ID LSF2_ARATH Reviewed; 282 AA. AC Q9SRK5; Q8LBS6; DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 13-SEP-2023, entry version 129. DE RecName: Full=Phosphoglucan phosphatase LSF2, chloroplastic; DE EC=3.1.3.- {ECO:0000269|PubMed:22100529, ECO:0000269|PubMed:23832589, ECO:0000269|PubMed:26231210}; DE AltName: Full=Phosphoglucan phosphatase like sex Four2 {ECO:0000303|PubMed:22100529, ECO:0000303|PubMed:23832589}; DE AltName: Full=Protein LIKE SEX4 2 {ECO:0000303|PubMed:23832589}; DE Flags: Precursor; GN Name=LSF2; OrderedLocusNames=At3g10940; ORFNames=F9F8.24; 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 [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 [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Shinn P., Chen H., Kim C.J., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. 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, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP INDUCTION, AND DISRUPTION PHENOTYPE. 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 [7] RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-157; CYS-193; RP 194-SER--GLY-198 AND PHE-261, 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 [8] {ECO:0007744|PDB:4KYQ, ECO:0007744|PDB:4KYR} RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 79-282 IN COMPLEX WITH THE RP SUBSTRATE ANALOGS MALTOHEXAOSE AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, RP ACTIVE SITE, AND MUTAGENESIS OF TYR-83; TYR-85; TYR-135; TRP-136; ARG-153; RP MET-155; ARG-157; PHE-162; TRP-180; CYS-193; LYS-245; PHE-261 AND GLU-268. RX PubMed=23832589; DOI=10.1105/tpc.113.112706; RA Meekins D.A., Guo H.F., Husodo S., Paasch B.C., Bridges T.M., Santelia D., RA Kotting O., Vander Kooi C.W., Gentry M.S.; RT "Structure of the Arabidopsis glucan phosphatase like sex four2 reveals a RT unique mechanism for starch dephosphorylation."; RL Plant Cell 25:2302-2314(2013). CC -!- FUNCTION: Starch-associated phosphoglucan phosphatase that selectively CC dephosphorylates the glucan C3 position. Probably participates in the CC regulation of starch degradation. {ECO:0000269|PubMed:22100529, CC ECO:0000269|PubMed:23832589, ECO:0000269|PubMed:26231210}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:22100529}. CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:22100529}. 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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth CC conditions, but starch of mutant plants contains high levels of C3- CC bound phosphate. {ECO:0000269|PubMed:22100529}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC009991; AAF01527.1; -; Genomic_DNA. DR EMBL; CP002686; AEE74980.1; -; Genomic_DNA. DR EMBL; BT024510; ABD19691.1; -; mRNA. DR EMBL; AK226225; BAE98389.1; -; mRNA. DR EMBL; AY087019; AAM64580.1; -; mRNA. DR RefSeq; NP_566383.1; NM_111931.3. DR PDB; 4KYQ; X-ray; 1.64 A; A=79-282. DR PDB; 4KYR; X-ray; 2.30 A; A=79-282. DR PDBsum; 4KYQ; -. DR PDBsum; 4KYR; -. DR AlphaFoldDB; Q9SRK5; -. DR SMR; Q9SRK5; -. DR STRING; 3702.AT3G10940.1; -. DR PaxDb; Q9SRK5; -. DR ProteomicsDB; 238804; -. DR EnsemblPlants; AT3G10940.1; AT3G10940.1; AT3G10940. DR GeneID; 820265; -. DR Gramene; AT3G10940.1; AT3G10940.1; AT3G10940. DR KEGG; ath:AT3G10940; -. DR Araport; AT3G10940; -. DR TAIR; AT3G10940; LSF2. DR eggNOG; KOG1716; Eukaryota. DR HOGENOM; CLU_085882_0_0_1; -. DR InParanoid; Q9SRK5; -. DR OMA; ELGIHHM; -. DR OrthoDB; 5472710at2759; -. DR PhylomeDB; Q9SRK5; -. DR PRO; PR:Q9SRK5; -. DR Proteomes; UP000006548; Chromosome 3. DR ExpressionAtlas; Q9SRK5; baseline and differential. DR Genevisible; Q9SRK5; AT. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0019203; F:carbohydrate phosphatase activity; IDA:UniProtKB. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro. DR GO; GO:2001070; F:starch binding; IDA:UniProtKB. DR GO; GO:0050308; F:sugar-phosphatase activity; IDA:TAIR. DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro. DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB. DR CDD; cd14526; DSP_laforin-like; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR045204; DSP_laforin-like. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000387; Tyr_Pase_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR46642; DUAL SPECIFICITY PHOSPHATASE, SUBGROUP, CATALYTIC DOMAIN; 1. DR PANTHER; PTHR46642:SF2; PHOSPHOGLUCAN PHOSPHATASE LSF2, CHLOROPLASTIC; 1. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Chloroplast; Hydrolase; Plastid; KW Protein phosphatase; Reference proteome; Transit peptide. FT TRANSIT 1..61 FT /note="Chloroplast" FT /evidence="ECO:0000255" FT CHAIN 62..282 FT /note="Phosphoglucan phosphatase LSF2, chloroplastic" FT /id="PRO_0000417335" FT DOMAIN 92..249 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT MOTIF 193..199 FT /note="Glucan phosphatase signature motif CXAGXGR" FT /evidence="ECO:0000305|PubMed:26231210" FT ACT_SITE 193 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000305|PubMed:26231210" FT BINDING 83 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 153..156 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 177..180 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 194..199 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 230 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 245 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 251 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 259..263 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT BINDING 268 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0007744|PDB:4KYR" FT MUTAGEN 83 FT /note="Y->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 85 FT /note="Y->A: Nearly abolishes starch C3 dephosphorylation. FT No effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 135 FT /note="Y->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 136 FT /note="W->A: Abolishes starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 153 FT /note="R->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 155 FT /note="M->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 157 FT /note="R->A: Decreases starch binding and starch C3 FT dephosphorylation. Moderate decrease of phosphatase FT activity with soluble substrates; when associated with A- FT 261. Nearly abolishes activity with water-insoluble starch; FT when associated with A-261." FT /evidence="ECO:0000269|PubMed:26231210" FT MUTAGEN 162 FT /note="F->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 180 FT /note="W->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 193 FT /note="C->S: Abolishes phosphatase activity." FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0000269|PubMed:26231210" FT MUTAGEN 194..198 FT /note="SAGLG->TTGFD: Abolishes glucan phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:26231210" FT MUTAGEN 245 FT /note="K->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT MUTAGEN 261 FT /note="F->A: Strongly decreases starch binding and starch FT C3 dephosphorylation. Moderate decrease of phosphatase FT activity with soluble substrates; when associated with A- FT 157. Nearly abolishes activity with water-insoluble starch; FT when associated with A-157." FT /evidence="ECO:0000269|PubMed:23832589, FT ECO:0000269|PubMed:26231210" FT MUTAGEN 268 FT /note="E->A: Decreases starch C3 dephosphorylation. No FT effect on phosphatase activity with p-nitrophenyl FT phosphate." FT /evidence="ECO:0000269|PubMed:23832589" FT CONFLICT 38..39 FT /note="RF -> SL (in Ref. 5; AAM64580)" FT /evidence="ECO:0000305" FT STRAND 80..83 FT /evidence="ECO:0007829|PDB:4KYR" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:4KYQ" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:4KYQ" FT STRAND 100..103 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 109..119 FT /evidence="ECO:0007829|PDB:4KYQ" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 130..136 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 140..149 FT /evidence="ECO:0007829|PDB:4KYQ" FT STRAND 153..156 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 164..184 FT /evidence="ECO:0007829|PDB:4KYQ" FT STRAND 186..192 FT /evidence="ECO:0007829|PDB:4KYQ" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 199..211 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 216..226 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 233..244 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:4KYR" FT HELIX 253..255 FT /evidence="ECO:0007829|PDB:4KYQ" FT TURN 258..261 FT /evidence="ECO:0007829|PDB:4KYQ" FT HELIX 266..278 FT /evidence="ECO:0007829|PDB:4KYQ" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:4KYQ" SQ SEQUENCE 282 AA; 32087 MW; BDB1A93855C98849 CRC64; MSVIGSKSCI FSVARYTREN EKSSCFTSIN KKSSLDLRFP RNLAGVSCKF SGENPGTNGV SLSSKNKMED YNTAMKRLMR SPYEYHHDLG MNYTLIRDEL IVGSQPQKPE DIDHLKQEQN VAYILNLQQD KDIEYWGIDL DSIVRRCKEL GIRHMRRPAK DFDPLSLRSQ LPKAVSSLEW AVSEGKGRVY VHCSAGLGRA PGVSIAYMYW FCDMNLNTAY DTLVSKRPCG PNKGAIRGAT YDLAKNDPWK EPFESLPENA FEDIADWERK LIQERVRALR GT //