GID1C_ARATH
ID GID1C_ARATH Reviewed; 344 AA.
AC Q940G6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Gibberellin receptor GID1C;
DE EC=3.-.-.-;
DE AltName: Full=AtCXE19;
DE AltName: Full=Carboxylesterase 19;
DE AltName: Full=GID1-like protein 3;
DE AltName: Full=Protein GA INSENSITIVE DWARF 1C;
DE Short=AtGID1C;
GN Name=GID1C; Synonyms=CXE19, GID1L3; OrderedLocusNames=At5g27320;
GN ORFNames=F21A20.30;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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).
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 stem elongation. Partially redundant with GID1A and
CC GID1B. {ECO:0000269|PubMed:16709201, ECO:0000269|PubMed:17194763,
CC 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 Q940G6; Q9LQT8: GAI; NbExp=8; IntAct=EBI-963794, EBI-963606;
CC Q940G6; Q9SYP2: PFP-ALPHA1; NbExp=3; IntAct=EBI-963794, EBI-1238145;
CC Q940G6; Q9SLH3: RGA; NbExp=11; IntAct=EBI-963794, EBI-963624;
CC Q940G6; Q9C8Y3: RGL1; NbExp=6; IntAct=EBI-963794, EBI-963647;
CC Q940G6; Q8GXW1: RGL2; NbExp=6; IntAct=EBI-963794, EBI-963665;
CC Q940G6; Q9LF53: RGL3; NbExp=4; IntAct=EBI-963794, EBI-15681313;
CC Q940G6; O64722: ZHD3; NbExp=3; IntAct=EBI-963794, EBI-1806244;
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; AC007123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93672.1; -; Genomic_DNA.
DR EMBL; AY054653; AAK96844.1; -; mRNA.
DR EMBL; AY128729; AAM91129.1; -; mRNA.
DR RefSeq; NP_198084.1; NM_122614.4.
DR AlphaFoldDB; Q940G6; -.
DR SMR; Q940G6; -.
DR BioGRID; 18064; 8.
DR DIP; DIP-37663N; -.
DR IntAct; Q940G6; 8.
DR STRING; 3702.AT5G27320.1; -.
DR ESTHER; arath-AT5G27320; Plant_carboxylesterase.
DR MEROPS; S09.A10; -.
DR PaxDb; Q940G6; -.
DR PRIDE; Q940G6; -.
DR ProteomicsDB; 222348; -.
DR EnsemblPlants; AT5G27320.1; AT5G27320.1; AT5G27320.
DR GeneID; 832790; -.
DR Gramene; AT5G27320.1; AT5G27320.1; AT5G27320.
DR KEGG; ath:AT5G27320; -.
DR Araport; AT5G27320; -.
DR TAIR; locus:2146425; AT5G27320.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_1_1; -.
DR InParanoid; Q940G6; -.
DR OMA; RAPENRF; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q940G6; -.
DR BioCyc; ARA:AT5G27320-MON; -.
DR PRO; PR:Q940G6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q940G6; baseline and differential.
DR Genevisible; Q940G6; 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: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:CAFA.
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..344
FT /note="Gibberellin receptor GID1C"
FT /id="PRO_0000071560"
FT MOTIF 111..113
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 189
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7,
FT ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 287
FT /evidence="ECO:0000250|UniProtKB:Q0ZPV7,
FT ECO:0000255|PROSITE-ProRule:PRU10038"
FT BINDING 113..114
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 114
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 125
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 125
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 189
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 189
FT /ligand="gibberellin A4"
FT /ligand_id="ChEBI:CHEBI:73251"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 236
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 318
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000250|UniProtKB:Q9MAA7"
FT BINDING 318
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 344 AA; 38426 MW; 40B4C048B1FB6C15 CRC64;
MAGSEEVNLI ESKTVVPLNT WVLISNFKLA YNLLRRPDGT FNRHLAEFLD RKVPANANPV
NGVFSFDVII DRQTNLLSRV YRPADAGTSP SITDLQNPVD GEIVPVIVFF HGGSFAHSSA
NSAIYDTLCR RLVGLCGAVV VSVNYRRAPE NRYPCAYDDG WAVLKWVNSS SWLRSKKDSK
VRIFLAGDSS GGNIVHNVAV RAVESRIDVL GNILLNPMFG GTERTESEKR LDGKYFVTVR
DRDWYWRAFL PEGEDREHPA CSPFGPRSKS LEGLSFPKSL VVVAGLDLIQ DWQLKYAEGL
KKAGQEVKLL YLEQATIGFY LLPNNNHFHT VMDEIAAFVN AECQ
