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Protein

Probable strigolactone esterase D14 homolog

Gene

D14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in strigolactone signaling pathway. 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. 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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971NucleophileBy similarity
Active sitei218 – 2181By similarity
Active sitei247 – 2471By similarity

GO - Molecular functioni

  1. hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. secondary shoot formation Source: UniProtKB
  2. strigolactone biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Protein family/group databases

MEROPSiS33.A18.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable strigolactone esterase D14 homolog
Alternative name(s):
Protein DWARF-14
Short name:
AtD14
Gene namesi
Name:D14
Ordered Locus Names:At3g03990
ORF Names:T11I18.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G03990.

Pathology & Biotechi

Disruption phenotypei

Increased shoot branching.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267Probable strigolactone esterase D14 homologPRO_0000422053Add
BLAST

Proteomic databases

PRIDEiQ9SQR3.

Expressioni

Gene expression databases

GenevestigatoriQ9SQR3.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G03990.1-P.

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

InParanoidiQ9SQR3.
OMAiCAYVGHS.
PhylomeDBiQ9SQR3.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[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.
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

STRINGi3702.AT3G03990.1-P.

Protein family/group databases

MEROPSiS33.A18.

Proteomic databases

PRIDEiQ9SQR3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G03990.

Phylogenomic databases

InParanoidiQ9SQR3.
OMAiCAYVGHS.
PhylomeDBiQ9SQR3.

Gene expression databases

GenevestigatoriQ9SQR3.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Specialisation within the DWARF14 protein family confers distinct responses to karrikins and strigolactones in Arabidopsis."
    Waters M.T., Nelson D.C., Scaffidi A., Flematti G.R., Sun Y.K., Dixon K.W., Smith S.M.
    Development 139:1285-1295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.

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: January 7, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

External Data

Dasty 3

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 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.