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BH063_ARATH
ID   BH063_ARATH             Reviewed;         335 AA.
AC   Q8GY61; O65678; Q8L851; Q8S3D9;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Transcription factor bHLH63;
DE   AltName: Full=Basic helix-loop-helix protein 63;
DE            Short=AtbHLH63;
DE            Short=bHLH 63;
DE   AltName: Full=Protein CRYPTOCHROME INTERACTING BASIC-HELIX-LOOP-HELIX 1;
DE   AltName: Full=Transcription factor EN 84;
DE   AltName: Full=bHLH transcription factor bHLH063;
GN   Name=BHLH63; Synonyms=CIB1, EN84; OrderedLocusNames=At4g34530;
GN   ORFNames=T4L20.110;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=12679534; DOI=10.1093/molbev/msg088;
RA   Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT   "The basic helix-loop-helix transcription factor family in plants: a
RT   genome-wide study of protein structure and functional diversity.";
RL   Mol. Biol. Evol. 20:735-747(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., 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., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   GENE FAMILY.
RX   PubMed=12897250; DOI=10.1105/tpc.013839;
RA   Toledo-Ortiz G., Huq E., Quail P.H.;
RT   "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL   Plant Cell 15:1749-1770(2003).
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=14600211; DOI=10.1105/tpc.151140;
RA   Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA   Jakoby M., Werber M., Weisshaar B.;
RT   "Update on the basic helix-loop-helix transcription factor gene family in
RT   Arabidopsis thaliana.";
RL   Plant Cell 15:2497-2502(2003).
RN   [8]
RP   FUNCTION, INTERACTION WITH CRY2, AND SUBCELLULAR LOCATION.
RX   PubMed=18988809; DOI=10.1126/science.1163927;
RA   Liu H., Yu X., Li K., Klejnot J., Yang H., Lisiero D., Lin C.;
RT   "Photoexcited CRY2 interacts with CIB1 to regulate transcription and floral
RT   initiation in Arabidopsis.";
RL   Science 322:1535-1539(2008).
RN   [9]
RP   INTERACTION WITH IBH1.
RX   PubMed=23161888; DOI=10.1105/tpc.112.105023;
RA   Ikeda M., Fujiwara S., Mitsuda N., Ohme-Takagi M.;
RT   "A triantagonistic basic helix-loop-helix system regulates cell elongation
RT   in Arabidopsis.";
RL   Plant Cell 24:4483-4497(2012).
RN   [10]
RP   BIOTECHNOLOGY.
RX   PubMed=22847441; DOI=10.1073/pnas.1211305109;
RA   Idevall-Hagren O., Dickson E.J., Hille B., Toomre D.K., De Camilli P.;
RT   "Optogenetic control of phosphoinositide metabolism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E2316-E2323(2012).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH CRY2.
RX   PubMed=24130508; DOI=10.1371/journal.pgen.1003861;
RA   Liu Y., Li X., Li K., Liu H., Lin C.;
RT   "Multiple bHLH proteins form heterodimers to mediate CRY2-dependent
RT   regulation of flowering-time in Arabidopsis.";
RL   PLoS Genet. 9:E1003861-E1003861(2013).
RN   [12]
RP   INDUCTION BY BLUE LIGHT.
RC   STRAIN=cv. Columbia;
RX   PubMed=24101505; DOI=10.1073/pnas.1308987110;
RA   Liu H., Wang Q., Liu Y., Zhao X., Imaizumi T., Somers D.E., Tobin E.M.,
RA   Lin C.;
RT   "Arabidopsis CRY2 and ZTL mediate blue-light regulation of the
RT   transcription factor CIB1 by distinct mechanisms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:17582-17587(2013).
RN   [13]
RP   INTERACTION WITH CRY2.
RX   PubMed=24780222; DOI=10.1016/j.ab.2014.04.023;
RA   Cui Y., Choudhury S.R., Irudayaraj J.;
RT   "Quantitative real-time kinetics of optogenetic proteins CRY2 and CIB1/N
RT   using single-molecule tools.";
RL   Anal. Biochem. 458:58-60(2014).
RN   [14]
RP   BIOTECHNOLOGY.
RX   PubMed=24718798; DOI=10.1007/978-1-4939-0470-9_8;
RA   Idevall-Hagren O., Decamilli P.;
RT   "Manipulation of plasma membrane phosphoinositides using photoinduced
RT   protein-protein interactions.";
RL   Methods Mol. Biol. 1148:109-128(2014).
RN   [15]
RP   BIOTECHNOLOGY.
RX   PubMed=25963241; DOI=10.1016/j.chembiol.2015.04.014;
RA   Duan L., Che D., Zhang K., Ong Q., Guo S., Cui B.;
RT   "Optogenetic control of molecular motors and organelle distributions in
RT   cells.";
RL   Chem. Biol. 22:671-682(2015).
CC   -!- FUNCTION: Transcription factor that binds DNA to G box 5'-CACGTG-3'
CC       and, to a lower extent, to E-box 5'-CANNTG-3' in vitro. Binds to
CC       chromatin DNA of the FT gene and promotes its expression, and thus
CC       triggers flowering in response to blue light.
CC       {ECO:0000269|PubMed:18988809, ECO:0000269|PubMed:24130508}.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with IBH1 (PubMed:23161888).
CC       Binds reversibly to CRY2 after blue light illumination
CC       (PubMed:18988809, PubMed:24780222, PubMed:24130508).
CC       {ECO:0000269|PubMed:18988809, ECO:0000269|PubMed:23161888,
CC       ECO:0000269|PubMed:24130508, ECO:0000269|PubMed:24780222, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q8GY61; Q9C8Z9: BHLH148; NbExp=3; IntAct=EBI-4469930, EBI-4434374;
CC       Q8GY61; Q96524: CRY2; NbExp=3; IntAct=EBI-4469930, EBI-531555;
CC       Q8GY61; Q9SKX1: IBH1; NbExp=3; IntAct=EBI-4469930, EBI-4433589;
CC       Q8GY61; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-4469930, EBI-15193025;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:18988809}.
CC   -!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves, and
CC       stems. {ECO:0000269|PubMed:12679534}.
CC   -!- INDUCTION: Accumulates strongly in response to blue light due to
CC       reduced preventing 26S proteasome-mediated degradation in an ADO1/ZTL
CC       and ADO2/LKP2 dependent manner, but levels decrease in the absence of
CC       blue light via 26S proteasome degradation (at protein level).
CC       {ECO:0000269|PubMed:24101505}.
CC   -!- BIOTECHNOLOGY: The blue light-mediated interaction between CRY2 and
CC       BHLH63/CIB1 is used to design an optogenetic control of target proteins
CC       or organelles. {ECO:0000269|PubMed:22847441,
CC       ECO:0000269|PubMed:24718798, ECO:0000269|PubMed:25963241}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF488596; AAM10952.1; -; mRNA.
DR   EMBL; AL023094; CAA18832.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161585; CAB80170.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86389.1; -; Genomic_DNA.
DR   EMBL; AK117846; BAC42487.1; -; mRNA.
DR   EMBL; AY120741; AAM53299.1; -; mRNA.
DR   EMBL; BT005313; AAO63377.1; -; mRNA.
DR   PIR; T05273; T05273.
DR   RefSeq; NP_195179.2; NM_119618.3.
DR   AlphaFoldDB; Q8GY61; -.
DR   SMR; Q8GY61; -.
DR   BioGRID; 14886; 40.
DR   DIP; DIP-59356N; -.
DR   IntAct; Q8GY61; 48.
DR   STRING; 3702.AT4G34530.1; -.
DR   PaxDb; Q8GY61; -.
DR   PRIDE; Q8GY61; -.
DR   EnsemblPlants; AT4G34530.1; AT4G34530.1; AT4G34530.
DR   GeneID; 829604; -.
DR   Gramene; AT4G34530.1; AT4G34530.1; AT4G34530.
DR   KEGG; ath:AT4G34530; -.
DR   Araport; AT4G34530; -.
DR   TAIR; locus:2139484; AT4G34530.
DR   eggNOG; ENOG502QT6X; Eukaryota.
DR   HOGENOM; CLU_025018_1_0_1; -.
DR   InParanoid; Q8GY61; -.
DR   OMA; FPNSSKM; -.
DR   OrthoDB; 1022319at2759; -.
DR   PhylomeDB; Q8GY61; -.
DR   PRO; PR:Q8GY61; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0045824; P:negative regulation of innate immune response; IMP:TAIR.
DR   GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR   GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IDA:TAIR.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR024097; bHLH_ZIP_TF.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR12565; PTHR12565; 3.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Flowering; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..335
FT                   /note="Transcription factor bHLH63"
FT                   /id="PRO_0000358758"
FT   DOMAIN          178..228
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          110..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        86
FT                   /note="L -> F (in Ref. 5; AAM53299)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="M -> V (in Ref. 1; AAM10952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  37540 MW;  05F0CA14FC2B3C7A CRC64;
     MNGAIGGDLL LNFPDMSVLE RQRAHLKYLN PTFDSPLAGF FADSSMITGG EMDSYLSTAG
     LNLPMMYGET TVEGDSRLSI SPETTLGTGN FKKRKFDTET KDCNEKKKKM TMNRDDLVEE
     GEEEKSKITE QNNGSTKSIK KMKHKAKKEE NNFSNDSSKV TKELEKTDYI HVRARRGQAT
     DSHSIAERVR REKISERMKF LQDLVPGCDK ITGKAGMLDE IINYVQSLQR QIEFLSMKLA
     IVNPRPDFDM DDIFAKEVAS TPMTVVPSPE MVLSGYSHEM VHSGYSSEMV NSGYLHVNPM
     QQVNTSSDPL SCFNNGEAPS MWDSHVQNLY GNLGV
 
 
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