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Protein

Phosphoglucan phosphatase DSP4, chloroplastic

Gene

DSP4

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

Functioni

Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Acts as major regulator of the initial steps of starch degradation at the granule surface. Functions during the day by dephosphorylating the night-accumulated phospho-oligosaccharides. Can release phosphate from both the C6 and the C3 positions.9 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei198Phosphocysteine intermediate1

GO - Molecular functioni

  • carbohydrate phosphatase activity Source: TAIR
  • polysaccharide binding Source: TAIR
  • protein tyrosine/serine/threonine phosphatase activity Source: InterPro

GO - Biological processi

  • circadian rhythm Source: InterPro
  • starch catabolic process Source: TAIR
  • starch metabolic process Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciARA:AT3G52180-MONOMER.
MetaCyc:AT3G52180-MONOMER.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucan phosphatase DSP4, chloroplastic (EC:3.1.3.-)
Alternative name(s):
AtPTPKIS1
Dual specificity protein phosphatase 4
Protein STARCH-EXCESS 4
Short name:
AtSEX4
Gene namesi
Name:DSP4
Synonyms:PTPKIS1, SEX4
Ordered Locus Names:At3g52180
ORF Names:F4F15.290
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G52180.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

Reduced plant size, slightly delayed flowering, leaves with large round starch granules and starch in excess.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi167F → M: Increases glucan phosphatase activity. 1 Publication1
Mutagenesisi167F → S: No effect on glucan phosphatase activity. 1 Publication1
Mutagenesisi167F → Y: Reduces glucan phosphatase activity 3-fold. 1 Publication1
Mutagenesisi198C → S: Loss of glucan phosphatase activity and starch-binding capacity. 4 Publications1
Mutagenesisi278W → G: Reduces starch binding efficiency. 1 Publication1
Mutagenesisi307K → A: Reduces starch binding efficiency. 1 Publication1
Mutagenesisi329G → R: Loss starch-binding capacity. 1 Publication1
Mutagenesisi333N → K: Loss of glucan phosphatase activity and starch-binding capacity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 54ChloroplastSequence analysisAdd BLAST54
ChainiPRO_000041733355 – 379Phosphoglucan phosphatase DSP4, chloroplasticAdd BLAST325

Proteomic databases

PaxDbiQ9FEB5.
PRIDEiQ9FEB5.

Expressioni

Inductioni

Expressed with a circadian rhythm showing a peak at the end of the day and then decreasing to reach the lowest levels at the end of the night.1 Publication

Gene expression databases

ExpressionAtlasiQ9FEB5. baseline and differential.
GenevisibleiQ9FEB5. AT.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KIN11P929582EBI-307215,EBI-307202

Protein-protein interaction databases

BioGridi9701. 1 interactor.
IntActiQ9FEB5. 1 interactor.
STRINGi3702.AT3G52180.1.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi92 – 94Combined sources3
Beta strandi98 – 102Combined sources5
Beta strandi105 – 108Combined sources4
Helixi115 – 122Combined sources8
Beta strandi125 – 130Combined sources6
Helixi134 – 140Combined sources7
Helixi144 – 152Combined sources9
Beta strandi158 – 161Combined sources4
Helixi169 – 190Combined sources22
Beta strandi192 – 197Combined sources6
Beta strandi199 – 203Combined sources5
Helixi204 – 215Combined sources12
Helixi221 – 231Combined sources11
Helixi238 – 250Combined sources13
Beta strandi254 – 262Combined sources9
Beta strandi269 – 273Combined sources5
Turni274 – 276Combined sources3
Beta strandi277 – 283Combined sources7
Turni288 – 290Combined sources3
Beta strandi292 – 310Combined sources19
Beta strandi313 – 315Combined sources3
Beta strandi332 – 337Combined sources6
Helixi344 – 352Combined sources9
Beta strandi354 – 356Combined sources3
Helixi361 – 373Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NMEX-ray2.40A/B90-379[»]
4PYHX-ray1.65A90-379[»]
ProteinModelPortaliQ9FEB5.
SMRiQ9FEB5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini112 – 259Tyrosine-protein phosphataseAdd BLAST148

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 204Substrate binding6
Regioni259 – 335Polysaccharide bindingAdd BLAST77

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 31Poly-Ser6

Domaini

Contains a C-terminal polysaccharide-binding domain which interacts with the phosphatase domain; this interaction is required for glucan phosphatase activity.

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
KOG1716. Eukaryota.
COG2453. LUCA.
HOGENOMiHOG000005968.
InParanoidiQ9FEB5.
OMAiCEIRDFD.
OrthoDBiEOG09360L0Y.
PhylomeDBiQ9FEB5.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR032640. AMPK1_CBM.
IPR030079. DSP4.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR014756. Ig_E-set.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10343:SF58. PTHR10343:SF58. 1 hit.
PfamiPF16561. AMPK1_CBM. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9FEB5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNCLQNLPRC SVSPLLGFGC IQRDHSSSSS SLKMLISPPI KANDPKSRLV
60 70 80 90 100
LHAVSESKSS SEMSGVAKDE EKSDEYSQDM TQAMGAVLTY RHELGMNYNF
110 120 130 140 150
IRPDLIVGSC LQTPEDVDKL RKIGVKTIFC LQQDPDLEYF GVDISSIQAY
160 170 180 190 200
AKKYSDIQHI RCEIRDFDAF DLRMRLPAVV GTLYKAVKRN GGVTYVHCTA
210 220 230 240 250
GMGRAPAVAL TYMFWVQGYK LMEAHKLLMS KRSCFPKLDA IRNATIDILT
260 270 280 290 300
GLKRKTVTLT LKDKGFSRVE ISGLDIGWGQ RIPLTLDKGT GFWILKRELP
310 320 330 340 350
EGQFEYKYII DGEWTHNEAE PFIGPNKDGH TNNYAKVVDD PTSVDGTTRE
360 370
RLSSEDPELL EEERSKLIQF LETCSEAEV
Length:379
Mass (Da):42,626
Last modified:March 1, 2001 - v1
Checksum:i4AA36B6E3E62A42B
GO

Sequence cautioni

The sequence CAB41338 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAC18327 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64S → R in AAL27495 (PubMed:14593172).Curated1
Sequence conflicti64S → R in AAN28817 (PubMed:14593172).Curated1
Sequence conflicti84M → K in AAM61237 (Ref. 5) Curated1
Sequence conflicti287D → G in AAL27495 (PubMed:14593172).Curated1
Sequence conflicti287D → G in AAN28817 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ302781 mRNA. Translation: CAC17593.1.
AJ302779 Genomic DNA. Translation: CAC18327.1. Sequence problems.
AJ302779 Genomic DNA. Translation: CAC18328.1.
AL049711 Genomic DNA. Translation: CAB41338.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE78909.1.
AF439823 mRNA. Translation: AAL27495.1.
AY143878 mRNA. Translation: AAN28817.1.
AY084675 mRNA. Translation: AAM61237.1.
PIRiT49097.
RefSeqiNP_566960.1. NM_115078.4. [Q9FEB5-1]
UniGeneiAt.24067.

Genome annotation databases

EnsemblPlantsiAT3G52180.1; AT3G52180.1; AT3G52180. [Q9FEB5-1]
GeneIDi824383.
GrameneiAT3G52180.1; AT3G52180.1; AT3G52180.
KEGGiath:AT3G52180.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ302781 mRNA. Translation: CAC17593.1.
AJ302779 Genomic DNA. Translation: CAC18327.1. Sequence problems.
AJ302779 Genomic DNA. Translation: CAC18328.1.
AL049711 Genomic DNA. Translation: CAB41338.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE78909.1.
AF439823 mRNA. Translation: AAL27495.1.
AY143878 mRNA. Translation: AAN28817.1.
AY084675 mRNA. Translation: AAM61237.1.
PIRiT49097.
RefSeqiNP_566960.1. NM_115078.4. [Q9FEB5-1]
UniGeneiAt.24067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NMEX-ray2.40A/B90-379[»]
4PYHX-ray1.65A90-379[»]
ProteinModelPortaliQ9FEB5.
SMRiQ9FEB5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9701. 1 interactor.
IntActiQ9FEB5. 1 interactor.
STRINGi3702.AT3G52180.1.

Protein family/group databases

CAZyiCBM48. Carbohydrate-Binding Module Family 48.

Proteomic databases

PaxDbiQ9FEB5.
PRIDEiQ9FEB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G52180.1; AT3G52180.1; AT3G52180. [Q9FEB5-1]
GeneIDi824383.
GrameneiAT3G52180.1; AT3G52180.1; AT3G52180.
KEGGiath:AT3G52180.

Organism-specific databases

TAIRiAT3G52180.

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
KOG1716. Eukaryota.
COG2453. LUCA.
HOGENOMiHOG000005968.
InParanoidiQ9FEB5.
OMAiCEIRDFD.
OrthoDBiEOG09360L0Y.
PhylomeDBiQ9FEB5.

Enzyme and pathway databases

BioCyciARA:AT3G52180-MONOMER.
MetaCyc:AT3G52180-MONOMER.

Miscellaneous databases

PROiQ9FEB5.

Gene expression databases

ExpressionAtlasiQ9FEB5. baseline and differential.
GenevisibleiQ9FEB5. AT.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR032640. AMPK1_CBM.
IPR030079. DSP4.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR014756. Ig_E-set.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. TYR_PHOSPHATASE_dom.
IPR020422. TYR_PHOSPHATASE_DUAL_dom.
[Graphical view]
PANTHERiPTHR10343:SF58. PTHR10343:SF58. 1 hit.
PfamiPF16561. AMPK1_CBM. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDSP4_ARATH
AccessioniPrimary (citable) accession number: Q9FEB5
Secondary accession number(s): Q8LFS3
, Q944A8, Q9FDY9, Q9SUY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: March 1, 2001
Last modified: November 30, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Starch binding efficiency is dependent on pH and redox conditions.1 Publication

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.