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Protein

Phosphoglucan phosphatase DSP4, chloroplastic

Gene

DSP4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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, but dephosphorylates preferentially the C6 position (PubMed:20018599, PubMed:26231210).11 Publications

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei90Substrate; via amide nitrogenCombined sources1
Binding sitei166SubstrateCombined sources1
Active sitei198Phosphocysteine intermediate6 Publications1
Binding sitei307SubstrateCombined sources1
Binding sitei332SubstrateCombined sources1

GO - Molecular functioni

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

GO - Biological processi

  • circadian rhythm Source: InterPro
  • starch catabolic process Source: UniProtKB
  • starch metabolic process Source: CACAO

Keywordsi

Molecular functionHydrolase
Biological processCarbohydrate 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.-6 Publications)
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

AraportiAT3G52180
TAIRilocus:2083845 AT3G52180

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

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
Mutagenesisi90Y → A: Reduces starch binding and glucan phosphatase activity. 1 Publication1
Mutagenesisi139Y → A: Mildly reduces starch binding and glucan phosphatase activity. 1 Publication1
Mutagenesisi140F → A: Reduces glucan phosphatase activity. 1 Publication1
Mutagenesisi140F → W: Changes substrate specificity and enhances glucan dephosphorylation at C3. Leads to preferential glucan dephosphorylation at C6; when associated with G-235. 1 Publication1
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. 6 Publications1
Mutagenesisi200 – 203AGMG → TGFD: Loss of glucan phosphatase activity. 1 Publication4
Mutagenesisi203G → D: Nearly abolishes glucan phosphatase activity. 1 Publication1
Mutagenesisi235F → A: Slightly reduces starch binding and glucan phosphatase activity. 1 Publication1
Mutagenesisi235F → G: Changes substrate specificity and enhances glucan dephosphorylation at C3. Leads to preferential glucan dephosphorylation at C6; when associated with W-140. 1 Publication1
Mutagenesisi237K → A: Slightly reduces glucan phosphatase activity. 1 Publication1
Mutagenesisi278W → A: Nearly abolishes glucan phosphatase activity. Strongly reduces starch binding efficiency. 1 Publication1
Mutagenesisi278W → G: Reduces starch binding efficiency. 1 Publication1
Mutagenesisi307K → A: Strongly reduces glucan phosphatase activity. Strongly reduces starch binding efficiency. 2 Publications1
Mutagenesisi314W → A: Nearly abolishes glucan phosphatase activity. 1 Publication1
Mutagenesisi329G → R: Loss starch-binding capacity. 1 Publication1
Mutagenesisi330H → A: Decreases glucan phosphatase activity. 1 Publication1
Mutagenesisi332N → A: Nearly abolishes glucan phosphatase activity. Loss of starch binding. 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 bindingCombined sources6
Regioni259 – 335Polysaccharide bindingAdd BLAST77

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi198 – 204Glucan phosphatase signature motif CXAGXGR1 Publication7

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.1 Publication

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1616 Eukaryota
KOG1716 Eukaryota
COG2453 LUCA
HOGENOMiHOG000005968
InParanoidiQ9FEB5
OMAiCTTVEIS
OrthoDBiEOG09360L0Y
PhylomeDBiQ9FEB5

Family and domain databases

Gene3Di2.60.40.10, 1 hit
3.90.190.10, 2 hits
InterProiView protein in InterPro
IPR032640 AMPK1_CBM
IPR030079 DSP4
IPR000340 Dual-sp_phosphatase_cat-dom
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
IPR029021 Prot-tyrosine_phosphatase-like
IPR000387 TYR_PHOSPHATASE_dom
IPR020422 TYR_PHOSPHATASE_DUAL_dom
PANTHERiPTHR10343:SF58 PTHR10343:SF58, 1 hit
PfamiView protein in Pfam
PF16561 AMPK1_CBM, 1 hit
PF00782 DSPc, 1 hit
SMARTiView protein in SMART
SM00195 DSPc, 1 hit
SUPFAMiSSF52799 SSF52799, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS50056 TYR_PHOSPHATASE_2, 1 hit

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 [Q9FEB5-1]
KEGGiath:AT3G52180

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiDSP4_ARATH
AccessioniPrimary (citable) accession number: Q9FEB5
Secondary accession number(s): Q8LFS3
, Q944A8, Q9FDY9, Q9SUY7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: March 1, 2001
Last modified: April 25, 2018
This is version 115 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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