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Entry version 130 (25 May 2022)
Sequence version 1 (01 Mar 2001)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei90Substrate; via amide nitrogenCombined sources1
Binding sitei166SubstrateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei198Phosphocysteine intermediatePROSITE-ProRule annotation6 Publications1
Binding sitei307SubstrateCombined sources1
Binding sitei332SubstrateCombined sources1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processCarbohydrate metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT3G52180-MONOMER

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
CBM48, Carbohydrate-Binding Module Family 48

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DSP4
Synonyms:PTPKIS1, SEX4
Ordered Locus Names:At3g52180
ORF Names:F4F15.290
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT3G52180

The Arabidopsis Information Resource

More...
TAIRi
locus:2083845, AT3G52180

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chloroplast, Plastid

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 54ChloroplastSequence analysisAdd BLAST54
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000041733355 – 379Phosphoglucan phosphatase DSP4, chloroplasticAdd BLAST325

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9FEB5

PRoteomics IDEntifications database

More...
PRIDEi
Q9FEB5

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9FEB5, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9FEB5, AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
9701, 1 interactor

Protein interaction database and analysis system

More...
IntActi
Q9FEB5, 1 interactor

STRING: functional protein association networks

More...
STRINGi
3702.AT3G52180.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
Q9FEB5

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9FEB5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini97 – 254Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni54 – 76DisorderedSequence analysisAdd BLAST23
Regioni199 – 204Substrate bindingCombined sources6
Regioni259 – 335Polysaccharide bindingAdd BLAST77
Regioni339 – 358DisorderedSequence analysisAdd BLAST20

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi198 – 204Glucan phosphatase signature motif CXAGXGR1 Publication7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi343 – 358Basic and acidic residuesSequence analysisAdd BLAST16

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1616, Eukaryota
KOG1716, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_047075_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9FEB5

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9FEB5

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14526, DSP_laforin-like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 1 hit
3.90.190.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR032640, AMPK1_CBM
IPR030079, DSP4
IPR045204, DSP_laforin-like
IPR000340, Dual-sp_phosphatase_cat-dom
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR029021, Prot-tyrosine_phosphatase-like
IPR000387, Tyr_Pase_dom
IPR020422, TYR_PHOSPHATASE_DUAL_dom

The PANTHER Classification System

More...
PANTHERi
PTHR46642:SF3, PTHR46642:SF3, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16561, AMPK1_CBM, 1 hit
PF00782, DSPc, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00195, DSPc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52799, SSF52799, 1 hit
SSF81296, SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50056, TYR_PHOSPHATASE_2, 1 hit
PS50054, TYR_PHOSPHATASE_DUAL, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. According to EST sequences.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9FEB5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4AA36B6E3E62A42B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1I9LQR5A0A1I9LQR5_ARATH
Dual specificity protein phosphatas...
SEX4 ATPTPKIS1, ATSEX4, DSP4, STARCH-EXCESS 4, At3g52180
284Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F4J5T0F4J5T0_ARATH
Dual specificity protein phosphatas...
SEX4 ATPTPKIS1, ATSEX4, DSP4, STARCH-EXCESS 4, At3g52180
292Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1I9LQR6A0A1I9LQR6_ARATH
Dual specificity protein phosphatas...
SEX4 ATPTPKIS1, ATSEX4, DSP4, STARCH-EXCESS 4, At3g52180
281Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

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PIRi
T49097

NCBI Reference Sequences

More...
RefSeqi
NP_566960.1, NM_115078.4 [Q9FEB5-1]

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
AT3G52180.1; AT3G52180.1; AT3G52180 [Q9FEB5-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
824383

Gramene; a comparative resource for plants

More...
Gramenei
AT3G52180.1; AT3G52180.1; AT3G52180 [Q9FEB5-1]

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ath:AT3G52180

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NMEX-ray2.40A/B90-379[»]
4PYHX-ray1.65A90-379[»]
AlphaFoldDBiQ9FEB5
SMRiQ9FEB5
ModBaseiSearch...
PDBe-KBiSearch...

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

Genome annotation databases

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

Organism-specific databases

AraportiAT3G52180
TAIRilocus:2083845, AT3G52180

Phylogenomic databases

eggNOGiKOG1616, Eukaryota
KOG1716, Eukaryota
HOGENOMiCLU_047075_2_0_1
InParanoidiQ9FEB5
PhylomeDBiQ9FEB5

Enzyme and pathway databases

BioCyciARA:AT3G52180-MONOMER

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9FEB5

Gene expression databases

ExpressionAtlasiQ9FEB5, baseline and differential
GenevisibleiQ9FEB5, AT

Family and domain databases

CDDicd14526, DSP_laforin-like, 1 hit
Gene3Di2.60.40.10, 1 hit
3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR032640, AMPK1_CBM
IPR030079, DSP4
IPR045204, DSP_laforin-like
IPR000340, Dual-sp_phosphatase_cat-dom
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR029021, Prot-tyrosine_phosphatase-like
IPR000387, Tyr_Pase_dom
IPR020422, TYR_PHOSPHATASE_DUAL_dom
PANTHERiPTHR46642:SF3, PTHR46642:SF3, 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
PS50054, TYR_PHOSPHATASE_DUAL, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDSP4_ARATH
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9FEB5
Secondary accession number(s): Q8LFS3
, Q944A8, Q9FDY9, Q9SUY7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: March 1, 2001
Last modified: May 25, 2022
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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