SPL14_ORYSJ
ID SPL14_ORYSJ Reviewed; 417 AA.
AC Q7EXZ2; B7F043; D8WJ58;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Squamosa promoter-binding-like protein 14 {ECO:0000303|PubMed:16861571};
DE Short=OsSPL14 {ECO:0000303|PubMed:16861571};
DE AltName: Full=Protein IDEAL PLANT ARCHITECTURE 1 {ECO:0000303|PubMed:20495565};
DE AltName: Full=Protein WEALTHY FARMER'S PANICLE {ECO:0000303|PubMed:20495564};
GN Name=SPL14 {ECO:0000303|PubMed:16861571};
GN Synonyms=IPA1 {ECO:0000303|PubMed:20495565},
GN WFP {ECO:0000303|PubMed:20495564};
GN OrderedLocusNames=Os08g0509600 {ECO:0000312|EMBL:BAT06187.1},
GN LOC_Os08g39890 {ECO:0000305};
GN ORFNames=B1168A08.33 {ECO:0000312|EMBL:BAD10674.1},
GN OSJNBa0016N23.108 {ECO:0000312|EMBL:BAD10733.1};
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND VARIANT ILE-292.
RX PubMed=20495565; DOI=10.1038/ng.591;
RA Jiao Y., Wang Y., Xue D., Wang J., Yan M., Liu G., Dong G., Zeng D., Lu Z.,
RA Zhu X., Qian Q., Li J.;
RT "Regulation of OsSPL14 by OsmiR156 defines ideal plant architecture in
RT rice.";
RL Nat. Genet. 42:541-544(2010).
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 TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16861571; DOI=10.1104/pp.106.084475;
RA Xie K., Wu C., Xiong L.;
RT "Genomic organization, differential expression, and interaction of SQUAMOSA
RT promoter-binding-like transcription factors and microRNA156 in rice.";
RL Plant Physiol. 142:280-293(2006).
RN [7]
RP GENE FAMILY.
RX PubMed=17629421; DOI=10.1016/j.gene.2007.02.034;
RA Yang Z., Wang X., Gu S., Hu Z., Xu H., Xu C.;
RT "Comparative study of SBP-box gene family in Arabidopsis and rice.";
RL Gene 407:1-11(2008).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20495564; DOI=10.1038/ng.592;
RA Miura K., Ikeda M., Matsubara A., Song X.J., Ito M., Asano K., Matsuoka M.,
RA Kitano H., Ashikari M.;
RT "OsSPL14 promotes panicle branching and higher grain productivity in
RT rice.";
RL Nat. Genet. 42:545-549(2010).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22960246; DOI=10.1093/pcp/pcs122;
RA Luo L., Li W., Miura K., Ashikari M., Kyozuka J.;
RT "Control of tiller growth of rice by OsSPL14 and strigolactones, which work
RT in two independent pathways.";
RL Plant Cell Physiol. 53:1793-1801(2012).
RN [10]
RP FUNCTION, INTERACTION WITH PCF1 AND PCF2, AND SUBCELLULAR LOCATION.
RX PubMed=24170127; DOI=10.1105/tpc.113.113639;
RA Lu Z., Yu H., Xiong G., Wang J., Jiao Y., Liu G., Jing Y., Meng X., Hu X.,
RA Qian Q., Fu X., Wang Y., Li J.;
RT "Genome-wide binding analysis of the transcription activator ideal plant
RT architecture1 reveals a complex network regulating rice plant
RT architecture.";
RL Plant Cell 25:3743-3759(2013).
RN [11]
RP FUNCTION.
RX PubMed=26519999; DOI=10.1016/j.gene.2015.10.062;
RA Srikanth B., Subhakara Rao I., Surekha K., Subrahmanyam D., Voleti S.R.,
RA Neeraja C.N.;
RT "Enhanced expression of OsSPL14 gene and its association with yield
RT components in rice (Oryza sativa) under low nitrogen conditions.";
RL Gene 576:441-450(2016).
RN [12]
RP FUNCTION, AND INTERACTION WITH D53.
RX PubMed=28809396; DOI=10.1038/cr.2017.102;
RA Song X., Lu Z., Yu H., Shao G., Xiong J., Meng X., Jing Y., Liu G.,
RA Xiong G., Duan J., Yao X.F., Liu C.M., Li H., Wang Y., Li J.;
RT "IPA1 functions as a downstream transcription factor repressed by D53 in
RT strigolactone signaling in rice.";
RL Cell Res. 27:1128-1141(2017).
RN [13]
RP INTERACTION WITH IPI1, SUBCELLULAR LOCATION, AND UBIQUITINATION BY IPI1.
RX PubMed=28298520; DOI=10.1105/tpc.16.00879;
RA Wang J., Yu H., Xiong G., Lu Z., Jiao Y., Meng X., Liu G., Chen X.,
RA Wang Y., Li J.;
RT "Tissue-specific ubiquitination by IPA1 INTERACTING PROTEIN1 modulates IPA1
RT protein levels to regulate plant architecture in rice.";
RL Plant Cell 29:697-707(2017).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT SER-163, AND MUTAGENESIS OF SER-163.
RX PubMed=30190406; DOI=10.1126/science.aat7675;
RA Wang J., Zhou L., Shi H., Chern M., Yu H., Yi H., He M., Yin J., Zhu X.,
RA Li Y., Li W., Liu J., Wang J., Chen X., Qing H., Wang Y., Liu G., Wang W.,
RA Li P., Wu X., Zhu L., Zhou J.M., Ronald P.C., Li S., Li J., Chen X.;
RT "A single transcription factor promotes both yield and immunity in rice.";
RL Science 361:1026-1028(2018).
RN [15]
RP FUNCTION, AND INTERACTION WITH SLR1.
RX PubMed=30886331; DOI=10.1038/s41477-019-0383-2;
RA Liu M., Shi Z., Zhang X., Wang M., Zhang L., Zheng K., Liu J., Hu X.,
RA Di C., Qian Q., He Z., Yang D.L.;
RT "Inducible overexpression of Ideal Plant Architecture1 improves both yield
RT and disease resistance in rice.";
RL Nat. Plants 5:389-400(2019).
RN [16]
RP INTERACTION WITH SHI1.
RX PubMed=30914468; DOI=10.1105/tpc.19.00023;
RA Duan E., Wang Y., Li X., Lin Q., Zhang T., Wang Y., Zhou C., Zhang H.,
RA Jiang L., Wang J., Lei C., Zhang X., Guo X., Wang H., Wan J.;
RT "OsSHI1 regulates plant architecture through modulating the transcriptional
RT activity of IPA1 in rice.";
RL Plant Cell 31:1026-1042(2019).
CC -!- FUNCTION: Transcriptional activator that binds to the SBP-box DNA core
CC binding motif 5'-GTAC-3' (PubMed:24170127). Can target the TCP motif
CC 5'-TGGGCC/T-3' through interaction with PCF1 and PCF2
CC (PubMed:24170127). Key regulator of the plant architecture that
CC controls shoot branching and panicle development (PubMed:20495565,
CC PubMed:20495564, PubMed:22960246). Promotes panicle branching
CC (PubMed:20495565, PubMed:20495564, PubMed:22960246, PubMed:26519999).
CC Promotes high grain yield (PubMed:20495565, PubMed:20495564,
CC PubMed:26519999). Binds to the promoters of TB1 and DEP1
CC (PubMed:24170127). Suppresses rice tillering mainly through positive
CC regulation of TB1 (PubMed:24170127). Regulates plant height and panicle
CC length through positive regulation of DEP1 (PubMed:24170127). Repressed
CC by D53 in strigolactone (SL) signaling (PubMed:28809396). Acts with D53
CC to mediate the SL-regulated tiller development (PubMed:28809396).
CC Functions as a direct downstream component of D53 in regulating tiller
CC number and SL-induced gene expression (PubMed:28809396). Binds directly
CC to the D53 promoter and plays a critical role in the negative feedback
CC regulation of SL-induced D53 expression (PubMed:28809396). Involved in
CC defense response against pathogens (PubMed:30190406, PubMed:30886331).
CC Phosphorylated at Ser-163 in response to infection by the fungal
CC pathogen Magnaporthe oryzae (PubMed:30190406). Phosphorylation reduces
CC SPL14/IPA1 binding to the GTAC site in the DEP1 promoter and enhances
CC binding to the TGGGCC site in the WRKY45 promoter (PubMed:30190406).
CC Binding to the promoter of the pathogen defense gene WRKY45 activates
CC its expression, leading to enhanced disease resistance
CC (PubMed:30190406). Reduces gibberellin-mediated disease susceptibility
CC by stabilizing SLR1 (PubMed:30886331). Possesses transactivation
CC activity in yeast cells (PubMed:20495564).
CC {ECO:0000269|PubMed:20495564, ECO:0000269|PubMed:20495565,
CC ECO:0000269|PubMed:22960246, ECO:0000269|PubMed:24170127,
CC ECO:0000269|PubMed:26519999, ECO:0000269|PubMed:28809396,
CC ECO:0000269|PubMed:30190406, ECO:0000269|PubMed:30886331}.
CC -!- SUBUNIT: Interacts with PCF1 and PCF2 (PubMed:24170127). Interacts with
CC IPI1 (PubMed:28298520). Interacts with D53 (PubMed:28809396). Interacts
CC with SLR1 (PubMed:30886331). Interacts (via C-terminus) with SHI1
CC (PubMed:30914468). {ECO:0000269|PubMed:24170127,
CC ECO:0000269|PubMed:28298520, ECO:0000269|PubMed:28809396,
CC ECO:0000269|PubMed:30886331, ECO:0000269|PubMed:30914468}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20495564,
CC ECO:0000269|PubMed:20495565, ECO:0000269|PubMed:24170127,
CC ECO:0000269|PubMed:28298520}.
CC -!- TISSUE SPECIFICITY: Expressed in young panicles (PubMed:16861571).
CC Expressed in the shoot apex at both the vegetative and reproductive
CC stages (PubMed:20495565, PubMed:20495564, PubMed:22960246). Highly
CC expressed in the promordia of primary and secondary branches
CC (PubMed:20495565, PubMed:22960246). Highly expressed in young panicles
CC (PubMed:20495564). {ECO:0000269|PubMed:16861571,
CC ECO:0000269|PubMed:20495564, ECO:0000269|PubMed:20495565,
CC ECO:0000269|PubMed:22960246}.
CC -!- INDUCTION: Negatively regulated by microRNA miR156.
CC {ECO:0000269|PubMed:16861571, ECO:0000269|PubMed:20495564,
CC ECO:0000269|PubMed:20495565, ECO:0000269|PubMed:22960246}.
CC -!- DOMAIN: The SBP-type zinc finger is required for the binding to DNA.
CC {ECO:0000305|PubMed:24170127}.
CC -!- PTM: Phosphorylated at Ser-163 in response to infection by the fungal
CC pathogen Magnaporthe oryzae. {ECO:0000269|PubMed:30190406}.
CC -!- PTM: Ubiquitinated by IPI1, which leads to proteasomal degradation.
CC {ECO:0000269|PubMed:28298520}.
CC -!- MISCELLANEOUS: Plants overexpressing SPL14/IPA1 exhibit enhanced
CC disease resistance against the bacterial pathogen Xanthomonas oryzae pv
CC oryzae (Xoo), and increased grain yield. {ECO:0000269|PubMed:30886331}.
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DR EMBL; GU136674; ADJ19220.1; -; Genomic_DNA.
DR EMBL; AP005816; BAD10674.1; -; Genomic_DNA.
DR EMBL; AP006049; BAD10733.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24118.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06187.1; -; Genomic_DNA.
DR EMBL; AK107191; BAG97990.1; -; mRNA.
DR AlphaFoldDB; Q7EXZ2; -.
DR SMR; Q7EXZ2; -.
DR STRING; 4530.OS08T0509600-01; -.
DR PaxDb; Q7EXZ2; -.
DR PRIDE; Q7EXZ2; -.
DR EnsemblPlants; Os08t0509600-01; Os08t0509600-01; Os08g0509600.
DR Gramene; Os08t0509600-01; Os08t0509600-01; Os08g0509600.
DR eggNOG; ENOG502QPVZ; Eukaryota.
DR HOGENOM; CLU_057950_0_0_1; -.
DR InParanoid; Q7EXZ2; -.
DR OMA; PWDTTTH; -.
DR PlantReactome; R-OSA-9030908; Underwater shoot and internode elongation.
DR PlantReactome; R-OSA-9035605; Regulation of seed size.
DR PlantReactome; R-OSA-9608575; Reproductive meristem phase change.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q7EXZ2; OS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IDA:UniProtKB.
DR Gene3D; 4.10.1100.10; -; 1.
DR InterPro; IPR004333; SBP_dom.
DR InterPro; IPR036893; SBP_sf.
DR InterPro; IPR044817; SPL.
DR PANTHER; PTHR31251; PTHR31251; 1.
DR Pfam; PF03110; SBP; 1.
DR SUPFAM; SSF103612; SSF103612; 1.
DR PROSITE; PS51141; ZF_SBP; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..417
FT /note="Squamosa promoter-binding-like protein 14"
FT /id="PRO_0000308241"
FT ZN_FING 101..178
FT /note="SBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..177
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00470"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30190406"
FT VARIANT 292
FT /note="L -> I (in strain: cv. Shaoniejing; induces an ideal
FT plant phenotype with a reduced tiller number, increased
FT lodging resistance and enhanced grain yield)"
FT /evidence="ECO:0000269|PubMed:20495565"
FT MUTAGEN 163
FT /note="S->D: Mimics constitutive phosphorylation; reduces
FT binding to the GTAC site in the DEP1 promoter and enhances
FT binding to the TGGGCC site in the WRKY45 promoter."
FT /evidence="ECO:0000269|PubMed:30190406"
SQ SEQUENCE 417 AA; 42379 MW; DBEC3A9399C515C7 CRC64;
MEMASGGGAA AAAGGGVGGS GGGGGGGDEH RQLHGLKFGK KIYFEDAAAA AGGGGTGSGS
GSASAAPPSS SSKAAGGGRG GGGKNKGKGV AAAAPPPPPP PPRCQVEGCG ADLSGIKNYY
CRHKVCFMHS KAPRVVVAGL EQRFCQQCSR FHLLPEFDQG KRSCRRRLAG HNERRRRPQT
PLASRYGRLA ASVGEHRRFR SFTLDFSYPR VPSSVRNAWP AIQPGDRISG GIQWHRNVAP
HGHSSAVAGY GANTYSGQGS SSSGPPVFAG PNLPPGGCLA GVGAATDSSC ALSLLSTQPW
DTTTHSAAAS HNQAAAMSTT TSFDGNPVAP SAMAGSYMAP SPWTGSRGHE GGGRSVAHQL
PHEVSLDEVH PGPSHHAHFS GELELALQGN GPAPAPRIDP GSGSTFDQTS NTMDWSL
