GID1A_ARATH
ID GID1A_ARATH Reviewed; 345 AA.
AC Q9MAA7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Gibberellin receptor GID1A;
DE EC=3.-.-.-;
DE AltName: Full=AtCXE10;
DE AltName: Full=Carboxylesterase 10;
DE AltName: Full=GID1-like protein 1;
DE AltName: Full=Protein GA INSENSITIVE DWARF 1A;
DE Short=AtGID1A;
GN Name=GID1A; Synonyms=CXE10, GID1L1; OrderedLocusNames=At3g05120;
GN ORFNames=T12H1.8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=14738307; DOI=10.1007/s00239-003-2492-8;
RA Marshall S.D., Putterill J.J., Plummer K.M., Newcomb R.D.;
RT "The carboxylesterase gene family from Arabidopsis thaliana.";
RL J. Mol. Evol. 57:487-500(2003).
RN [5]
RP FUNCTION, INTERACTION WITH GAI AND RGA, AND DISRUPTION PHENOTYPE.
RX PubMed=17194763; DOI=10.1105/tpc.106.047415;
RA Griffiths J., Murase K., Rieu I., Zentella R., Zhang Z.L., Powers S.J.,
RA Gong F., Phillips A.L., Hedden P., Sun T.P., Thomas S.G.;
RT "Genetic characterization and functional analysis of the GID1 gibberellin
RT receptors in Arabidopsis.";
RL Plant Cell 18:3399-3414(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH GAI; RGA; RGL1; RGL2 AND RGL3.
RX PubMed=16709201; DOI=10.1111/j.1365-313x.2006.02748.x;
RA Nakajima M., Shimada A., Takashi Y., Kim Y.C., Park S.H.,
RA Ueguchi-Tanaka M., Suzuki H., Katoh E., Iuchi S., Kobayashi M., Maeda T.,
RA Matsuoka M., Yamaguchi I.;
RT "Identification and characterization of Arabidopsis gibberellin
RT receptors.";
RL Plant J. 46:880-889(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17521411; DOI=10.1111/j.1365-313x.2007.03098.x;
RA Iuchi S., Suzuki H., Kim Y.C., Iuchi A., Kuromori T., Ueguchi-Tanaka M.,
RA Asami T., Yamaguchi I., Matsuoka M., Kobayashi M., Nakajima M.;
RT "Multiple loss-of-function of Arabidopsis gibberellin receptor AtGID1s
RT completely shuts down a gibberellin signal.";
RL Plant J. 50:958-966(2007).
RN [8]
RP INTERACTION WITH RGL2.
RX PubMed=19500306; DOI=10.1111/j.1365-313x.2009.03936.x;
RA Suzuki H., Park S.-H., Okubo K., Kitamura J., Ueguchi-Tanaka M., Iuchi S.,
RA Katoh E., Kobayashi M., Yamaguchi I., Matsuoka M., Asami T., Nakajima M.;
RT "Differential expression and affinities of Arabidopsis gibberellin
RT receptors can explain variation in phenotypes of multiple knock-out
RT mutants.";
RL Plant J. 60:48-55(2009).
RN [9] {ECO:0007744|PDB:2ZSH, ECO:0007744|PDB:2ZSI}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-344 IN COMPLEXES WITH
RP GIBBERELLIN A3 AND GIBBERELLIN A4.
RX PubMed=19037309; DOI=10.1038/nature07519;
RA Murase K., Hirano Y., Sun T.P., Hakoshima T.;
RT "Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.";
RL Nature 456:459-463(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 gibberellin GA4, but
CC has no affinity for the biologically inactive GAs. In response to GA,
CC interacts with specific DELLA proteins, known as repressors of GA-
CC induced growth, and targets them for degradation via proteasome. Seems
CC to be required for GA signaling that controls root growth, seed
CC germination, stem elongation and flower development. Partially
CC redundant with GID1B and GID1C. {ECO:0000269|PubMed:16709201,
CC ECO:0000269|PubMed:17194763, ECO:0000269|PubMed:17521411}.
CC -!- SUBUNIT: Interacts (via N-terminus) with the DELLA proteins GAI, RGA,
CC RGL1, RGL2 and RGL3 (via N-terminus) in a GA-dependent manner.
CC {ECO:0000269|PubMed:16709201, ECO:0000269|PubMed:17194763,
CC ECO:0000269|PubMed:19037309, ECO:0000269|PubMed:19500306}.
CC -!- INTERACTION:
CC Q9MAA7; Q9SV55: AFPH2; NbExp=3; IntAct=EBI-963597, EBI-1787005;
CC Q9MAA7; Q9LQT8: GAI; NbExp=14; IntAct=EBI-963597, EBI-963606;
CC Q9MAA7; Q9STX3: GID2; NbExp=3; IntAct=EBI-963597, EBI-619033;
CC Q9MAA7; O04294: IMPA3; NbExp=3; IntAct=EBI-963597, EBI-1644689;
CC Q9MAA7; Q9SG92: MES17; NbExp=3; IntAct=EBI-963597, EBI-25529686;
CC Q9MAA7; Q9SLH3: RGA; NbExp=13; IntAct=EBI-963597, EBI-963624;
CC Q9MAA7; Q9C8Y3: RGL1; NbExp=7; IntAct=EBI-963597, EBI-963647;
CC Q9MAA7; Q8GXW1: RGL2; NbExp=8; IntAct=EBI-963597, EBI-963665;
CC Q9MAA7; Q9LF53: RGL3; NbExp=5; IntAct=EBI-963597, EBI-15681313;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:14738307}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. {ECO:0000269|PubMed:17194763, ECO:0000269|PubMed:17521411}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC009177; AAF27018.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74188.1; -; Genomic_DNA.
DR EMBL; AY136305; AAM96971.1; -; mRNA.
DR EMBL; BT002605; AAO00965.1; -; mRNA.
DR RefSeq; NP_187163.1; NM_111384.4.
DR PDB; 2ZSH; X-ray; 1.80 A; A=1-344.
DR PDB; 2ZSI; X-ray; 1.80 A; A=1-344.
DR PDBsum; 2ZSH; -.
DR PDBsum; 2ZSI; -.
DR AlphaFoldDB; Q9MAA7; -.
DR SMR; Q9MAA7; -.
DR BioGRID; 5009; 11.
DR DIP; DIP-37659N; -.
DR IntAct; Q9MAA7; 12.
DR STRING; 3702.AT3G05120.1; -.
DR ESTHER; arath-gid1; Plant_carboxylesterase.
DR MEROPS; S09.A10; -.
DR PaxDb; Q9MAA7; -.
DR PRIDE; Q9MAA7; -.
DR ProteomicsDB; 222347; -.
DR EnsemblPlants; AT3G05120.1; AT3G05120.1; AT3G05120.
DR GeneID; 819674; -.
DR Gramene; AT3G05120.1; AT3G05120.1; AT3G05120.
DR KEGG; ath:AT3G05120; -.
DR Araport; AT3G05120; -.
DR TAIR; locus:2096314; AT3G05120.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_1_1; -.
DR InParanoid; Q9MAA7; -.
DR OMA; ARCQLYR; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9MAA7; -.
DR BioCyc; ARA:AT3G05120-MON; -.
DR EvolutionaryTrace; Q9MAA7; -.
DR PRO; PR:Q9MAA7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MAA7; baseline and differential.
DR Genevisible; Q9MAA7; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0010331; F:gibberellin binding; IDA:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0048444; P:floral organ morphogenesis; IGI:TAIR.
DR GO; GO:0048530; P:fruit morphogenesis; IMP:CAFA.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IGI:TAIR.
DR GO; GO:1905516; P:positive regulation of fertilization; IGI:CAFA.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0010325; P:raffinose family oligosaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IMP:CAFA.
DR DisProt; DP00723; -.
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; Acetylation; Gibberellin signaling pathway; Hydrolase;
KW Nucleus; Receptor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LT10"
FT CHAIN 2..345
FT /note="Gibberellin receptor GID1A"
FT /id="PRO_0000071558"
FT MOTIF 113..115
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 191
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7,
FT ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 289
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7,
FT ECO:0000255|PROSITE-ProRule:PRU10038"
FT BINDING 115..116
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSI"
FT BINDING 116
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSH"
FT BINDING 127
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSH"
FT BINDING 127
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSI"
FT BINDING 191
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSH"
FT BINDING 191
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSI"
FT BINDING 238
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSH"
FT BINDING 320
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSH"
FT BINDING 320
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000269|PubMed:19037309,
FT ECO:0007744|PDB:2ZSI"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LT10"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:2ZSH"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:2ZSH"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2ZSH"
FT HELIX 328..342
FT /evidence="ECO:0007829|PDB:2ZSH"
SQ SEQUENCE 345 AA; 38618 MW; FE1ED6E13BC1A48D CRC64;
MAASDEVNLI ESRTVVPLNT WVLISNFKVA YNILRRPDGT FNRHLAEYLD RKVTANANPV
DGVFSFDVLI DRRINLLSRV YRPAYADQEQ PPSILDLEKP VDGDIVPVIL FFHGGSFAHS
SANSAIYDTL CRRLVGLCKC VVVSVNYRRA PENPYPCAYD DGWIALNWVN SRSWLKSKKD
SKVHIFLAGD SSGGNIAHNV ALRAGESGID VLGNILLNPM FGGNERTESE KSLDGKYFVT
VRDRDWYWKA FLPEGEDREH PACNPFSPRG KSLEGVSFPK SLVVVAGLDL IRDWQLAYAE
GLKKAGQEVK LMHLEKATVG FYLLPNNNHF HNVMDEISAF VNAEC
