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 22-JAN-2014, entry version 82. DE RecName: Full=Phosphoglucan phosphatase LSF2, chloroplastic; DE EC=3.1.3.-; DE AltName: Full=Phosphoglucan phosphatase like sex Four2; DE AltName: Full=Protein LIKE SEX4 2; 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; core eudicotyledons; 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., 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 Resource (TAIR); RL Submitted (APR-2011) 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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND RP 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). CC -!- FUNCTION: Starch-associated phosphoglucan phosphatase that can CC release phosphate from the C3 glucan position. Probably CC participates in the regulation of starch degradation. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. CC -!- TISSUE SPECIFICITY: Widely expressed. 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. CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth CC conditions, but starch of mutant plants contains high levels of CC C3-bound phosphate. CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain. 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_111931.2. 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; 85-243. DR STRING; 3702.AT3G10940.1-P; -. DR PRIDE; Q9SRK5; -. DR EnsemblPlants; AT3G10940.1; AT3G10940.1; AT3G10940. DR GeneID; 820265; -. DR KEGG; ath:AT3G10940; -. DR TAIR; AT3G10940; -. DR HOGENOM; HOG000243950; -. DR InParanoid; Q9SRK5; -. DR OMA; GMNYTLI; -. DR PhylomeDB; Q9SRK5; -. DR ProtClustDB; CLSN2688252; -. DR BioCyc; ARA:AT3G10940-MONOMER; -. DR Genevestigator; Q9SRK5; -. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:RefGenome. 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; IBA:RefGenome. DR GO; GO:0005983; P:starch catabolic process; IMP:UniProtKB. DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom. DR InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat. DR InterPro; IPR024950; DUSP. DR InterPro; IPR000387; Tyr/Dual-sp_Pase. DR PANTHER; PTHR10159; PTHR10159; 1. DR Pfam; PF00782; DSPc; 1. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG. 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 (Potential). FT CHAIN 62 282 Phosphoglucan phosphatase LSF2, FT chloroplastic. FT /FTId=PRO_0000417335. FT DOMAIN 92 247 Tyrosine-protein phosphatase. FT REGION 193 199 Substrate binding (By similarity). FT ACT_SITE 193 193 Phosphocysteine intermediate (By FT similarity). FT CONFLICT 38 39 RF -> SL (in Ref. 5; AAM64580). FT STRAND 80 83 FT HELIX 87 89 FT STRAND 93 97 FT STRAND 100 103 FT HELIX 109 119 FT STRAND 121 126 FT HELIX 130 136 FT HELIX 140 149 FT STRAND 153 156 FT HELIX 164 184 FT STRAND 186 192 FT STRAND 194 198 FT HELIX 199 211 FT HELIX 216 226 FT HELIX 233 244 FT HELIX 248 250 FT HELIX 253 255 FT TURN 258 261 FT HELIX 266 278 FT TURN 279 281 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 //