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PIL13_ORYSJ
ID   PIL13_ORYSJ             Reviewed;         410 AA.
AC   Q10CH5;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Transcription factor PHYTOCHROME INTERACTING FACTOR-LIKE 13 {ECO:0000303|PubMed:17485859};
DE            Short=OsPIL13 {ECO:0000303|PubMed:17485859};
DE            Short=PIF-like protein 13 {ECO:0000305};
DE   AltName: Full=Basic helix-loop-helix protein 152 {ECO:0000303|PubMed:16896230};
DE            Short=OsbHLH152 {ECO:0000303|PubMed:16896230};
DE   AltName: Full=OsPIL1 {ECO:0000303|PubMed:22984180};
GN   Name=PIL13 {ECO:0000303|PubMed:17485859};
GN   Synonyms=BHLH152 {ECO:0000303|PubMed:16896230},
GN   PIL1 {ECO:0000303|PubMed:22984180};
GN   OrderedLocusNames=Os03g0782500 {ECO:0000312|EMBL:BAF13379.1},
GN   LOC_Os03g56950 {ECO:0000312|EMBL:ABF99196.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16896230; DOI=10.1104/pp.106.080580;
RA   Li X., Duan X., Jiang H., Sun Y., Tang Y., Yuan Z., Guo J., Liang W.,
RA   Chen L., Yin J., Ma H., Wang J., Zhang D.;
RT   "Genome-wide analysis of basic/helix-loop-helix transcription factor family
RT   in rice and Arabidopsis.";
RL   Plant Physiol. 141:1167-1184(2006).
RN   [7]
RP   FUNCTION, INTERACTION WITH PRR1, AND INDUCTION.
RX   PubMed=17485859; DOI=10.1271/bbb.60643;
RA   Nakamura Y., Kato T., Yamashino T., Murakami M., Mizuno T.;
RT   "Characterization of a set of phytochrome-interacting factor-like bHLH
RT   proteins in Oryza sativa.";
RL   Biosci. Biotechnol. Biochem. 71:1183-1191(2007).
RN   [8]
RP   INTERACTION WITH LF AND PRR1, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Zhonghua 11;
RX   PubMed=21549224; DOI=10.1016/j.nbt.2011.04.006;
RA   Zhao X.L., Shi Z.Y., Peng L.T., Shen G.Z., Zhang J.L.;
RT   "An atypical HLH protein OsLF in rice regulates flowering time and
RT   interacts with OsPIL13 and OsPIL15.";
RL   New Biotechnol. 28:788-797(2011).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=22984180; DOI=10.1073/pnas.1207324109;
RA   Todaka D., Nakashima K., Maruyama K., Kidokoro S., Osakabe Y., Ito Y.,
RA   Matsukura S., Fujita Y., Yoshiwara K., Ohme-Takagi M., Kojima M.,
RA   Sakakibara H., Shinozaki K., Yamaguchi-Shinozaki K.;
RT   "Rice phytochrome-interacting factor-like protein OsPIL1 functions as a key
RT   regulator of internode elongation and induces a morphological response to
RT   drought stress.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:15947-15952(2012).
CC   -!- FUNCTION: Transcription factor that may act as negative regulator of
CC       phyB-dependent light signal transduction (PubMed:17485859).
CC       Transcription activator that acts as positive regulator of internode
CC       elongation. May function via regulation of cell wall-related genes. May
CC       play a role in a drought-associated growth-restriction mechanism in
CC       response to drought stress (PubMed:22984180).
CC       {ECO:0000269|PubMed:17485859, ECO:0000269|PubMed:22984180}.
CC   -!- SUBUNIT: Interacts with PRR1 (PubMed:17485859, PubMed:21549224).
CC       Interacts with LF (PubMed:21549224). {ECO:0000269|PubMed:17485859,
CC       ECO:0000269|PubMed:21549224}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC       ECO:0000269|PubMed:21549224, ECO:0000269|PubMed:22984180}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the node portions of the stem.
CC       Expressed in the leaves and the basal part of shoots.
CC       {ECO:0000269|PubMed:22984180}.
CC   -!- INDUCTION: Induced by light in dark-grown etiolated seedlings
CC       (PubMed:17485859). Circadian oscillation under 12 h light/12 h dark
CC       cycle conditions, with peaks in the middle of the light period
CC       (PubMed:17485859, PubMed:22984180). Down-regulated by cold and drought
CC       stresses (PubMed:22984180). {ECO:0000269|PubMed:17485859,
CC       ECO:0000269|PubMed:22984180}.
CC   -!- MISCELLANEOUS: Overexpression of PIL13 in transgenic plants promotes
CC       internode elongation. Expression of a chimeric repressor in transgenic
CC       plants results in short internode sections. Alteration of internode
CC       cell size causes the change in internode length.
CC       {ECO:0000269|PubMed:22984180}.
CC   -!- SIMILARITY: Belongs to the bHLH protein family. {ECO:0000305}.
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DR   EMBL; DP000009; ABF99196.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99198.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13379.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS86695.1; -; Genomic_DNA.
DR   EMBL; AK105637; BAG97322.1; -; mRNA.
DR   AlphaFoldDB; Q10CH5; -.
DR   SMR; Q10CH5; -.
DR   IntAct; Q10CH5; 1.
DR   STRING; 4530.OS03T0782500-01; -.
DR   PaxDb; Q10CH5; -.
DR   PRIDE; Q10CH5; -.
DR   EnsemblPlants; Os03t0782500-01; Os03t0782500-01; Os03g0782500.
DR   Gramene; Os03t0782500-01; Os03t0782500-01; Os03g0782500.
DR   eggNOG; ENOG502QTIX; Eukaryota.
DR   HOGENOM; CLU_030314_3_1_1; -.
DR   InParanoid; Q10CH5; -.
DR   OMA; QLWHSVT; -.
DR   PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR   PlantReactome; R-OSA-5679411; Gibberellin signaling.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0080006; P:internode patterning; IMP:UniProtKB.
DR   GO; GO:0090229; P:negative regulation of red or far-red light signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR031066; bHLH_ALC-like_plant.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR45855; PTHR45855; 1.
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; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..410
FT                   /note="Transcription factor PHYTOCHROME INTERACTING FACTOR-
FT                   LIKE 13"
FT                   /id="PRO_0000444469"
FT   DOMAIN          220..269
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          82..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          137..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..233
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          234..269
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          357..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..106
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   410 AA;  43855 MW;  B16555CFBEC589B9 CRC64;
     MAICSTDNEL VELLWHNGGV VAQPQAAQAR VVSSSGRGQS ASVLTGDDTE TAAWFPDTLD
     DALEKDLYTQ LWRSVTGDAF PAAAAAGPSS HHAPPPDLPP PAARPPMRSG IGSSWTGDIC
     SAFCGSNHIP ETAAQRCRDA GAALPPERPR RSSTHDGAGT SSSGGSGSNF GASGLPSESA
     SAHKRKGRED SDSRSEDAEC EATEETKSSS RRYGSKRRTR AAEVHNLSER RRRDRINEKM
     RALQELIPHC NKTDKASILD EAIEYLKSLQ MQVQIMWMTT GMAPMMFPGA HQFMPPMAVG
     MNSACMPAAQ GLSHMSRLPY MNHSMPNHIP LNSSPAMNPM NVANQMQNIQ LREASNPFLH
     PDGWQTVPPQ VSGPYASGPQ VAQQNQIPKA SASTVLPNSG AEQPPTSDGI
 
 
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