosphate; protein concentrations ranging from 0.08 to 0.2 mg/mL)
- Nuclear magnetic resonance (NMR) (293 K; pH: 7; 1-1.5 mM protein; 15N labeled AtCry1-CT; 40 mM sodium phosphate, 50 mM NaCl; 7% (v/v) D2O, 0.02% NaN3)
- Sensitivity to proteolysis (298 K; PBS buffer; trypsin titration)
| References:
- Partch CL, Clarkson MW, Ozgur S, Lee AL, Sancar A. "Role of structural plasticity in signal transduction by the cryptochrome blue-light photoreceptor." Biochemistry. 2005; 44(10): 3795-805. PubMed: 15751956
| Comments:The C-terminal domain of AtCry1 (AtCry1-CT, residues 506-
681) was studied.
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References |
- Partch CL, Sancar A. "Photochemistry and photobiology of cryptochrome blue-light photopigments: the search for a photocycle." Photochem Photobiol. 2005; 81(6): 1291-304. PubMed: 16164372
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Comments |
UniGene ID: Rra.13924, Rsa.16362
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