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   24-JAN-2024, entry version 133.
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 a 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; 9.
DR   DIP; DIP-37663N; -.
DR   IntAct; Q940G6; 8.
DR   STRING; 3702.Q940G6; -.
DR   ESTHER; arath-AT5G27320; Plant_carboxylesterase.
DR   MEROPS; S09.A10; -.
DR   PaxDb; 3702-AT5G27320-1; -.
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; AT5G27320; GID1C.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_012494_22_1_1; -.
DR   InParanoid; Q940G6; -.
DR   OMA; MANEIAT; -.
DR   OrthoDB; 5397115at2759; -.
DR   PhylomeDB; Q940G6; -.
DR   BioCyc; ARA:AT5G27320-MONOMER; -.
DR   PRO; PR:Q940G6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q940G6; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009739; P:response to gibberellin; IGI:CAFA.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   PANTHER; PTHR23024; ARYLACETAMIDE DEACETYLASE; 1.
DR   PANTHER; PTHR23024:SF492; GIBBERELLIN RECEPTOR GID1C; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR   PROSITE; PS01174; LIPASE_GDXG_SER; 1.
DR   Genevisible; Q940G6; AT.
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
//