GID1B_ARATH
ID GID1B_ARATH Reviewed; 358 AA.
AC Q9LYC1; Q0WRW2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Gibberellin receptor GID1B;
DE EC=3.-.-.-;
DE AltName: Full=AtCXE14;
DE AltName: Full=Carboxylesterase 14;
DE AltName: Full=GID1-like protein 2;
DE AltName: Full=Protein GA INSENSITIVE DWARF 1B;
DE Short=AtGID1B;
GN Name=GID1B; Synonyms=CXE14, GID1L2; OrderedLocusNames=At3g63010;
GN ORFNames=T20O10.110;
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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).
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 and flower development. May function as a dominant GA
CC receptor at low GA concentrations in germination. Partially redundant
CC with GID1A and GID1C. {ECO:0000269|PubMed:16709201,
CC ECO:0000269|PubMed:17194763, ECO:0000269|PubMed:17521411}.
CC -!- SUBUNIT: Interacts with the DELLA proteins GAI, RGA, RGL1, RGL2 and
CC RGL3 in a GA-dependent manner. {ECO:0000269|PubMed:16709201,
CC ECO:0000269|PubMed:17194763, ECO:0000269|PubMed:19500306}.
CC -!- INTERACTION:
CC Q9LYC1; Q9M872: At3g02700/F16B3_33; NbExp=3; IntAct=EBI-963686, EBI-25529828;
CC Q9LYC1; A0A178V0E5: At4g16447; NbExp=3; IntAct=EBI-963686, EBI-25529855;
CC Q9LYC1; Q9FMT4: At5g14170; NbExp=3; IntAct=EBI-963686, EBI-3387100;
CC Q9LYC1; Q9FVU9: CSN5B; NbExp=3; IntAct=EBI-963686, EBI-697501;
CC Q9LYC1; O64688: E1-BETA-2; NbExp=3; IntAct=EBI-963686, EBI-25520038;
CC Q9LYC1; Q9S7U7: F28J7.1; NbExp=3; IntAct=EBI-963686, EBI-4428777;
CC Q9LYC1; Q9LQT8: GAI; NbExp=8; IntAct=EBI-963686, EBI-963606;
CC Q9LYC1; Q9STX3: GID2; NbExp=3; IntAct=EBI-963686, EBI-619033;
CC Q9LYC1; Q8LF89: GRXC8; NbExp=3; IntAct=EBI-963686, EBI-4434651;
CC Q9LYC1; Q9SG92: MES17; NbExp=3; IntAct=EBI-963686, EBI-25529686;
CC Q9LYC1; Q9C6Z3: PDH-E1 BETA; NbExp=3; IntAct=EBI-963686, EBI-4436231;
CC Q9LYC1; Q9SLH3: RGA; NbExp=13; IntAct=EBI-963686, EBI-963624;
CC Q9LYC1; Q9C8Y3: RGL1; NbExp=6; IntAct=EBI-963686, EBI-963647;
CC Q9LYC1; Q8GXW1: RGL2; NbExp=5; IntAct=EBI-963686, EBI-963665;
CC Q9LYC1; Q9LF53: RGL3; NbExp=4; IntAct=EBI-963686, 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; AL163816; CAB87746.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80423.1; -; Genomic_DNA.
DR EMBL; AK228182; BAF00137.1; -; mRNA.
DR EMBL; BT028997; ABI93906.1; -; mRNA.
DR PIR; T48090; T48090.
DR RefSeq; NP_191860.1; NM_116166.5.
DR AlphaFoldDB; Q9LYC1; -.
DR SMR; Q9LYC1; -.
DR BioGRID; 10790; 16.
DR DIP; DIP-37662N; -.
DR IntAct; Q9LYC1; 17.
DR STRING; 3702.AT3G63010.1; -.
DR ESTHER; arath-GID1B; Plant_carboxylesterase.
DR PaxDb; Q9LYC1; -.
DR PRIDE; Q9LYC1; -.
DR ProteomicsDB; 222261; -.
DR EnsemblPlants; AT3G63010.1; AT3G63010.1; AT3G63010.
DR GeneID; 825476; -.
DR Gramene; AT3G63010.1; AT3G63010.1; AT3G63010.
DR KEGG; ath:AT3G63010; -.
DR Araport; AT3G63010; -.
DR TAIR; locus:2099152; AT3G63010.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_1_1; -.
DR InParanoid; Q9LYC1; -.
DR OMA; HGFDGMR; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9LYC1; -.
DR BioCyc; ARA:AT3G63010-MON; -.
DR PRO; PR:Q9LYC1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LYC1; baseline and differential.
DR Genevisible; Q9LYC1; AT.
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; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0048444; P:floral organ morphogenesis; IGI:TAIR.
DR GO; GO:0048530; P:fruit morphogenesis; IGI:CAFA.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IGI:TAIR.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:CAFA.
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; IGI:TAIR.
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 Acetylation; Gibberellin signaling pathway; Hydrolase; Nucleus; Receptor;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LT10"
FT CHAIN 2..358
FT /note="Gibberellin receptor GID1B"
FT /id="PRO_0000071559"
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:0000250|UniProtKB:Q9MAA7"
FT BINDING 116
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 127
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 127
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 191
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 191
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 238
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 320
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 320
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LT10"
SQ SEQUENCE 358 AA; 40300 MW; 8D24F47BC40CE4D4 CRC64;
MAGGNEVNLN ECKRIVPLNT WVLISNFKLA YKVLRRPDGS FNRDLAEFLD RKVPANSFPL
DGVFSFDHVD STTNLLTRIY QPASLLHQTR HGTLELTKPL STTEIVPVLI FFHGGSFTHS
SANSAIYDTF CRRLVTICGV VVVSVDYRRS PEHRYPCAYD DGWNALNWVK SRVWLQSGKD
SNVYVYLAGD SSGGNIAHNV AVRATNEGVK VLGNILLHPM FGGQERTQSE KTLDGKYFVT
IQDRDWYWRA YLPEGEDRDH PACNPFGPRG QSLKGVNFPK SLVVVAGLDL VQDWQLAYVD
GLKKTGLEVN LLYLKQATIG FYFLPNNDHF HCLMEELNKF VHSIEDSQSK SSPVLLTP
