SLR1_ORYSJ
ID SLR1_ORYSJ Reviewed; 625 AA.
AC Q7G7J6; B9FB42; Q18ND8; Q9MB96;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=DELLA protein SLR1 {ECO:0000303|PubMed:11340177};
DE AltName: Full=Gibberellic acid-insensitive mutant protein {ECO:0000303|PubMed:10713441};
DE AltName: Full=OsGAI {ECO:0000303|PubMed:10713441};
DE AltName: Full=Protein SLENDER RICE1 {ECO:0000303|PubMed:11340177};
GN Name=SLR1 {ECO:0000303|PubMed:11340177};
GN Synonyms=GAI {ECO:0000303|PubMed:10713441};
GN OrderedLocusNames=Os03g0707600 {ECO:0000312|EMBL:BAF12946.1},
GN LOC_Os03g49990 {ECO:0000312|EMBL:ABF98475.1};
GN ORFNames=OsJ_12286 {ECO:0000312|EMBL:EEE59780.1},
GN OSJNBb0022E02.5 {ECO:0000312|EMBL:AAK50137.1};
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Seedling;
RX PubMed=10713441; DOI=10.1016/s0378-1119(00)00018-4;
RA Ogawa M., Kusano T., Katsumi M., Sano H.;
RT "Rice gibberellin-insensitive gene homolog, OsGAI, encodes a nuclear-
RT localized protein capable of gene activation at transcriptional level.";
RL Gene 245:21-29(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, POSSIBLE
RP HOMODIMERIZATION, AND DEGRADATION.
RX PubMed=11826299; DOI=10.1105/tpc.010319;
RA Itoh H., Ueguchi-Tanaka M., Sato Y., Ashikari M., Matsuoka M.;
RT "The gibberellin signaling pathway is regulated by the appearance and
RT disappearance of SLENDER RICE1 in nuclei.";
RL Plant Cell 14:57-70(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP MUTAGENESIS OF 39-ASP--ALA-55.
RX PubMed=11340177; DOI=10.2307/3871359;
RA Ikeda A., Ueguchi-Tanaka M., Sonoda Y., Kitano H., Koshioka M.,
RA Futsuhara Y., Matsuoka M., Yamaguchi J.;
RT "slender rice, a constitutive gibberellin response mutant, is caused by a
RT null mutation of the SLR1 gene, an ortholog of the height-regulating gene
RT GAI/RGA/RHT/D8.";
RL Plant Cell 13:999-1010(2001).
RN [9]
RP DEVELOPMENTAL STAGE.
RX PubMed=12834406; DOI=10.1046/j.1365-313x.2003.01780.x;
RA Kaneko M., Itoh H., Inukai Y., Sakamoto T., Ueguchi-Tanaka M., Ashikari M.,
RA Matsuoka M.;
RT "Where do gibberellin biosynthesis and gibberellin signaling occur in rice
RT plants?";
RL Plant J. 35:104-115(2003).
RN [10]
RP PHOSPHORYLATION, UBIQUITINATION, DEGRADATION, AND INTERACTION WITH GID2.
RX PubMed=12649483; DOI=10.1126/science.1081077;
RA Sasaki A., Itoh H., Gomi K., Ueguchi-Tanaka M., Ishiyama K., Kobayashi M.,
RA Jeong D.-H., An G., Kitano H., Ashikari M., Matsuoka M.;
RT "Accumulation of phosphorylated repressor for gibberellin signaling in an
RT F-box mutant.";
RL Science 299:1896-1898(2003).
RN [11]
RP PHOSPHORYLATION, AND INTERACTION WITH GID2.
RX PubMed=14756772; DOI=10.1111/j.1365-313x.2003.01990.x;
RA Gomi K., Sasaki A., Itoh H., Ueguchi-Tanaka M., Ashikari M., Kitano H.,
RA Matsuoka M.;
RT "GID2, an F-box subunit of the SCF E3 complex, specifically interacts with
RT phosphorylated SLR1 protein and regulates the gibberellin-dependent
RT degradation of SLR1 in rice.";
RL Plant J. 37:626-634(2004).
RN [12]
RP INTERACTION WITH GID1.
RX PubMed=16193045; DOI=10.1038/nature04028;
RA Ueguchi-Tanaka M., Ashikari M., Nakajima M., Itoh H., Katoh E.,
RA Kobayashi M., Chow T.-Y., Hsing Y.-I., Kitano H., Yamaguchi I.,
RA Matsuoka M.;
RT "GIBBERELLIN INSENSITIVE DWARF1 encodes a soluble receptor for
RT gibberellin.";
RL Nature 437:693-698(2005).
RN [13]
RP PHOSPHORYLATION.
RX PubMed=15979983; DOI=10.1093/pcp/pci152;
RA Itoh H., Sasaki A., Ueguchi-Tanaka M., Ishiyama K., Kobayashi M.,
RA Hasegawa Y., Minami E., Ashikari M., Matsuoka M.;
RT "Dissection of the phosphorylation of rice DELLA protein, SLENDER RICE1.";
RL Plant Cell Physiol. 46:1392-1399(2005).
RN [14]
RP FUNCTION, INTERACTION WITH HD16/EL1, PHOSPHORYLATION, AND MUTAGENESIS OF
RP SER-196 AND SER-510.
RX PubMed=20400938; DOI=10.1038/emboj.2010.75;
RA Dai C., Xue H.W.;
RT "Rice early flowering1, a CKI, phosphorylates DELLA protein SLR1 to
RT negatively regulate gibberellin signalling.";
RL EMBO J. 29:1916-1927(2010).
RN [15]
RP INTERACTION WITH D14 AND GID1, AND SUBCELLULAR LOCATION.
RX PubMed=24131983; DOI=10.1038/ncomms3613;
RA Nakamura H., Xue Y.L., Miyakawa T., Hou F., Qin H.M., Fukui K., Shi X.,
RA Ito E., Ito S., Park S.H., Miyauchi Y., Asano A., Totsuka N., Ueda T.,
RA Tanokura M., Asami T.;
RT "Molecular mechanism of strigolactone perception by DWARF14.";
RL Nat. Commun. 4:2613-2613(2013).
RN [16]
RP INTERACTION WITH HD16/EL1, AND PHOSPHORYLATION.
RC STRAIN=cv. Koshihikari, and cv. Nipponbare;
RX PubMed=23789941; DOI=10.1111/tpj.12268;
RA Hori K., Ogiso-Tanaka E., Matsubara K., Yamanouchi U., Ebana K., Yano M.;
RT "Hd16, a gene for casein kinase I, is involved in the control of rice
RT flowering time by modulating the day-length response.";
RL Plant J. 76:36-46(2013).
CC -!- FUNCTION: Probable transcriptional regulator that acts as a repressor
CC of the gibberellin (GA) signaling pathway. Probably acts by
CC participating in large multiprotein complexes that repress
CC transcription of GA-inducible genes. Upon GA application, it is
CC degraded by the proteasome, allowing the GA signaling pathway. In
CC contrast, its overexpression prevents the GA signaling pathway and
CC induces a dwarf phenotype. {ECO:0000269|PubMed:10713441,
CC ECO:0000269|PubMed:11826299, ECO:0000269|PubMed:20400938}.
CC -!- SUBUNIT: May be a homodimer. Interacts directly with the GID2 component
CC of the SCF(GID2) complex. Interacts with GID1 in a GA-dependent manner,
CC probably leading to its interaction with GID2 and its subsequent
CC degradation (PubMed:12649483, PubMed:14756772, PubMed:16193045).
CC Interacts with D14 and GID1 in an strigolactone-dependent manner
CC (PubMed:24131983). Interacts with HD16/EL1 (PubMed:20400938,
CC PubMed:23789941). {ECO:0000269|PubMed:12649483,
CC ECO:0000269|PubMed:14756772, ECO:0000269|PubMed:16193045,
CC ECO:0000269|PubMed:20400938, ECO:0000269|PubMed:23789941,
CC ECO:0000269|PubMed:24131983}.
CC -!- INTERACTION:
CC Q7G7J6; Q852L0: HD16; NbExp=2; IntAct=EBI-7913631, EBI-7913614;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10713441,
CC ECO:0000269|PubMed:11826299, ECO:0000269|PubMed:24131983}.
CC -!- TISSUE SPECIFICITY: Expressed in nodes, internodes, leaf sheats of
CC young seedlings and ears of adult plants. Weakly expressed in leaf
CC blade and root. {ECO:0000269|PubMed:10713441}.
CC -!- DEVELOPMENTAL STAGE: At the vegetative stage, it is expressed in
CC rapidly elongating and dividing organs and tissues. At the
CC influorescence or floral stage, it is expressed in the shoot meristems
CC and stamen primordia. {ECO:0000269|PubMed:12834406}.
CC -!- INDUCTION: Up-regulated following GA3 but not ABA application.
CC {ECO:0000269|PubMed:10713441}.
CC -!- DOMAIN: The DELLA motif is required for its GA-induced degradation.
CC -!- PTM: Phosphorylated on Ser/Thr residues in the N-terminal part. Both
CC phosphorylated and unphosphorylated forms are degraded upon GA
CC treatment, suggesting that phosphorylation does not trigger
CC ubiquitination (PubMed:12649483, PubMed:14756772, PubMed:15979983).
CC Phosphorylated by HD16/EL1. Phosphorylation enhances its stability
CC (PubMed:20400938, PubMed:23789941). {ECO:0000269|PubMed:12649483,
CC ECO:0000269|PubMed:14756772, ECO:0000269|PubMed:15979983,
CC ECO:0000269|PubMed:20400938, ECO:0000269|PubMed:23789941}.
CC -!- PTM: Ubiquitinated. Upon GA application it is ubiquitinated by the
CC SCF(GID2) complex, leading to its subsequent degradation.
CC {ECO:0000269|PubMed:12649483}.
CC -!- SIMILARITY: Belongs to the GRAS family. DELLA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EEE59780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB030956; BAA90749.1; -; mRNA.
DR EMBL; AB262980; BAE96289.1; -; Genomic_DNA.
DR EMBL; AC087797; AAK50137.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98475.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12946.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS85987.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE59780.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015631543.1; XM_015776057.1.
DR AlphaFoldDB; Q7G7J6; -.
DR SMR; Q7G7J6; -.
DR BioGRID; 802897; 3.
DR DIP; DIP-59774N; -.
DR IntAct; Q7G7J6; 2.
DR MINT; Q7G7J6; -.
DR STRING; 4530.OS03T0707600-01; -.
DR PaxDb; Q7G7J6; -.
DR PRIDE; Q7G7J6; -.
DR EnsemblPlants; Os03t0707600-01; Os03t0707600-01; Os03g0707600.
DR GeneID; 4333860; -.
DR Gramene; Os03t0707600-01; Os03t0707600-01; Os03g0707600.
DR KEGG; osa:4333860; -.
DR eggNOG; ENOG502QPMG; Eukaryota.
DR HOGENOM; CLU_011924_4_0_1; -.
DR InParanoid; Q7G7J6; -.
DR OMA; VQQENFA; -.
DR OrthoDB; 559310at2759; -.
DR PlantReactome; R-OSA-5679411; Gibberellin signaling.
DR PlantReactome; R-OSA-6787011; Jasmonic acid signaling.
DR PlantReactome; R-OSA-9030908; Underwater shoot and internode elongation.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q7G7J6; OS.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.1290; -; 1.
DR InterPro; IPR038088; DELLA_N_sf.
DR InterPro; IPR030006; TF_DELLA.
DR InterPro; IPR021914; TF_DELLA_N.
DR InterPro; IPR005202; TF_GRAS.
DR PANTHER; PTHR31636; PTHR31636; 1.
DR PANTHER; PTHR31636:SF47; PTHR31636:SF47; 1.
DR Pfam; PF12041; DELLA; 1.
DR Pfam; PF03514; GRAS; 1.
DR PROSITE; PS50985; GRAS; 1.
PE 1: Evidence at protein level;
KW Gibberellin signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..625
FT /note="DELLA protein SLR1"
FT /id="PRO_0000132247"
FT DOMAIN 232..621
FT /note="GRAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..294
FT /note="Leucine repeat I (LRI)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 241..278
FT /note="Required for possible homodimerization"
FT REGION 313..378
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 392..431
FT /note="Leucine repeat II (LRII)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 441..542
FT /note="PFYRE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT REGION 545..621
FT /note="SAW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 39..43
FT /note="DELLA motif"
FT MOTIF 246..250
FT /note="LxCxE motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 344..348
FT /note="VHIID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT MOTIF 449..453
FT /note="LXXLL motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01191"
FT COMPBIAS 182..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 39..55
FT /note="Missing: Induces a dwarf phenotype."
FT /evidence="ECO:0000269|PubMed:11340177"
FT MUTAGEN 196
FT /note="S->A: Decreases protein stability and enhances
FT gibberellin signaling."
FT /evidence="ECO:0000269|PubMed:20400938"
FT MUTAGEN 510
FT /note="S->A: Decreases protein stability and enhances
FT gibberellin signaling."
FT /evidence="ECO:0000269|PubMed:20400938"
FT MUTAGEN 510
FT /note="S->D: Increases protein stability and suppresses
FT gibberellin signaling."
FT /evidence="ECO:0000269|PubMed:20400938"
SQ SEQUENCE 625 AA; 65406 MW; 034FF02719D42E97 CRC64;
MKREYQEAGG SSGGGSSADM GSCKDKVMAG AAGEEEDVDE LLAALGYKVR SSDMADVAQK
LEQLEMAMGM GGVSAPGAAD DGFVSHLATD TVHYNPSDLS SWVESMLSEL NAPLPPIPPA
PPAARHASTS STVTGGGGSG FFELPAAADS SSSTYALRPI SLPVVATADP SAADSARDTK
RMRTGGGSTS SSSSSSSSLG GGASRGSVVE AAPPATQGAA AANAPAVPVV VVDTQEAGIR
LVHALLACAE AVQQENFAAA EALVKQIPTL AASQGGAMRK VAAYFGEALA RRVYRFRPAD
STLLDAAFAD LLHAHFYESC PYLKFAHFTA NQAILEAFAG CHRVHVVDFG IKQGMQWPAL
LQALALRPGG PPSFRLTGVG PPQPDETDAL QQVGWKLAQF AHTIRVDFQY RGLVAATLAD
LEPFMLQPEG EADANEEPEV IAVNSVFELH RLLAQPGALE KVLGTVHAVR PRIVTVVEQE
ANHNSGSFLD RFTESLHYYS TMFDSLEGGS SGQAELSPPA AGGGGGTDQV MSEVYLGRQI
CNVVACEGAE RTERHETLGQ WRNRLGRAGF EPVHLGSNAY KQASTLLALF AGGDGYRVEE
KEGCLTLGWH TRPLIATSAW RVAAA
