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Protein

Strigolactone esterase D14

Gene

D14

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

Functioni

Involved in strigolactone signaling pathway (PubMed:22357928). Does not move long distances acropetally in the plant to regulate shoot branching and is rapidly degraded in the presence of strigolactones (PubMed:24610723). Functions downstream of strigolactone synthesis, as a component of hormone signaling and as an enzyme that participates in the conversion of strigolactones to the bioactive form (PubMed:22357928). Acts probably as a strigolactone receptor (PubMed:24610723). Strigolactones are hormones that inhibit tillering and shoot branching through the MAX-dependent pathway, contribute to the regulation of shoot architectural response to phosphate-limiting conditions and function as rhizosphere signal that stimulates hyphal branching of arbuscular mycorrhizal fungi and trigger seed germination of root parasitic weeds (PubMed:22357928). Hydrolyzes methyl carlactonoate (MeCLA), but not carlactone (CL) or carlactonoic acid (CLA) (PubMed:25425668). Hydrolyzes the butenolide ring of strigolactones (PubMed:23381136). The initial nucleophilic attack causes an electron shift, followed by the addition of a water molecule, to lead to the release of the ABC ring product and the formation of a 'Ser-97'-stabilized open lactone intermediate (PubMed:23381136). Has no esterase activity for 4-nitrophenyl butyrate (PubMed:23381136). Binds and hydrolyzes the synthetic strigolactone analog GR24 in vitro. Forms a stable covalent complex with the D-ring of strigolactone, which is essential for hormone bioactivity. The D-ring is attached to His-247 of the catalytic triad. The hydrolysis of strigolactone into a covalently linked intermediate molecule initiates a conformational change of D14 to facilitate interaction with MAX2 and formation of the D14-MAX2-SKP1/ASK1 complex to trigger strigolactone signaling. This mechanism defines D14 as a non-canonical hormone receptor with dual functions to generate and sense the active form of strigolactone (PubMed:27479325).5 Publications

Miscellaneous

The initial nucleophilic attack of strigolactones by D14 causes an electron shift, followed by the addition of a water molecule, to lead to the release of the ABC ring product and the formation of a S97-stabilized open lactone intermediate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei97Nucleophile2 Publications1
Active sitei2181 Publication1
Active sitei2471 Publication1

GO - Molecular functioni

GO - Biological processi

  • cellular response to strigolactone Source: TAIR
  • secondary shoot formation Source: UniProtKB
  • strigolactone biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase

Protein family/group databases

ESTHERiarath-AtD14 RsbQ-like
MEROPSiS33.A18

Names & Taxonomyi

Protein namesi
Recommended name:
Strigolactone esterase D141 Publication (EC:3.1.-.-1 Publication)
Alternative name(s):
Protein DWARF 141 Publication
Short name:
AtD141 Publication
Gene namesi
Name:D141 Publication
Ordered Locus Names:At3g03990Imported
ORF Names:T11I18.10Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

AraportiAT3G03990
TAIRilocus:2095913 AT3G03990

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

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Increased shoot branching.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97S → A: Loss of activity. 1 Publication1
Mutagenesisi158G → E: Loss of interaction with MAX2. 1 Publication1
Mutagenesisi169P → L in d14-seto; loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004220531 – 267Strigolactone esterase D14Add BLAST267

Proteomic databases

PaxDbiQ9SQR3
PRIDEiQ9SQR3

Expressioni

Tissue specificityi

Expressed at high levels in rosette and cauline leaves and at lower levels in axillary buds, inflorescences, stems, roots and developing vascular tissue of cotyledons.1 Publication

Inductioni

Not regulated by strigolactone, auxin signaling or bud growth status.1 Publication

Gene expression databases

ExpressionAtlasiQ9SQR3 baseline and differential
GenevisibleiQ9SQR3 AT

Interactioni

Subunit structurei

Interacts with SMXL6, SMXL7 and SMXL8 (PubMed:26546446, PubMed:25713176). The interaction with SMXLs occurs in the presence of (2'R) stereoisomers of strigolactones, but not (2'S) stereoisomers (PubMed:25713176). Interacts with MAX2. Forms a complex with MAX2 and SKP1A/ASK1 in presence of strigolactone (PubMed:27479325).3 Publications

Protein-protein interaction databases

BioGridi4889, 1 interactor
STRINGi3702.AT3G03990.1

Structurei

Secondary structure

1267
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Beta strandi14 – 16Combined sources3
Beta strandi19 – 25Combined sources7
Beta strandi28 – 30Combined sources3
Helixi32 – 35Combined sources4
Turni36 – 38Combined sources3
Helixi39 – 41Combined sources3
Turni42 – 44Combined sources3
Beta strandi45 – 51Combined sources7
Beta strandi54 – 56Combined sources3
Helixi61 – 63Combined sources3
Turni66 – 70Combined sources5
Helixi73 – 86Combined sources14
Beta strandi91 – 95Combined sources5
Helixi98 – 109Combined sources12
Helixi111 – 113Combined sources3
Beta strandi114 – 120Combined sources7
Beta strandi134 – 136Combined sources3
Helixi138 – 155Combined sources18
Turni156 – 158Combined sources3
Helixi172 – 177Combined sources6
Helixi178 – 181Combined sources4
Helixi184 – 195Combined sources12
Beta strandi200 – 202Combined sources3
Helixi203 – 205Combined sources3
Beta strandi210 – 214Combined sources5
Beta strandi219 – 221Combined sources3
Helixi226 – 232Combined sources7
Beta strandi237 – 241Combined sources5
Turni249 – 251Combined sources3
Helixi254 – 263Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IH4X-ray3.50A/B/C/D1-267[»]
5HZGX-ray3.30A/E1-267[»]
ProteinModelPortaliQ9SQR3
SMRiQ9SQR3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiENOG410IJKB Eukaryota
COG0596 LUCA
HOGENOMiHOG000251386
InParanoidiQ9SQR3
OMAiLNDNDYH
OrthoDBiEOG09360KGQ
PhylomeDBiQ9SQR3

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
PfamiView protein in Pfam
PF12697 Abhydrolase_6, 1 hit
SUPFAMiSSF53474 SSF53474, 1 hit

Sequencei

Sequence statusi: Complete.

Q9SQR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQHNILEAL NVRVVGTGDR ILFLAHGFGT DQSAWHLILP YFTQNYRVVL
60 70 80 90 100
YDLVCAGSVN PDYFDFNRYT TLDPYVDDLL NIVDSLGIQN CAYVGHSVSA
110 120 130 140 150
MIGIIASIRR PELFSKLILI GFSPRFLNDE DYHGGFEEGE IEKVFSAMEA
160 170 180 190 200
NYEAWVHGFA PLAVGADVPA AVREFSRTLF NMRPDISLFV SRTVFNSDLR
210 220 230 240 250
GVLGLVRVPT CVIQTAKDVS VPASVAEYLR SHLGGDTTVE TLKTEGHLPQ
260
LSAPAQLAQF LRRALPR
Length:267
Mass (Da):29,625
Last modified:May 1, 2000 - v1
Checksum:i47E326EEE2AE5204
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti236D → E in AAM65892 (Ref. 4) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC011698 Genomic DNA Translation: AAF05858.1
CP002686 Genomic DNA Translation: AEE74023.1
AY064145 mRNA Translation: AAL36052.1
AY097402 mRNA Translation: AAM19918.1
AY088353 mRNA Translation: AAM65892.1
RefSeqiNP_566220.1, NM_111270.3
UniGeneiAt.27069

Genome annotation databases

EnsemblPlantsiAT3G03990.1; AT3G03990.1; AT3G03990
GeneIDi819554
GrameneiAT3G03990.1; AT3G03990.1; AT3G03990
KEGGiath:AT3G03990

Similar proteinsi

Entry informationi

Entry nameiD14_ARATH
AccessioniPrimary (citable) accession number: Q9SQR3
Secondary accession number(s): Q8L9M4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: May 1, 2000
Last modified: April 25, 2018
This is version 103 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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