GID1_ORYSJ
ID GID1_ORYSJ Reviewed; 354 AA.
AC Q6L545; Q0DI89;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Gibberellin receptor GID1 {ECO:0000303|PubMed:16193045};
DE EC=3.-.-.- {ECO:0000305};
DE AltName: Full=Gibberellin-insensitive dwarf protein 1 {ECO:0000303|PubMed:16193045};
DE AltName: Full=Protein GIBBERELLIN INSENSITIVE DWARF1 {ECO:0000303|PubMed:16193045};
GN Name=GID1 {ECO:0000303|PubMed:16193045};
GN OrderedLocusNames=Os05g0407500 {ECO:0000312|EMBL:BAF17434.1},
GN LOC_Os05g33730 {ECO:0000305};
GN ORFNames=OJ1657_H11.10 {ECO:0000312|EMBL:AAT38036.1},
GN P0040B10.6 {ECO:0000312|EMBL:AAV59435.1};
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, INTERACTION
RP WITH SLR1, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-196 AND ARG-251.
RC STRAIN=cv. Taichung 65;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP INTERACTION WITH SLR1.
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 [9] {ECO:0007744|PDB:3EBL, ECO:0007744|PDB:3ED1}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-354 IN COMPLEXES WITH
RP GIBBERELLIN A3 AND GIBBERELLIN A4.
RX PubMed=19037316; DOI=10.1038/nature07546;
RA Shimada A., Ueguchi-Tanaka M., Nakatsu T., Nakajima M., Naoe Y., Ohmiya H.,
RA Kato H., Matsuoka M.;
RT "Structural basis for gibberellin recognition by its receptor GID1.";
RL Nature 456:520-523(2008).
CC -!- FUNCTION: Functions as soluble gibberellin (GA) receptor. GA is an
CC essential hormone that regulates growth and development in plants.
CC Binds with high affinity the biologically active GAs such as GA1, GA3
CC and GA4, but has low or no affinity for the biologically inactive GAs.
CC Upon GA-binding, it interacts with the DELLA protein SLR1, a repressor
CC of GA signaling. This leads to SLR1 degradation by the proteasome,
CC allowing the GA signaling pathway. {ECO:0000269|PubMed:16193045}.
CC -!- SUBUNIT: Interacts with the DELLA protein SLR1 in a GA-dependent
CC manner, resulting in subsequent SLR1 degradation.
CC {ECO:0000269|PubMed:16193045, ECO:0000269|PubMed:19037316,
CC ECO:0000269|PubMed:24131983}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16193045}.
CC -!- DISRUPTION PHENOTYPE: Severe dwarf phenotype with wide and dark-green
CC leaf blades. Plants insensitive to gibberellic acid (GA).
CC {ECO:0000269|PubMed:16193045}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB211399; BAE45340.1; -; mRNA.
DR EMBL; AC105319; AAT38036.1; -; Genomic_DNA.
DR EMBL; AC137928; AAV59435.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17434.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93968.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE63694.1; -; Genomic_DNA.
DR EMBL; AK074026; BAG93769.1; -; mRNA.
DR RefSeq; XP_015639961.1; XM_015784475.1.
DR PDB; 3EBL; X-ray; 1.90 A; A/B/C/D/E/F=2-354.
DR PDB; 3ED1; X-ray; 1.90 A; A/B/C/D/E/F=2-354.
DR PDBsum; 3EBL; -.
DR PDBsum; 3ED1; -.
DR AlphaFoldDB; Q6L545; -.
DR SMR; Q6L545; -.
DR BioGRID; 807801; 4.
DR DIP; DIP-59773N; -.
DR IntAct; Q6L545; 1.
DR STRING; 4530.OS05T0407500-01; -.
DR ESTHER; orysa-gid1; Plant_carboxylesterase.
DR PaxDb; Q6L545; -.
DR PRIDE; Q6L545; -.
DR EnsemblPlants; Os05t0407500-01; Os05t0407500-01; Os05g0407500.
DR GeneID; 4338764; -.
DR Gramene; Os05t0407500-01; Os05t0407500-01; Os05g0407500.
DR KEGG; osa:4338764; -.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_1_1; -.
DR InParanoid; Q6L545; -.
DR OMA; RAPENRF; -.
DR OrthoDB; 1263520at2759; -.
DR PlantReactome; R-OSA-5679411; Gibberellin signaling.
DR EvolutionaryTrace; Q6L545; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6L545; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0010331; F:gibberellin binding; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0048444; P:floral organ morphogenesis; IBA:GO_Central.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010325; P:raffinose family oligosaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IC:Gramene.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Gibberellin signaling pathway; Hydrolase; Nucleus; Receptor;
KW Reference proteome.
FT CHAIN 1..354
FT /note="Gibberellin receptor GID1"
FT /id="PRO_0000071557"
FT MOTIF 120..122
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 296
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT BINDING 122..123
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3ED1"
FT BINDING 122..123
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3EBL"
FT BINDING 134
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3ED1"
FT BINDING 134
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3EBL"
FT BINDING 198
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3ED1"
FT BINDING 198
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3EBL"
FT BINDING 250
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3ED1"
FT BINDING 327
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3ED1"
FT BINDING 327
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037316,
FT ECO:0007744|PDB:3EBL"
FT MUTAGEN 196
FT /note="G->D: In gid1-1; abolishes binding to GA and ability
FT to degrade SLR1."
FT /evidence="ECO:0000269|PubMed:16193045"
FT MUTAGEN 251
FT /note="R->T: In gid1-2; abolishes binding to GA and ability
FT to degrade SLR1."
FT /evidence="ECO:0000269|PubMed:16193045"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 185..188
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:3EBL"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:3EBL"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:3EBL"
FT HELIX 335..352
FT /evidence="ECO:0007829|PDB:3EBL"
SQ SEQUENCE 354 AA; 39457 MW; EF98C64CE20B96F3 CRC64;
MAGSDEVNRN ECKTVVPLHT WVLISNFKLS YNILRRADGT FERDLGEYLD RRVPANARPL
EGVSSFDHII DQSVGLEVRI YRAAAEGDAE EGAAAVTRPI LEFLTDAPAA EPFPVIIFFH
GGSFVHSSAS STIYDSLCRR FVKLSKGVVV SVNYRRAPEH RYPCAYDDGW TALKWVMSQP
FMRSGGDAQA RVFLSGDSSG GNIAHHVAVR AADEGVKVCG NILLNAMFGG TERTESERRL
DGKYFVTLQD RDWYWKAYLP EDADRDHPAC NPFGPNGRRL GGLPFAKSLI IVSGLDLTCD
RQLAYADALR EDGHHVKVVQ CENATVGFYL LPNTVHYHEV MEEISDFLNA NLYY
