DSP4_ARATH
ID DSP4_ARATH Reviewed; 379 AA.
AC Q9FEB5; Q8LFS3; Q944A8; Q9FDY9; Q9SUY7;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Phosphoglucan phosphatase DSP4, chloroplastic;
DE EC=3.1.3.- {ECO:0000269|PubMed:16772378, ECO:0000269|PubMed:19141707, ECO:0000269|PubMed:19754155, ECO:0000269|PubMed:20018599, ECO:0000269|PubMed:24799671, ECO:0000269|PubMed:26231210};
DE AltName: Full=AtPTPKIS1;
DE AltName: Full=Dual specificity protein phosphatase 4;
DE AltName: Full=Protein STARCH-EXCESS 4;
DE Short=AtSEX4;
DE Flags: Precursor;
GN Name=DSP4; Synonyms=PTPKIS1, SEX4; OrderedLocusNames=At3g52180;
GN ORFNames=F4F15.290;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INTERACTION WITH KIN11.
RX PubMed=12148529; DOI=10.1046/j.1365-313x.2002.01250.x;
RA Fordham-Skelton A.P., Chilley P., Lumbreras V., Reignoux S., Fenton T.R.,
RA Dahm C.C., Pages M., Gatehouse J.A.;
RT "A novel higher plant protein tyrosine phosphatase interacts with SNF1-
RT related protein kinases via a KIS (kinase interaction sequence) domain.";
RL Plant J. 29:705-715(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=16513634; DOI=10.1074/jbc.m600519200;
RA Niittylae T., Comparot-Moss S., Lue W.L., Messerli G., Trevisan M.,
RA Seymour M.D., Gatehouse J.A., Villadsen D., Smith S.M., Chen J.,
RA Zeeman S.C., Smith A.M.;
RT "Similar protein phosphatases control starch metabolism in plants and
RT glycogen metabolism in mammals.";
RL J. Biol. Chem. 281:11815-11818(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION OF POLYSACCHARIDE-BINDING
RP DOMAIN, AND MUTAGENESIS OF TRP-278 AND LYS-307.
RX PubMed=16623901; DOI=10.1111/j.1365-313x.2006.02704.x;
RA Kerk D., Conley T.R., Rodriguez F.A., Tran H.T., Nimick M., Muench D.G.,
RA Moorhead G.B.;
RT "A chloroplast-localized dual-specificity protein phosphatase in
RT Arabidopsis contains a phylogenetically dispersed and ancient carbohydrate-
RT binding domain, which binds the polysaccharide starch.";
RL Plant J. 46:400-413(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP CYS-198, AND ACTIVE SITE.
RX PubMed=16772378; DOI=10.1073/pnas.0603329103;
RA Sokolov L.N., Dominguez-Solis J.R., Allary A.L., Buchanan B.B., Luan S.;
RT "A redox-regulated chloroplast protein phosphatase binds to starch
RT diurnally and functions in its accumulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9732-9737(2006).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF CYS-198; GLY-329 AND ASN-333.
RX PubMed=19754155; DOI=10.1021/bi9008853;
RA Hsu S., Kim Y., Li S., Durrant E.S., Pace R.M., Woods V.L. Jr.,
RA Gentry M.S.;
RT "Structural insights into glucan phosphatase dynamics using amide hydrogen-
RT deuterium exchange mass spectrometry.";
RL Biochemistry 48:9891-9902(2009).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF CYS-198.
RX PubMed=19141707; DOI=10.1105/tpc.108.064360;
RA Koetting O., Santelia D., Edner C., Eicke S., Marthaler T., Gentry M.S.,
RA Comparot-Moss S., Chen J., Smith A.M., Steup M., Ritte G., Zeeman S.C.;
RT "STARCH-EXCESS4 is a laforin-like Phosphoglucan phosphatase required for
RT starch degradation in Arabidopsis thaliana.";
RL Plant Cell 21:334-346(2009).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=19776162; DOI=10.1104/pp.109.144931;
RA Streb S., Egli B., Eicke S., Zeeman S.C.;
RT "The debate on the pathway of starch synthesis: a closer look at low-starch
RT mutants lacking plastidial phosphoglucomutase supports the chloroplast-
RT localized pathway.";
RL Plant Physiol. 151:1769-1772(2009).
RN [12]
RP FUNCTION.
RX PubMed=20018599; DOI=10.1104/pp.109.149914;
RA Hejazi M., Fettke J., Koetting O., Zeeman S.C., Steup M.;
RT "The Laforin-like dual-specificity phosphatase SEX4 from Arabidopsis
RT hydrolyzes both C6- and C3-phosphate esters introduced by starch-related
RT dikinases and thereby affects phase transition of alpha-glucans.";
RL Plant Physiol. 152:711-722(2010).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=22100529; DOI=10.1105/tpc.111.092155;
RA Santelia D., Koetting O., Seung D., Schubert M., Thalmann M., Bischof S.,
RA Meekins D.A., Lutz A., Patron N., Gentry M.S., Allain F.H., Zeeman S.C.;
RT "The phosphoglucan phosphatase like sex Four2 dephosphorylates starch at
RT the C3-position in Arabidopsis.";
RL Plant Cell 23:4096-4111(2011).
RN [14]
RP FUNCTION.
RX PubMed=22321580; DOI=10.1111/j.1467-7652.2012.00684.x;
RA Weise S.E., Aung K., Jarou Z.J., Mehrshahi P., Li Z., Hardy A.C.,
RA Carr D.J., Sharkey T.D.;
RT "Engineering starch accumulation by manipulation of phosphate metabolism of
RT starch.";
RL Plant Biotechnol. J. 10:545-554(2012).
RN [15]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-198; 199-THR--GLY-203 AND GLY-203,
RP MOTIF, AND ACTIVE SITE.
RX PubMed=26231210; DOI=10.1074/jbc.m115.658203;
RA Meekins D.A., Raththagala M., Auger K.D., Turner B.D., Santelia D.,
RA Koetting O., Gentry M.S., Vander Kooi C.W.;
RT "Mechanistic insights into glucan phosphatase activity against polyglucan
RT substrates.";
RL J. Biol. Chem. 290:23361-23370(2015).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 90-379 IN COMPLEX WITH PHOSPHATE,
RP FUNCTION, IDENTIFICATION OF PHOSPHATE-BINDING DOMAIN, INTERACTION OF
RP CATALYTIC AND POLYSACCHARIDE BINDING DOMAINS, MUTAGENESIS OF PHE-167 AND
RP CYS-198, AND ACTIVE SITE.
RX PubMed=20679247; DOI=10.1073/pnas.1009386107;
RA Vander Kooi C.W., Taylor A.O., Pace R.M., Meekins D.A., Guo H.F., Kim Y.,
RA Gentry M.S.;
RT "Structural basis for the glucan phosphatase activity of Starch Excess4.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15379-15384(2010).
RN [17] {ECO:0007744|PDB:4PYH}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 90-379 IN COMPLEX WITH THE
RP SUBSTRATE ANALOGS MALTOHEPTAOSE AND PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, MUTAGENESIS OF TYR-90; TYR-139; PHE-140; CYS-198; PHE-235;
RP LYS-237; TRP-278; LYS-307; TRP-314; HIS-330 AND ASN-332, AND ACTIVE SITE.
RX PubMed=24799671; DOI=10.1073/pnas.1400757111;
RA Meekins D.A., Raththagala M., Husodo S., White C.J., Guo H.F., Kotting O.,
RA Vander Kooi C.W., Gentry M.S.;
RT "Phosphoglucan-bound structure of starch phosphatase Starch Excess4 reveals
RT the mechanism for C6 specificity.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7272-7277(2014).
CC -!- FUNCTION: Starch granule-associated phosphoglucan phosphatase involved
CC in the control of starch accumulation. Acts as major regulator of the
CC initial steps of starch degradation at the granule surface. Functions
CC during the day by dephosphorylating the night-accumulated phospho-
CC oligosaccharides. Can release phosphate from both the C6 and the C3
CC positions, but dephosphorylates preferentially the C6 position
CC (PubMed:20018599, PubMed:26231210). {ECO:0000269|PubMed:16513634,
CC ECO:0000269|PubMed:16623901, ECO:0000269|PubMed:16772378,
CC ECO:0000269|PubMed:19141707, ECO:0000269|PubMed:19754155,
CC ECO:0000269|PubMed:20018599, ECO:0000269|PubMed:20679247,
CC ECO:0000269|PubMed:22100529, ECO:0000269|PubMed:22321580,
CC ECO:0000269|PubMed:24799671, ECO:0000269|PubMed:26231210}.
CC -!- INTERACTION:
CC Q9FEB5; P92958: KIN11; NbExp=2; IntAct=EBI-307215, EBI-307202;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16513634, ECO:0000269|PubMed:16623901,
CC ECO:0000269|PubMed:16772378}. Note=Associated with starch granule.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FEB5-1; Sequence=Displayed;
CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak at the end
CC of the day and then decreasing to reach the lowest levels at the end of
CC the night. {ECO:0000269|PubMed:22100529}.
CC -!- DOMAIN: Contains a C-terminal polysaccharide-binding domain which
CC interacts with the phosphatase domain; this interaction is required for
CC glucan phosphatase activity. {ECO:0000269|PubMed:20679247}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size, slightly delayed flowering,
CC leaves with large round starch granules and starch in excess.
CC {ECO:0000269|PubMed:16513634, ECO:0000269|PubMed:16772378,
CC ECO:0000269|PubMed:19776162}.
CC -!- MISCELLANEOUS: Starch binding efficiency is dependent on pH and redox
CC conditions. {ECO:0000305|PubMed:16772378}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41338.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC18327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ302781; CAC17593.1; -; mRNA.
DR EMBL; AJ302779; CAC18327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ302779; CAC18328.1; -; Genomic_DNA.
DR EMBL; AL049711; CAB41338.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78909.1; -; Genomic_DNA.
DR EMBL; AF439823; AAL27495.1; -; mRNA.
DR EMBL; AY143878; AAN28817.1; -; mRNA.
DR EMBL; AY084675; AAM61237.1; -; mRNA.
DR PIR; T49097; T49097.
DR RefSeq; NP_566960.1; NM_115078.4. [Q9FEB5-1]
DR PDB; 3NME; X-ray; 2.40 A; A/B=90-379.
DR PDB; 4PYH; X-ray; 1.65 A; A=90-379.
DR PDBsum; 3NME; -.
DR PDBsum; 4PYH; -.
DR AlphaFoldDB; Q9FEB5; -.
DR SMR; Q9FEB5; -.
DR BioGRID; 9701; 1.
DR IntAct; Q9FEB5; 1.
DR STRING; 3702.AT3G52180.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR PaxDb; Q9FEB5; -.
DR PRIDE; Q9FEB5; -.
DR EnsemblPlants; AT3G52180.1; AT3G52180.1; AT3G52180. [Q9FEB5-1]
DR GeneID; 824383; -.
DR Gramene; AT3G52180.1; AT3G52180.1; AT3G52180. [Q9FEB5-1]
DR KEGG; ath:AT3G52180; -.
DR Araport; AT3G52180; -.
DR TAIR; locus:2083845; AT3G52180.
DR eggNOG; KOG1616; Eukaryota.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_047075_2_0_1; -.
DR InParanoid; Q9FEB5; -.
DR PhylomeDB; Q9FEB5; -.
DR BioCyc; ARA:AT3G52180-MON; -.
DR BioCyc; MetaCyc:AT3G52180-MON; -.
DR PRO; PR:Q9FEB5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FEB5; baseline and differential.
DR Genevisible; Q9FEB5; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:2001066; F:amylopectin binding; IDA:UniProtKB.
DR GO; GO:0019203; F:carbohydrate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:TAIR.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB.
DR GO; GO:0005982; P:starch metabolic process; IMP:TAIR.
DR CDD; cd14526; DSP_laforin-like; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR030079; DSP4.
DR InterPro; IPR045204; DSP_laforin-like.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR46642:SF3; PTHR46642:SF3; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Carbohydrate metabolism; Chloroplast;
KW Hydrolase; Plastid; Protein phosphatase; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..379
FT /note="Phosphoglucan phosphatase DSP4, chloroplastic"
FT /id="PRO_0000417333"
FT DOMAIN 97..254
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..335
FT /note="Polysaccharide binding"
FT REGION 339..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 198..204
FT /note="Glucan phosphatase signature motif CXAGXGR"
FT /evidence="ECO:0000305|PubMed:26231210"
FT COMPBIAS 343..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000305|PubMed:16772378, ECO:0000305|PubMed:19141707,
FT ECO:0000305|PubMed:19754155, ECO:0000305|PubMed:20679247,
FT ECO:0000305|PubMed:24799671, ECO:0000305|PubMed:26231210"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4PYH"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4PYH"
FT BINDING 199..204
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:3NME, ECO:0007744|PDB:4PYH"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4PYH"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4PYH"
FT MUTAGEN 90
FT /note="Y->A: Reduces starch binding and glucan phosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 139
FT /note="Y->A: Mildly reduces starch binding and glucan
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 140
FT /note="F->A: Reduces glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 140
FT /note="F->W: Changes substrate specificity and enhances
FT glucan dephosphorylation at C3. Leads to preferential
FT glucan dephosphorylation at C6; when associated with G-
FT 235."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 167
FT /note="F->M: Increases glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:20679247"
FT MUTAGEN 167
FT /note="F->S: No effect on glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:20679247"
FT MUTAGEN 167
FT /note="F->Y: Reduces glucan phosphatase activity 3-fold."
FT /evidence="ECO:0000269|PubMed:20679247"
FT MUTAGEN 198
FT /note="C->S: Loss of glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:16772378,
FT ECO:0000269|PubMed:19141707, ECO:0000269|PubMed:19754155,
FT ECO:0000269|PubMed:20679247, ECO:0000269|PubMed:24799671,
FT ECO:0000269|PubMed:26231210"
FT MUTAGEN 200..203
FT /note="AGMG->TGFD: Loss of glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:26231210"
FT MUTAGEN 203
FT /note="G->D: Nearly abolishes glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:26231210"
FT MUTAGEN 235
FT /note="F->A: Slightly reduces starch binding and glucan
FT phosphatase activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 235
FT /note="F->G: Changes substrate specificity and enhances
FT glucan dephosphorylation at C3. Leads to preferential
FT glucan dephosphorylation at C6; when associated with W-
FT 140."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 237
FT /note="K->A: Slightly reduces glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 278
FT /note="W->A: Nearly abolishes glucan phosphatase activity.
FT Strongly reduces starch binding efficiency."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 278
FT /note="W->G: Reduces starch binding efficiency."
FT /evidence="ECO:0000269|PubMed:16623901"
FT MUTAGEN 307
FT /note="K->A: Strongly reduces glucan phosphatase activity.
FT Strongly reduces starch binding efficiency."
FT /evidence="ECO:0000269|PubMed:16623901,
FT ECO:0000269|PubMed:24799671"
FT MUTAGEN 314
FT /note="W->A: Nearly abolishes glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 329
FT /note="G->R: Loss starch-binding capacity."
FT /evidence="ECO:0000269|PubMed:19754155"
FT MUTAGEN 330
FT /note="H->A: Decreases glucan phosphatase activity."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 332
FT /note="N->A: Nearly abolishes glucan phosphatase activity.
FT Loss of starch binding."
FT /evidence="ECO:0000269|PubMed:24799671"
FT MUTAGEN 333
FT /note="N->K: Loss of glucan phosphatase activity and
FT starch-binding capacity."
FT /evidence="ECO:0000269|PubMed:19754155"
FT CONFLICT 64
FT /note="S -> R (in Ref. 4; AAL27495/AAN28817)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="M -> K (in Ref. 5; AAM61237)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> G (in Ref. 4; AAL27495/AAN28817)"
FT /evidence="ECO:0000305"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 144..152
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 169..190
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:4PYH"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:4PYH"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 292..310
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 344..352
FT /evidence="ECO:0007829|PDB:4PYH"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:4PYH"
FT HELIX 361..373
FT /evidence="ECO:0007829|PDB:4PYH"
SQ SEQUENCE 379 AA; 42626 MW; 4AA36B6E3E62A42B CRC64;
MNCLQNLPRC SVSPLLGFGC IQRDHSSSSS SLKMLISPPI KANDPKSRLV LHAVSESKSS
SEMSGVAKDE EKSDEYSQDM TQAMGAVLTY RHELGMNYNF IRPDLIVGSC LQTPEDVDKL
RKIGVKTIFC LQQDPDLEYF GVDISSIQAY AKKYSDIQHI RCEIRDFDAF DLRMRLPAVV
GTLYKAVKRN GGVTYVHCTA GMGRAPAVAL TYMFWVQGYK LMEAHKLLMS KRSCFPKLDA
IRNATIDILT GLKRKTVTLT LKDKGFSRVE ISGLDIGWGQ RIPLTLDKGT GFWILKRELP
EGQFEYKYII DGEWTHNEAE PFIGPNKDGH TNNYAKVVDD PTSVDGTTRE RLSSEDPELL
EEERSKLIQF LETCSEAEV
