LSF1_ARATH
ID LSF1_ARATH Reviewed; 591 AA.
AC F4J117; Q8LCU3; Q9SSA3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Phosphoglucan phosphatase LSF1, chloroplastic;
DE EC=3.1.3.-;
DE AltName: Full=Phosphoglucan phosphatase like sex Four1;
DE AltName: Full=Protein LIKE SEX4 1;
DE Flags: Precursor;
GN Name=LSF1; Synonyms=PTPKIS2; OrderedLocusNames=At3g01510; ORFNames=F4P13.6;
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].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17631522; DOI=10.1104/pp.107.104224;
RA Edner C., Li J., Albrecht T., Mahlow S., Hejazi M., Hussain H., Kaplan F.,
RA Guy C., Smith S.M., Steup M., Ritte G.;
RT "Glucan, water dikinase activity stimulates breakdown of starch granules by
RT plastidial beta-amylases.";
RL Plant Physiol. 145:17-28(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20018601; DOI=10.1104/pp.109.148981;
RA Comparot-Moss S., Koetting O., Stettler M., Edner C., Graf A., Weise S.E.,
RA Streb S., Lue W.L., MacLean D., Mahlow S., Ritte G., Steup M., Chen J.,
RA Zeeman S.C., Smith A.M.;
RT "A putative phosphatase, LSF1, is required for normal starch turnover in
RT Arabidopsis leaves.";
RL Plant Physiol. 152:685-697(2010).
CC -!- FUNCTION: Starch granule-associated phosphoglucan phosphatase involved
CC in the control of starch accumulation. Participates in the regulation
CC of the initial steps of starch degradation at the granule surface. May
CC release a different set of phosphate groups from those removed by DSP4.
CC {ECO:0000269|PubMed:20018601}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:20018601}. Note=Located on the surface of starch
CC granules.
CC -!- DISRUPTION PHENOTYPE: Slight reduction in rosette size and fresh weight
CC and increased starch content in leaves. {ECO:0000269|PubMed:20018601}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01536.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009325; AAF01536.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73678.1; -; Genomic_DNA.
DR EMBL; AY086403; AAM64470.1; -; mRNA.
DR RefSeq; NP_566139.1; NM_111017.3.
DR AlphaFoldDB; F4J117; -.
DR SMR; F4J117; -.
DR BioGRID; 6460; 1.
DR STRING; 3702.AT3G01510.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; F4J117; -.
DR PaxDb; F4J117; -.
DR PRIDE; F4J117; -.
DR ProteomicsDB; 238591; -.
DR EnsemblPlants; AT3G01510.1; AT3G01510.1; AT3G01510.
DR GeneID; 821127; -.
DR Gramene; AT3G01510.1; AT3G01510.1; AT3G01510.
DR KEGG; ath:AT3G01510; -.
DR Araport; AT3G01510; -.
DR TAIR; locus:2084133; AT3G01510.
DR eggNOG; KOG1616; Eukaryota.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_020896_0_0_1; -.
DR InParanoid; F4J117; -.
DR OrthoDB; 956412at2759; -.
DR PRO; PR:F4J117; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J117; baseline and differential.
DR Genevisible; F4J117; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009569; C:chloroplast starch grain; IDA:UniProtKB.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0043036; C:starch grain; IDA:TAIR.
DR GO; GO:0019203; F:carbohydrate phosphatase activity; IMP:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IEA:InterPro.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IMP:UniProtKB.
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; 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; IPR030066; LSF1.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR47661:SF2; PTHR47661:SF2; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 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..591
FT /note="Phosphoglucan phosphatase LSF1, chloroplastic"
FT /id="PRO_0000417334"
FT DOMAIN 291..453
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 390
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 390..396
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 102
FT /note="I -> V (in Ref. 3; AAM64470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 591 AA; 65741 MW; 8B68E0B0AC2D7B8F CRC64;
MAFLQQISGL GALERSCPSI MIGSSFRSGN GRVFDGRGIA YLGSREKFGF NRRRRVVLRV
VAMSSSSTPF KMNLNEYMVT LEKPLGIRFA LSADGKIFVH AIKKGSNAEK ARIIMVGDTL
KKASDSSGGT LVEIKDFGDT KKMLVEKTGS FSLVLERPFS PFPIQYLLHL SDLDLLYNRG
RVSFVTWNKN LLSSNLRASS QGSGNSGYAA FSSKFFTPQG WKLLNRQSNS FQSGTKKNIL
SPPISPLVSV FSEDVPGDGE WGYGNFPLEE YIKALDRSKG ELSYNHALGM RYSKITEQIY
VGSCIQTEED VENLSEAGIT AILNFQGGTE AQNWGIDSQS INDACQKSEV LMINYPIKDA
DSFDLRKKLP LCVGLLLRLL KKNHRVFVTC TTGFDRSSAC VIAYLHWMTD TSLHAAYSFV
TGLHACKPDR PAIAWATWDL IAMVDDGKHD GTPTHSVTFV WNGHEGEEVL LVGDFTGNWK
EPIKATHKGG PRFETEVRLT QGKYYYKYII NGDWRHSATS PTERDDRGNT NNIIVVGDVA
NVRPTIQQPR KDANIIKVIE RVLTESERFR LAKAARCIAF SVCPIRLCPK S
