ID   P2C46_ARATH             Reviewed;         379 AA.
AC   Q9SD12;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Probable protein phosphatase 2C 46 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C46 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
DE   Flags: Precursor;
GN   Name=PP2C46 {ECO:0000303|PubMed:19021904};
GN   Synonyms=PP2C-D6 {ECO:0000303|PubMed:24858935};
GN   OrderedLocusNames=At3g51370 {ECO:0000312|Araport:AT3G51370};
GN   ORFNames=F26O13.10 {ECO:0000312|EMBL:CAB63001.1};
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 [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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
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   [5]
RP   INTERACTION WITH SAUR19, 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   -!- SUBUNIT: Interacts with SAUR19. {ECO:0000269|PubMed:24858935}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SD12-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SD12-2; Sequence=VSP_036772, VSP_036773;
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BX823319; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AL133452; CAB63001.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78784.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78785.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM65136.1; -; Genomic_DNA.
DR   EMBL; BX823319; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; T45768; T45768.
DR   RefSeq; NP_001327130.1; NM_001339513.1. [Q9SD12-1]
DR   RefSeq; NP_566949.2; NM_114996.4. [Q9SD12-1]
DR   RefSeq; NP_974411.1; NM_202682.2. [Q9SD12-2]
DR   AlphaFoldDB; Q9SD12; -.
DR   SMR; Q9SD12; -.
DR   BioGRID; 9618; 1.
DR   STRING; 3702.Q9SD12; -.
DR   PaxDb; 3702-AT3G51370-1; -.
DR   ProteomicsDB; 248716; -. [Q9SD12-1]
DR   EnsemblPlants; AT3G51370.1; AT3G51370.1; AT3G51370. [Q9SD12-1]
DR   EnsemblPlants; AT3G51370.2; AT3G51370.2; AT3G51370. [Q9SD12-2]
DR   EnsemblPlants; AT3G51370.3; AT3G51370.3; AT3G51370. [Q9SD12-1]
DR   GeneID; 824300; -.
DR   Gramene; AT3G51370.1; AT3G51370.1; AT3G51370. [Q9SD12-1]
DR   Gramene; AT3G51370.2; AT3G51370.2; AT3G51370. [Q9SD12-2]
DR   Gramene; AT3G51370.3; AT3G51370.3; AT3G51370. [Q9SD12-1]
DR   KEGG; ath:AT3G51370; -.
DR   Araport; AT3G51370; -.
DR   TAIR; AT3G51370; PP2C.D6.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_2_0_1; -.
DR   InParanoid; Q9SD12; -.
DR   OMA; MEHNASI; -.
DR   OrthoDB; 999128at2759; -.
DR   PhylomeDB; Q9SD12; -.
DR   PRO; PR:Q9SD12; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SD12; baseline and differential.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 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   PANTHER; PTHR47992:SF258; PROTEIN PHOSPHATASE 2C 46-RELATED; 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.
DR   Genevisible; Q9SD12; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..379
FT                   /note="Probable protein phosphatase 2C 46"
FT                   /id="PRO_0000367970"
FT   DOMAIN          42..353
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         84
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         84
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         85
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         344
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LHJ9"
FT   VAR_SEQ         1..85
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036772"
FT   VAR_SEQ         86..105
FT                   /note="HGGPETSRFVNDHLFQHLKR -> MHTRLQTNRAETKILFEFSG (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036773"
SQ   SEQUENCE   379 AA;  42179 MW;  342934B0CA4CB760 CRC64;
     MLSTLMKLLS ACLWPSSSSG KSSDSTGKQD GLLWYKDFGQ HLVGEFSMAV VQANNLLEDQ
     SQVESGPLST LDSGPYGTFI GIYDGHGGPE TSRFVNDHLF QHLKRFAAEQ ASMSVDVIKK
     AYEATEEGFL GVVTKQWPTK PQIAAVGSCC LVGVICGGML YIANVGDSRA VLGRAMKATG
     EVIALQLSAE HNVSIESVRQ EMHSLHPDDS HIVMLKHNVW RVKGLIQISR SIGDVYLKKA
     EFNKEPLYTK YRIREPFKRP ILSGEPTITE HEIQPQDKFL IFASDGLWEQ MSNQEAVDIV
     QNHPRNGIAR RLVKMALQEA AKKREMRYSD LKKIERGVRR HFHDDITVVI IFLDTNQVSS
     VKGPPLSIRG GGMTFPKKI
//