Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Strigolactone esterase D14

Gene

D14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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). May function downstream of strigolactone synthesis, as a component of hormone signaling or 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).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971Nucleophile2 Publications
Active sitei218 – 21811 Publication
Active sitei247 – 24711 Publication

GO - Molecular functioni

GO - Biological processi

  • cellular response to strigolactone Source: TAIR
  • secondary shoot formation Source: UniProtKB
  • strigolactone biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

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

TAIRiAT3G03990.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Increased shoot branching.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 971S → A: Loss of activity. 1 Publication
Mutagenesisi169 – 1691P → L in d14-seto; loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Strigolactone esterase D14PRO_0000422053Add
BLAST

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

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).2 Publications

Protein-protein interaction databases

BioGridi4889. 1 interaction.
STRINGi3702.AT3G03990.1.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 115Combined sources
Beta strandi14 – 163Combined sources
Beta strandi21 – 255Combined sources
Helixi32 – 387Combined sources
Helixi40 – 434Combined sources
Beta strandi46 – 516Combined sources
Beta strandi54 – 563Combined sources
Helixi61 – 633Combined sources
Turni66 – 683Combined sources
Beta strandi70 – 734Combined sources
Helixi74 – 8512Combined sources
Beta strandi94 – 963Combined sources
Helixi98 – 10912Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi118 – 1214Combined sources
Helixi138 – 15013Combined sources
Helixi152 – 16413Combined sources
Helixi170 – 18112Combined sources
Helixi184 – 19512Combined sources
Helixi202 – 2054Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi219 – 2213Combined sources
Helixi225 – 2317Combined sources
Helixi249 – 2524Combined sources
Helixi254 – 2629Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IH4X-ray3.50A/B/C/D1-267[»]
ProteinModelPortaliQ9SQR3.
SMRiQ9SQR3. Positions 6-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiENOG410IJKB. Eukaryota.
COG0596. LUCA.
HOGENOMiHOG000251386.
InParanoidiQ9SQR3.
OMAiRCAYVGH.
OrthoDBiEOG09360KGQ.
PhylomeDBiQ9SQR3.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR031143. D14_fam.
[Graphical view]
PANTHERiPTHR10992:SF891. PTHR10992:SF891. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361D → E in AAM65892 (Ref. 4) Curated

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_111270.2.
UniGeneiAt.27069.

Genome annotation databases

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

Cross-referencesi

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_111270.2.
UniGeneiAt.27069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IH4X-ray3.50A/B/C/D1-267[»]
ProteinModelPortaliQ9SQR3.
SMRiQ9SQR3. Positions 6-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4889. 1 interaction.
STRINGi3702.AT3G03990.1.

Protein family/group databases

ESTHERiarath-AtD14. RsbQ-like.
MEROPSiS33.A18.

Proteomic databases

PaxDbiQ9SQR3.
PRIDEiQ9SQR3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G03990.

Phylogenomic databases

eggNOGiENOG410IJKB. Eukaryota.
COG0596. LUCA.
HOGENOMiHOG000251386.
InParanoidiQ9SQR3.
OMAiRCAYVGH.
OrthoDBiEOG09360KGQ.
PhylomeDBiQ9SQR3.

Miscellaneous databases

PROiQ9SQR3.

Gene expression databases

GenevisibleiQ9SQR3. AT.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR031143. D14_fam.
[Graphical view]
PANTHERiPTHR10992:SF891. PTHR10992:SF891. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiD14_ARATH
AccessioniPrimary (citable) accession number: Q9SQR3
Secondary accession number(s): Q8L9M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.