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Protein

Gibberellin receptor GID1A

Gene

GID1A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Functions as soluble gibberellin (GA) receptor. GA is an essential hormone that regulates growth and development in plants. Binds with high affinity the biologically active gibberellin GA4, but has no affinity for the biologically inactive GAs. In response to GA, interacts with specific DELLA proteins, known as repressors of GA-induced growth, and targets them for degradation via proteasome. Seems to be required for GA signaling that controls root growth, seed germination, stem elongation and flower development. Partially redundant with GID1B and GID1C.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei127Gibberellin1 Publication1
Active sitei191PROSITE-ProRule annotationBy similarity1
Binding sitei191Gibberellin1 Publication1
Binding sitei238Gibberellin; via carbonyl oxygen1 Publication1
Active sitei289PROSITE-ProRule annotationBy similarity1
Binding sitei320Gibberellin; via amide nitrogen1 Publication1

GO - Molecular functioni

  • gibberellin binding Source: UniProtKB
  • hydrolase activity Source: GO_Central

GO - Biological processi

  • catabolic process Source: GO_Central
  • floral organ morphogenesis Source: TAIR
  • fruit morphogenesis Source: CAFA
  • gibberellin mediated signaling pathway Source: TAIR
  • positive regulation of fertilization Source: CAFA
  • positive regulation of gibberellic acid mediated signaling pathway Source: TAIR
  • response to gibberellin Source: CAFA

Keywordsi

Molecular functionHydrolase, Receptor
Biological processGibberellin signaling pathway

Enzyme and pathway databases

BioCyciARA:AT3G05120-MONOMER

Protein family/group databases

ESTHERiarath-gid1 Plant_carboxylesterase
MEROPSiS09.A10

Names & Taxonomyi

Protein namesi
Recommended name:
Gibberellin receptor GID1A (EC:3.-.-.-)
Alternative name(s):
AtCXE10
Carboxylesterase 10
GID1-like protein 1
Protein GA INSENSITIVE DWARF 1A
Short name:
AtGID1A
Gene namesi
Name:GID1A
Synonyms:CXE10, GID1L1
Ordered Locus Names:At3g05120
ORF Names:T12H1.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G05120
TAIRilocus:2096314 AT3G05120

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth condition.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000715582 – 345Gibberellin receptor GID1AAdd BLAST344

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9MAA7

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

ExpressionAtlasiQ9MAA7 baseline and differential
GenevisibleiQ9MAA7 AT

Interactioni

Subunit structurei

Interacts (via N-terminus) with the DELLA proteins GAI, RGA, RGL1, RGL2 and RGL3 (via N-terminus) in a GA-dependent manner.4 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi5009, 6 interactors
DIPiDIP-37659N
IntActiQ9MAA7, 6 interactors
STRINGi3702.AT3G05120.1

Structurei

Secondary structure

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 13Combined sources4
Helixi18 – 34Combined sources17
Helixi43 – 49Combined sources7
Beta strandi63 – 71Combined sources9
Turni72 – 75Combined sources4
Beta strandi76 – 83Combined sources8
Beta strandi103 – 105Combined sources3
Beta strandi107 – 112Combined sources6
Turni116 – 118Combined sources3
Helixi125 – 138Combined sources14
Beta strandi140 – 145Combined sources6
Turni150 – 152Combined sources3
Helixi157 – 170Combined sources14
Helixi173 – 175Combined sources3
Turni178 – 180Combined sources3
Beta strandi184 – 190Combined sources7
Helixi193 – 205Combined sources13
Turni206 – 208Combined sources3
Beta strandi213 – 218Combined sources6
Helixi228 – 233Combined sources6
Turni234 – 236Combined sources3
Helixi241 – 251Combined sources11
Turni261 – 263Combined sources3
Beta strandi280 – 286Combined sources7
Helixi292 – 304Combined sources13
Beta strandi309 – 314Combined sources6
Turni319 – 322Combined sources4
Beta strandi323 – 325Combined sources3
Helixi328 – 342Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZSHX-ray1.80A1-344[»]
2ZSIX-ray1.80A1-344[»]
DisProtiDP00723
ProteinModelPortaliQ9MAA7
SMRiQ9MAA7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9MAA7

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 116Gibberellin binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi113 – 115Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity3

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Phylogenomic databases

eggNOGiKOG1515 Eukaryota
COG0657 LUCA
HOGENOMiHOG000152323
InParanoidiQ9MAA7
KOiK14493
OMAiNDGWDAF
OrthoDBiEOG09360EOQ
PhylomeDBiQ9MAA7

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR013094 AB_hydrolase_3
IPR002168 Lipase_GDXG_HIS_AS
IPR033140 Lipase_GDXG_put_SER_AS
PfamiView protein in Pfam
PF07859 Abhydrolase_3, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS01173 LIPASE_GDXG_HIS, 1 hit
PS01174 LIPASE_GDXG_SER, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MAA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASDEVNLI ESRTVVPLNT WVLISNFKVA YNILRRPDGT FNRHLAEYLD
60 70 80 90 100
RKVTANANPV DGVFSFDVLI DRRINLLSRV YRPAYADQEQ PPSILDLEKP
110 120 130 140 150
VDGDIVPVIL FFHGGSFAHS SANSAIYDTL CRRLVGLCKC VVVSVNYRRA
160 170 180 190 200
PENPYPCAYD DGWIALNWVN SRSWLKSKKD SKVHIFLAGD SSGGNIAHNV
210 220 230 240 250
ALRAGESGID VLGNILLNPM FGGNERTESE KSLDGKYFVT VRDRDWYWKA
260 270 280 290 300
FLPEGEDREH PACNPFSPRG KSLEGVSFPK SLVVVAGLDL IRDWQLAYAE
310 320 330 340
GLKKAGQEVK LMHLEKATVG FYLLPNNNHF HNVMDEISAF VNAEC
Length:345
Mass (Da):38,618
Last modified:October 1, 2000 - v1
Checksum:iFE1ED6E13BC1A48D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009177 Genomic DNA Translation: AAF27018.1
CP002686 Genomic DNA Translation: AEE74188.1
AY136305 mRNA Translation: AAM96971.1
BT002605 mRNA Translation: AAO00965.1
RefSeqiNP_187163.1, NM_111384.4
UniGeneiAt.18371
At.74127

Genome annotation databases

EnsemblPlantsiAT3G05120.1; AT3G05120.1; AT3G05120
GeneIDi819674
GrameneiAT3G05120.1; AT3G05120.1; AT3G05120
KEGGiath:AT3G05120

Similar proteinsi

Entry informationi

Entry nameiGID1A_ARATH
AccessioniPrimary (citable) accession number: Q9MAA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: October 1, 2000
Last modified: April 25, 2018
This is version 117 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health