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Description:
Cryptochrome 1 apoprotein (Blue light photoreceptor).
Molecular weight: 76794
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
07-MAR-2006, entry version 49.
Phylogenetic order:
Eukaryota Viridiplantae Streptophyta Embryophyta Tracheophyta Spermatophyta Magnoliophyta eudicotyledons core eudicotyledons rosids eurosids II Brassicales Brassicaceae Arabidopsis.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein CRY1_ARATH:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | S66907 | AAB28724.1 | - |
| EMBL | S66909 | AAB28725.2.1 | ALT_FRAME |
| EMBL | AF128396 | AAD17364.1 | ALT_SEQ |
| EMBL | AL161513 | CAB78016.1 | ALT_SEQ |
| EMBL | AF361588 | AAK32756.1 | - |
| EMBL | AY124863 | AAM70572.1 | - |
| PIR | S39058 | S39058. | |
| PDB | 1U3C | X-ray | A=1-509. |
| PDB | 1U3D | X-ray | A=1-509. |
| IntAct | Q43125 | -.1 | |
| GenomeReviews | CT486007_GR | AT4G08920.1 | |
| TAIR | At4g08920 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| InterPro | IPR002081 | DNA_photolyase_1. | |
| InterPro | IPR006050 | DNA_photolyase_N. | |
| InterPro | IPR006051 | FAD_bd_N. | |
| InterPro | IPR005101 | Photolyse_FAD_bd. | |
| Pfam | PF00875 | DNA_photolyase | 1. |
| Pfam | PF03441 | FAD_binding_7 | 1. |
| PRINTS | PR00147 | DNAPHOTLYASE. | |
| ProDom | PD004390 | FAD_binding_N | 1. |
| PROSITE | PS00394 | DNA_PHOTOLYASES_1_1 | 1. |
| PROSITE | PS00691 | DNA_PHOTOLYASES_1_2 | 1. |
Keywords:
3D-structure; ATP-binding; Chromophore; FAD; Flavoprotein; Nucleotide-binding; Photoreceptor protein; Receptor; Sensory transduction.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=94050142; PubMed=8232555; DOI=10.1038/366162a0;
RA Ahmad M., Cashmore A.R.;
RT "HY4 gene of A. thaliana encodes a protein with characteristics of a
RT blue-light photoreceptor.";
RL Nature 366:162-166(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA Van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP CHARACTERIZATION.
RX MEDLINE=97111378; PubMed=8953250;
RA Lin C., Ahmad M., Cashmore A.R.;
RT "Arabidopsis cryptochrome 1 is a soluble protein mediating blue light-
RT dependent regulation of plant growth and development.";
RL Plant J. 10:893-902(1996).
RN [5]
RP INTERACTION WITH ADO1.
RX MEDLINE=21160352; PubMed=11260718; DOI=10.1038/35068589;
RA Jarillo J.A., Capel J., Tang R.-H., Yang H.-Q., Alonso J.M.,
RA Ecker J.R., Cashmore A.R.;
RT "An Arabidopsis circadian clock component interacts with both CRY1 and
RT phyB.";
RL Nature 410:487-490(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-509 IN COMPLEX WITH FAD
RP AND ATP, AND BINDING SITES.
RX PubMed=15299148; DOI=10.1073/pnas.0404851101;
RA Brautigam C.A., Smith B.S., Ma Z., Palnitkar M., Tomchick D.R.,
RA Machius M., Deisenhofer J.;
RT "Structure of the photolyase-like domain of cryptochrome 1 from
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12142-12147(2004).
Feature:
CHAIN 1 681 Cryptochrome 1 apoprotein.
/FTId=PRO_0000085121.
NP_BIND 247 251 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
STRAND 24 24
TURN 25 26
HELIX 28 36
STRAND 37 37
STRAND 39 45
HELIX 47 50
TURN 51 52
HELIX 57 76
TURN 77 78
STRAND 81 85
STRAND 87 87
HELIX 89 100
STRAND 104 108
STRAND 112 112
HELIX 113 127
TURN 128 130
STRAND 132 136
STRAND 139 139
STRAND 141 142
HELIX 144 146
STRAND 150 152
STRAND 156 157
HELIX 158 166
TURN 167 167
STRAND 169 170
STRAND 180 180
STRAND 184 184
TURN 185 186
HELIX 187 189
STRAND 190 191
HELIX 200 206
TURN 207 208
HELIX 209 212
STRAND 216 216
HELIX 217 228
TURN 229 230
HELIX 231 234
TURN 235 240
STRAND 242 244
TURN 245 246
STRAND 247 247
HELIX 251 255
TURN 256 257
STRAND 258 259
HELIX 261 278
TURN 279 279
HELIX 281 305
STRAND 306 307
TURN 308 312
STRAND 313 313
STRAND 315 315
TURN 318 321
HELIX 328 336
TURN 337 337
STRAND 339 340
HELIX 342 354
STRAND 355 355
HELIX 359 371
TURN 372 372
STRAND 373 373
HELIX 377 387
TURN 389 390
HELIX 393 404
TURN 405 405
STRAND 407 407
TURN 408 409
STRAND 413 414
HELIX 419 426
TURN 428 429
STRAND 430 430
HELIX 431 436
HELIX 438 440
TURN 441 442
HELIX 445 448
TURN 449 449
TURN 451 453
STRAND 454 454
HELIX 456 462
TURN 463 463
STRAND 466 466
TURN 467 469
STRAND 470 470
STRAND 474 475
HELIX 477 495
Comments:
-!- FUNCTION: Mediates blue light-induced gene expression in addition
to its role in blue light-dependent inhibition of stem growth. Is
involved in the blue light-induction of CHS gene expression.
-!- COFACTOR: Binds 1 FAD noncovalently per subunit.
-!- SUBUNIT: Interacts with ADO1.
-!- INTERACTION:
Q9LDF6:LKP1; NbExp=1; IntAct=EBI-300703, EBI-300691;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
-!- CAUTION: Was originally (Ref.1) thought to be a DNA photolyase.
-!- CAUTION: Ref.1 (AAB28725) sequence differs from that shown due to
a frameshift in position 546.
-!- CAUTION: Ref.2 sequences differ from that shown due to erroneous
gene model prediction.
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Sequence length: 681
MSGSVSGCGS GGCSIVWFRR DLRVEDNPAL AAAVRAGPVI ALFVWAPEEE GHYHPGRVSR
WWLKNSLAQL DSSLRSLGTC LITKRSTDSV ASLLDVVKST GASQIFFNHL YDPLSLVRDH
RAKDVLTAQG IAVRSFNADL LYEPWEVTDE LGRPFSMFAA FWERCLSMPY DPESPLLPPK
KIISGDVSKC VADPLVFEDD SEKGSNALLA RAWSPGWSNG DKALTTFING PLLEYSKNRR
KADSATTSFL SPHLHFGEVS VRKVFHLVRI KQVAWANEGN EAGEESVNLF LKSIGLREYS
RYISFNHPYS HERPLLGHLK FFPWAVDENY FKAWRQGRTG YPLVDAGMRE LWATGWLHDR
IRVVVSSFFV KVLQLPWRWG MKYFWDTLLD ADLESDALGW QYITGTLPDS REFDRIDNPQ
FEGYKFDPNG EYVRRWLPEL SRLPTDWIHH PWNAPESVLQ AAGIELGSNY PLPIVGLDEA
KARLHEALSQ MWQLEAASRA AIENGSEEGL GDSAEVEEAP IEFPRDITME ETEPTRLNPN
RRYEDQMVPS ITSSLIRPEE DEESSLNLRN SVGDSRAEVP RNMVNTNQAQ QRRAEPASNQ
VTAMIPEFNI RIVAESTEDS TAESSSSGRR ERSGGIVPEW SPGYSEQFPS EENRIGGGST
TSSYLQNHHE ILNWRRLSQT G