P2C48_ARATH
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 03-AUG-2022, entry version 133.
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},
GN PP2C48 {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 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 [5]
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 [6]
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 [7]
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=H2O + O-phospho-L-seryl-[protein] = 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=H2O + O-phospho-L-threonyl-[protein] = 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; 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 IntAct; Q94CL8; 1.
DR STRING; 3702.AT3G55050.2; -.
DR PaxDb; Q94CL8; -.
DR PRIDE; Q94CL8; -.
DR ProteomicsDB; 248801; -.
DR DNASU; 824671; -.
DR EnsemblPlants; AT3G55050.1; AT3G55050.1; AT3G55050.
DR EnsemblPlants; AT3G55050.2; AT3G55050.2; AT3G55050.
DR GeneID; 824671; -.
DR Gramene; AT3G55050.1; AT3G55050.1; AT3G55050.
DR Gramene; AT3G55050.2; AT3G55050.2; AT3G55050.
DR KEGG; ath:AT3G55050; -.
DR Araport; AT3G55050; -.
DR TAIR; locus:2097238; AT3G55050.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_2_0_1; -.
DR InParanoid; Q94CL8; -.
DR OMA; FYNIKRY; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q94CL8; -.
DR PRO; PR:Q94CL8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94CL8; baseline and differential.
DR Genevisible; Q94CL8; AT.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
