ID   P2C48_ARATH             Reviewed;         384 AA.
AC   Q94CL8; Q9M2W1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   04-NOV-2026, entry version 151.
DE   RecName: Full=Probable protein phosphatase 2C 48 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C48 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
DE   AltName: Full=Protein phosphatase 2C 6 {ECO:0000303|Ref.1};
GN   Name=PP2C6 {ECO:0000303|Ref.1};
GN   Synonyms=PP2C-D4 {ECO:0000303|PubMed:24858935}, PP2C48
GN   {ECO:0000303|PubMed:19021904};
GN   OrderedLocusNames=At3g55050 {ECO:0000312|Araport:AT3G55050};
GN   ORFNames=T15C9.50 {ECO:0000312|EMBL:CAB82700.1};
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 [GENOMIC DNA].
RA   Bargues M., Terol J., Paricio N., Perez-Alonso M.;
RT   "PP2C6, a new member of the PP2C family in Arabidopsis thaliana.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19021904; DOI=10.1186/1471-2164-9-550;
RA   Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.;
RT   "Genome-wide and expression analysis of protein phosphatase 2C in rice and
RT   Arabidopsis.";
RL   BMC Genomics 9:550-550(2008).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=24858935; DOI=10.1105/tpc.114.126037;
RA   Spartz A.K., Ren H., Park M.Y., Grandt K.N., Lee S.H., Murphy A.S.,
RA   Sussman M.R., Overvoorde P.J., Gray W.M.;
RT   "SAUR inhibition of PP2C-D phosphatases activates plasma membrane H+-
RT   ATPases to promote cell expansion in Arabidopsis.";
RL   Plant Cell 26:2129-2142(2014).
CC   -!- FUNCTION: May dephosphorylate and repress plasma membrane H(+)-ATPases
CC       (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively
CC       plant growth and fitness. {ECO:0000250|UniProtKB:Q84JD5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000250|UniProtKB:Q9LHJ9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000250|UniProtKB:Q9LHJ9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P35813};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P35813};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:P35813};
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB82700.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ302053; CAC44619.1; -; Genomic_DNA.
DR   EMBL; AL132970; CAB82700.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE79332.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79333.1; -; Genomic_DNA.
DR   EMBL; OZ408685; CAO7044498.1; -; Genomic_DNA.
DR   EMBL; BT014892; AAT44968.1; -; mRNA.
DR   EMBL; BT021925; AAX49374.1; -; mRNA.
DR   EMBL; AK229292; BAF01155.1; -; mRNA.
DR   PIR; T47644; T47644.
DR   RefSeq; NP_191065.2; NM_115363.3.
DR   RefSeq; NP_974438.1; NM_202709.2.
DR   AlphaFoldDB; Q94CL8; -.
DR   SMR; Q94CL8; -.
DR   BioGRID; 9987; 1.
DR   FunCoup; Q94CL8; 3498.
DR   IntAct; Q94CL8; 1.
DR   STRING; 3702.Q94CL8; -.
DR   iPTMnet; Q94CL8; -.
DR   PaxDb; 3702-Q94CL8; -.
DR   ProteomicsDB; 248801; -.
DR   DNASU; 824671; -.
DR   GeneID; 824671; -.
DR   KEGG; ath:AT3G55050; -.
DR   Araport; AT3G55050; -.
DR   TAIR; AT3G55050; PP2C.D4.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_2_0_1; -.
DR   InParanoid; Q94CL8; -.
DR   OMA; ATCSIKA; -.
DR   PhylomeDB; Q94CL8; -.
DR   PRO; PR:Q94CL8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   Proteomes; UP001984100; Chromosome 3.
DR   ExpressionAtlas; Q94CL8; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-ARBA.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:1902531; P:regulation of intracellular signal transduction; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   FunFam; 3.60.40.10:FF:000008; Phosphatase 2C family protein; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..384
FT                   /note="Probable protein phosphatase 2C 48"
FT                   /id="PRO_0000367972"
FT   DOMAIN          47..358
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         89
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         89
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         90
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         290
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         349
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LHJ9"
SQ   SEQUENCE   384 AA;  42851 MW;  26015C8E6737AE3A CRC64;
     MVSTTFRRIV SPCWRPFGIG EDSSPGSDDT NGRLDGLLWY KDSGNHITGE FSMAVVQANN
     LLEDHSQLES GPISLHESGP EATFVGVYDG HGGPEAARFV NDRLFYNIKR YTSEQRGMSP
     DVITRGFVAT EEEFLGLVQE QWKTKPQIAS VGACCLVGIV CNGLLYVANA GDSRVVLGKV
     ANPFKELKAV QLSTEHNASI ESVREELRLL HPDDPNIVVL KHKVWRVKGI IQVSRSIGDA
     YLKRAEFNQE PLLPKFRVPE RFEKPIMRAE PTITVHKIHP EDQFLIFASD GLWEHLSNQE
     AVDIVNSCPR NGVARKLVKA ALQEAAKKRE MRYSDLEKIE RGIRRHFHDD ITVIVVFLHA
     TNFATRTPIS VKGGGLLSAH NPVL
//