Reviewed, UniProtKB/Swiss-Prot Q43125 (CRY1_ARATH)

Names and origin

Protein names

Recommended name:
    Cryptochrome-1
Alternative name(s):
    Blue light photoreceptor
    Protein OUT OF PHASE 2
      Short name=OOP2
    Protein BLUE LIGHT UNINHIBITED 1
    Protein ELONGATED HYPOCOTYL 4

Gene names

Name:	CRY1
Synonyms:	BLU1, HY4
Ordered Locus Names:	At4g08920
ORF Names:	T3H13.5, T3H13.14

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	681 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Cofactor	Binds 1 FAD per subunit. Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
Enzyme regulation	Light exposure induces a conformational change in the C-terminal domain CCT1 required for activity.
Subunit structure	Homodimer. Interacts with ADO1, COP1 and PHYA.
Subcellular location	Cytoplasm. Nucleus. Note= The nuclear pool is involved in hypocotyl and petiole growth inhibition and anthocyanin production, while the cytoplasmic pool is involved in root growth and cotyledon expansion.
Tissue specificity	Widely expressed.
Domain	The N-terminal domain CNT1 (1-489) is sufficient for autophosphorylation and is required for dimerization. The C-terminal domain CCT1 (490-681) of the homodimer binds to COP1.
Post-translational modification	Autophosphorylated; in response to blue light.
Miscellaneous	Plants lacking CRY1 show reduced root elongation in blue light.
Sequence similarities	Belongs to the DNA photolyase class-1 family. Contains 1 DNA photolyase domain.
Caution	Was originally (Ref.1) thought to be a DNA photolyase.
Sequence caution	The sequence AAB28725.2 differs from that shown. Reason: Frameshift at position 546. The sequence AAD17364.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB78016.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Sensory transduction
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Chromophore FAD Flavoprotein Nucleotide-binding
Molecular function	Photoreceptor protein Receptor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: InterPro protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA photolyase activity Inferred from electronic annotation. Source: InterPro identical protein binding Ref.15 Inferred from physical interaction. Source: IntAct photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		3	EBI-300703,EBI-300703
ADO1	Q94BT6	1	EBI-300703,EBI-300691

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 681

681

Cryptochrome-1

PRO_0000085121

Regions

Nucleotide binding

247 – 251

5

FAD

Sites

Binding site

235

1

FAD

Binding site

359

1

ATP

Binding site

359

1

FAD

Binding site

360

1

ATP

Binding site

390

1

FAD; via carbonyl oxygen

Binding site

392

1

FAD; via amide nitrogen

Binding site

409

1

ATP

Amino acid modifications

Disulfide bond

80 ↔ 190

Experimental info

Mutagenesis

66

1

S → N: Loss of dimerization and activity

Mutagenesis

340

1

G → E: Loss of activity

Mutagenesis

347

1

G → R: Loss of dimerization and activity

Mutagenesis

462

1

A → V: Loss of dimerization and activity

Sequence conflict

40

1

I → N in AAK32756. Ref.3

Sequence conflict

654

1

R → G in AAM70572. Ref.3

Secondary structure

1

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681

Helix Strand Turn

Details...

Beta strand

14 – 20

7

Helix

28 – 36

9

Beta strand

39 – 45

7

Helix

47 – 50

4

Helix

57 – 76

20

Beta strand

81 – 85

5

Helix

89 – 100

12

Beta strand

104 – 108

5

Helix

113 – 127

15

Turn

128 – 130

3

Beta strand

132 – 136

5

Helix

144 – 146

3

Beta 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

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	Q43125-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 372A7E798D6FC076	FASTA	681	76,794
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HY4 gene of A. thaliana encodes a protein with characteristics of a blue-light photoreceptor." Ahmad M., Cashmore A.R. Nature 366:162-166(1993) [PubMed: 8232555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." 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. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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.