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 07-JUN-2017, entry version 105. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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., RA Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., RA Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., RA De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P., RA Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., RA Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., RA Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., RA Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., RA Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., RA Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., RA Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., RA 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., RA Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., RA Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., RA Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., RA Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., RA Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., RA Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., RA Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., RA Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA 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 RT thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Portal (Araport); RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. 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., RA Hayashizaki Y., 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 RP SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22100529; DOI=10.1105/tpc.111.092155; RA Santelia D., Koetting O., Seung D., Schubert M., Thalmann M., RA Bischof S., Meekins D.A., Lutz A., Patron N., Gentry M.S., RA Allain F.H., Zeeman S.C.; RT "The phosphoglucan phosphatase like sex Four2 dephosphorylates starch RT at 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 RT polyglucan substrates."; RL J. Biol. Chem. 290:23361-23370(2015). RN [8] {ECO:0000244|PDB:4KYQ, ECO:0000244|PDB:4KYR} RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 79-282 IN COMPLEX WITH THE RP SUBSTRATE ANALOGS MALTOHEXAOSE AND PHOSPHATE, FUNCTION, CATALYTIC RP ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF TYR-83; TYR-85; TYR-135; RP TRP-136; ARG-153; MET-155; ARG-157; PHE-162; TRP-180; CYS-193; RP 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., RA Santelia D., Kotting O., Vander Kooi C.W., Gentry M.S.; RT "Structure of the Arabidopsis glucan phosphatase like sex four2 RT reveals a unique mechanism for starch dephosphorylation."; RL Plant Cell 25:2302-2314(2013). CC -!- FUNCTION: Starch-associated phosphoglucan phosphatase that CC selectively dephosphorylates the glucan C3 position. Probably CC participates in the regulation of starch degradation. CC {ECO:0000269|PubMed:22100529, ECO:0000269|PubMed:23832589, CC ECO:0000269|PubMed:26231210}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast CC {ECO:0000269|PubMed:22100529}. CC -!- TISSUE SPECIFICITY: Widely expressed. CC {ECO:0000269|PubMed:22100529}. CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak at the CC end of the day and then decreasing to reach the lowest levels at CC the end of 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 CC C3-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 UniGene; At.39834; -. 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 ProteinModelPortal; Q9SRK5; -. DR SMR; Q9SRK5; -. DR STRING; 3702.AT3G10940.1; -. DR PaxDb; Q9SRK5; -. DR PRIDE; Q9SRK5; -. 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; locus:2085542; AT3G10940. DR eggNOG; KOG1716; Eukaryota. DR eggNOG; COG2453; LUCA. DR HOGENOM; HOG000243950; -. DR InParanoid; Q9SRK5; -. DR OMA; YLHCTAG; -. DR OrthoDB; EOG09360L0Y; -. DR PhylomeDB; Q9SRK5; -. DR BioCyc; ARA:AT3G10940-MONOMER; -. DR PRO; PR:Q9SRK5; -. DR Proteomes; UP000006548; Chromosome 3. 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:0046838; P:phosphorylated carbohydrate dephosphorylation; IDA:UniProtKB. DR GO; GO:0005983; P:starch catabolic process; IDA:UniProtKB. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR024950; DUSP. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom. DR PANTHER; PTHR10159; PTHR10159; 1. DR Pfam; PF00782; DSPc; 1. DR SMART; SM00195; DSPc; 1. DR SUPFAM; SSF52799; SSF52799; 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; Complete proteome; KW Hydrolase; Plastid; Reference proteome; Transit peptide. FT TRANSIT 1 61 Chloroplast. {ECO:0000255}. FT CHAIN 62 282 Phosphoglucan phosphatase LSF2, FT chloroplastic. FT /FTId=PRO_0000417335. FT DOMAIN 92 247 Tyrosine-protein phosphatase. FT REGION 153 156 Substrate binding. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT REGION 177 180 Substrate binding. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT REGION 194 199 Substrate binding. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT REGION 259 263 Substrate binding. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT MOTIF 193 199 Glucan phosphatase signature motif FT CXAGXGR. {ECO:0000305|PubMed:26231210}. FT ACT_SITE 193 193 Phosphocysteine intermediate. FT {ECO:0000305|PubMed:26231210}. FT BINDING 83 83 Substrate; via carbonyl oxygen. FT {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT BINDING 161 161 Substrate. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT BINDING 230 230 Substrate; via amide nitrogen. FT {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT BINDING 245 245 Substrate. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT BINDING 251 251 Substrate. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT BINDING 268 268 Substrate. {ECO:0000244|PDB:4KYR, FT ECO:0000269|PubMed:23832589}. FT MUTAGEN 83 83 Y->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 85 85 Y->A: Nearly abolishes starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 135 135 Y->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 136 136 W->A: Abolishes starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 153 153 R->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 155 155 M->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 157 157 R->A: Decreases starch binding and starch FT C3 dephosphorylation. Moderate decrease FT of phosphatase activity with soluble FT substrates; when associated with A-261. FT Nearly abolishes activity with water- FT insoluble starch; when associated with A- FT 261. {ECO:0000269|PubMed:26231210}. FT MUTAGEN 162 162 F->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 180 180 W->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 193 193 C->S: Abolishes phosphatase activity. FT {ECO:0000269|PubMed:23832589, FT ECO:0000269|PubMed:26231210}. FT MUTAGEN 194 198 SAGLG->TTGFD: Abolishes glucan FT phosphatase activity. FT {ECO:0000269|PubMed:26231210}. FT MUTAGEN 245 245 K->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT MUTAGEN 261 261 F->A: Strongly decreases starch binding FT and starch C3 dephosphorylation. Moderate FT decrease of phosphatase activity with FT soluble substrates; when associated with FT A-157. Nearly abolishes activity with FT water-insoluble starch; when associated FT with A-157. {ECO:0000269|PubMed:23832589, FT ECO:0000269|PubMed:26231210}. FT MUTAGEN 268 268 E->A: Decreases starch C3 FT dephosphorylation. No effect on FT phosphatase activity with p-nitrophenyl FT phosphate. {ECO:0000269|PubMed:23832589}. FT CONFLICT 38 39 RF -> SL (in Ref. 5; AAM64580). FT {ECO:0000305}. FT STRAND 80 83 {ECO:0000244|PDB:4KYR}. FT HELIX 87 89 {ECO:0000244|PDB:4KYQ}. FT STRAND 93 97 {ECO:0000244|PDB:4KYQ}. FT STRAND 100 103 {ECO:0000244|PDB:4KYQ}. FT HELIX 109 119 {ECO:0000244|PDB:4KYQ}. FT STRAND 121 126 {ECO:0000244|PDB:4KYQ}. FT HELIX 130 136 {ECO:0000244|PDB:4KYQ}. FT HELIX 140 149 {ECO:0000244|PDB:4KYQ}. FT STRAND 153 156 {ECO:0000244|PDB:4KYQ}. FT HELIX 164 184 {ECO:0000244|PDB:4KYQ}. FT STRAND 186 192 {ECO:0000244|PDB:4KYQ}. FT STRAND 194 198 {ECO:0000244|PDB:4KYQ}. FT HELIX 199 211 {ECO:0000244|PDB:4KYQ}. FT HELIX 216 226 {ECO:0000244|PDB:4KYQ}. FT HELIX 233 244 {ECO:0000244|PDB:4KYQ}. FT HELIX 248 250 {ECO:0000244|PDB:4KYR}. FT HELIX 253 255 {ECO:0000244|PDB:4KYQ}. FT TURN 258 261 {ECO:0000244|PDB:4KYQ}. FT HELIX 266 278 {ECO:0000244|PDB:4KYQ}. FT TURN 279 281 {ECO:0000244|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 //