DSP4_CASSA
ID DSP4_CASSA Reviewed; 375 AA.
AC G4LTX4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Phosphoglucan phosphatase DSP4, amyloplastic {ECO:0000250|UniProtKB:Q9FEB5};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q9FEB5};
DE AltName: Full=Dual specificity protein phosphatase 4 {ECO:0000303|PubMed:21631532};
DE Short=CsDSP4 {ECO:0000303|PubMed:21631532};
DE Flags: Precursor;
GN Name=DSP4 {ECO:0000312|EMBL:AAU43782.1};
GN Synonyms=SEX4 {ECO:0000303|PubMed:21631532};
OS Castanea sativa (Sweet chestnut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Fagaceae; Castanea.
OX NCBI_TaxID=21020;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAU43782.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Stem {ECO:0000269|PubMed:21631532};
RX PubMed=21631532; DOI=10.1111/j.1365-3040.2011.02365.x;
RA Berrocal-Lobo M., Ibanez C., Acebo P., Ramos A., Perez-Solis E.,
RA Collada C., Casado R., Aragoncillo C., Allona I.;
RT "Identification of a homolog of Arabidopsis DSP4 (SEX4) in chestnut: its
RT induction and accumulation in stem amyloplasts during winter or in response
RT to the cold.";
RL Plant Cell Environ. 34:1693-1704(2011).
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 (By similarity). {ECO:0000250|UniProtKB:Q9FEB5}.
CC -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC {ECO:0000269|PubMed:21631532}. Nucleus {ECO:0000269|PubMed:21631532}.
CC Note=In dormant or cold-stressed trees, localizes to both the
CC amyloplast stroma and nucleus. In conditions of vegetative growth,
CC detected in the nucleus only. {ECO:0000269|PubMed:21631532}.
CC -!- TISSUE SPECIFICITY: Expressed in phloem parenchyma of 16-24 week old
CC seedlings and 2 year old trees (at protein level). Expressed in leaves
CC of 16-24 week old seedlings and 2 year old trees.
CC {ECO:0000269|PubMed:21631532}.
CC -!- DEVELOPMENTAL STAGE: Shows seasonal variation in expression levels with
CC maximal levels from November-March (at protein level). Shows diurnal
CC fluctuations in expression level, with peak levels at dusk, under
CC conditions of natural light but not under conditions of continuous
CC light: may not have true circadian rhythmicity.
CC {ECO:0000269|PubMed:21631532}.
CC -!- INDUCTION: By cold stress for at least 9 days at 4 degrees Celsius.
CC {ECO:0000269|PubMed:21631532}.
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:0000250|UniProtKB:Q9FEB5}.
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DR EMBL; AY616240; AAU43782.1; -; mRNA.
DR AlphaFoldDB; G4LTX4; -.
DR SMR; G4LTX4; -.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009507; C:chloroplast; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019203; F:carbohydrate phosphatase activity; IEA:InterPro.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0007623; P:circadian rhythm; IEA:InterPro.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0005982; P:starch metabolic process; IEA:InterPro.
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 Amyloplast; Carbohydrate metabolism; Hydrolase; Nucleus; Plastid;
KW Protein phosphatase; Transit peptide.
FT TRANSIT 1..42
FT /note="Amyloplast"
FT /evidence="ECO:0000255"
FT CHAIN 43..375
FT /note="Phosphoglucan phosphatase DSP4, amyloplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000426727"
FT DOMAIN 92..249
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..330
FT /note="Polysaccharide binding"
FT /evidence="ECO:0000250|UniProtKB:Q9FEB5"
FT ACT_SITE 193
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 194..199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 42387 MW; 1B2030115EDA0AED CRC64;
MFCVQNLPRS SALPLQSFKS HQRRPPCSVN TLGVMSNVNL HRSMAVKAIS GPTSSAETSD
ANVEEEKSET YSTNMTEAMG AVLTYRHELG INYNFIRPDL IVGSCLQTPE DVDKLRSIGV
KTIFCLQQNS DLEYFGVDIN GIREYAKTYD DIQHLRAEIR DFDAFDLRVR LPAVVSKLYK
AINRNGGVTY VHCTAGLGRA PAVTLAYMFW VQGYKLIEAH NLLQSKRSCF PKLDAIKSAA
ADILTGLRKK VVTLTWKNPD CTTLEISGLD IGWGQRIPLQ FDEEQGLWIL RRELAEGCYE
YKYIVDGEWT INENELVTSA NKDGHVNNFV QVFDDNPDSF NANLRKRLTG DDPDLSMDER
LKIRQFLESI PDEEQ
