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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981Phosphocysteine intermediate

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi167 – 1671F → M: Increases glucan phosphatase activity. 1 Publication
Mutagenesisi167 – 1671F → S: No effect on glucan phosphatase activity. 1 Publication
Mutagenesisi167 – 1671F → Y: Reduces glucan phosphatase activity 3-fold. 1 Publication
Mutagenesisi198 – 1981C → S: Loss of glucan phosphatase activity and starch-binding capacity. 4 Publications
Mutagenesisi278 – 2781W → G: Reduces starch binding efficiency. 1 Publication
Mutagenesisi307 – 3071K → A: Reduces starch binding efficiency. 1 Publication
Mutagenesisi329 – 3291G → R: Loss starch-binding capacity. 1 Publication
Mutagenesisi333 – 3331N → K: Loss of glucan phosphatase activity and starch-binding capacity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454ChloroplastSequence analysisAdd
BLAST
Chaini55 – 379325Phosphoglucan phosphatase DSP4, chloroplasticPRO_0000417333Add
BLAST

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 interaction.
IntActiQ9FEB5. 1 interaction.
STRINGi3702.AT3G52180.1.

Structurei

Secondary structure

1
379
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi92 – 943Combined sources
Beta strandi98 – 1025Combined sources
Beta strandi105 – 1084Combined sources
Helixi115 – 1228Combined sources
Beta strandi125 – 1306Combined sources
Helixi134 – 1407Combined sources
Helixi144 – 1529Combined sources
Beta strandi158 – 1614Combined sources
Helixi169 – 19022Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi199 – 2035Combined sources
Helixi204 – 21512Combined sources
Helixi221 – 23111Combined sources
Helixi238 – 25013Combined sources
Beta strandi254 – 2629Combined sources
Beta strandi269 – 2735Combined sources
Turni274 – 2763Combined sources
Beta strandi277 – 2837Combined sources
Turni288 – 2903Combined sources
Beta strandi292 – 31019Combined sources
Beta strandi313 – 3153Combined sources
Beta strandi332 – 3376Combined sources
Helixi344 – 3529Combined sources
Beta strandi354 – 3563Combined sources
Helixi361 – 37313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NMEX-ray2.40A/B90-379[»]
4PYHX-ray1.65A90-379[»]
ProteinModelPortaliQ9FEB5.
SMRiQ9FEB5. Positions 90-378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 259148Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 2046Substrate binding
Regioni259 – 33577Polysaccharide bindingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 316Poly-Ser

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.
OMAiFCLQQDS.
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 CAB41338.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAC18327.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641S → R in AAL27495 (PubMed:14593172).Curated
Sequence conflicti64 – 641S → R in AAN28817 (PubMed:14593172).Curated
Sequence conflicti84 – 841M → K in AAM61237 (Ref. 5) Curated
Sequence conflicti287 – 2871D → G in AAL27495 (PubMed:14593172).Curated
Sequence conflicti287 – 2871D → G in AAN28817 (PubMed:14593172).Curated

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_115078.3. [Q9FEB5-1]
UniGeneiAt.24067.

Genome annotation databases

EnsemblPlantsiAT3G52180.1; AT3G52180.1; AT3G52180. [Q9FEB5-1]
GeneIDi824383.

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_115078.3. [Q9FEB5-1]
UniGeneiAt.24067.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NMEX-ray2.40A/B90-379[»]
4PYHX-ray1.65A90-379[»]
ProteinModelPortaliQ9FEB5.
SMRiQ9FEB5. Positions 90-378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi9701. 1 interaction.
IntActiQ9FEB5. 1 interaction.
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.

Organism-specific databases

TAIRiAT3G52180.

Phylogenomic databases

eggNOGiKOG1616. Eukaryota.
KOG1716. Eukaryota.
COG2453. LUCA.
HOGENOMiHOG000005968.
InParanoidiQ9FEB5.
OMAiFCLQQDS.
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...

Publicationsi

« Hide 'large scale' publications
  1. "A novel higher plant protein tyrosine phosphatase interacts with SNF1-related protein kinases via a KIS (kinase interaction sequence) domain."
    Fordham-Skelton A.P., Chilley P., Lumbreras V., Reignoux S., Fenton T.R., Dahm C.C., Pages M., Gatehouse J.A.
    Plant J. 29:705-715(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH KIN11.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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].
  6. "Similar protein phosphatases control starch metabolism in plants and glycogen metabolism in mammals."
    Niittylae T., Comparot-Moss S., Lue W.L., Messerli G., Trevisan M., Seymour M.D., Gatehouse J.A., Villadsen D., Smith S.M., Chen J., Zeeman S.C., Smith A.M.
    J. Biol. Chem. 281:11815-11818(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  7. "A chloroplast-localized dual-specificity protein phosphatase in Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-binding domain, which binds the polysaccharide starch."
    Kerk D., Conley T.R., Rodriguez F.A., Tran H.T., Nimick M., Muench D.G., Moorhead G.B.
    Plant J. 46:400-413(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF POLYSACCHARIDE-BINDING DOMAIN, MUTAGENESIS OF TRP-278 AND LYS-307.
  8. "A redox-regulated chloroplast protein phosphatase binds to starch diurnally and functions in its accumulation."
    Sokolov L.N., Dominguez-Solis J.R., Allary A.L., Buchanan B.B., Luan S.
    Proc. Natl. Acad. Sci. U.S.A. 103:9732-9737(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-198.
  9. "Structural insights into glucan phosphatase dynamics using amide hydrogen-deuterium exchange mass spectrometry."
    Hsu S., Kim Y., Li S., Durrant E.S., Pace R.M., Woods V.L. Jr., Gentry M.S.
    Biochemistry 48:9891-9902(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-198; GLY-329 AND ASN-333.
  10. "STARCH-EXCESS4 is a laforin-like Phosphoglucan phosphatase required for starch degradation in Arabidopsis thaliana."
    Koetting O., Santelia D., Edner C., Eicke S., Marthaler T., Gentry M.S., Comparot-Moss S., Chen J., Smith A.M., Steup M., Ritte G., Zeeman S.C.
    Plant Cell 21:334-346(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-198.
  11. "The debate on the pathway of starch synthesis: a closer look at low-starch mutants lacking plastidial phosphoglucomutase supports the chloroplast-localized pathway."
    Streb S., Egli B., Eicke S., Zeeman S.C.
    Plant Physiol. 151:1769-1772(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  12. "The Laforin-like dual-specificity phosphatase SEX4 from Arabidopsis hydrolyzes both C6- and C3-phosphate esters introduced by starch-related dikinases and thereby affects phase transition of alpha-glucans."
    Hejazi M., Fettke J., Koetting O., Zeeman S.C., Steup M.
    Plant Physiol. 152:711-722(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The phosphoglucan phosphatase like sex Four2 dephosphorylates starch at the C3-position in Arabidopsis."
    Santelia D., Koetting O., Seung D., Schubert M., Thalmann M., Bischof S., Meekins D.A., Lutz A., Patron N., Gentry M.S., Allain F.H., Zeeman S.C.
    Plant Cell 23:4096-4111(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  14. "Engineering starch accumulation by manipulation of phosphate metabolism of starch."
    Weise S.E., Aung K., Jarou Z.J., Mehrshahi P., Li Z., Hardy A.C., Carr D.J., Sharkey T.D.
    Plant Biotechnol. J. 10:545-554(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 90-379, FUNCTION, IDENTIFICATION OF PHOSPHATE-BINDING DOMAIN, INTERACTION OF CATALYTIC AND POLYSACCHARIDE BINDING DOMAINS, MUTAGENESIS OF PHE-167 AND CYS-198.

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: May 11, 2016
This is version 101 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.