ID   P2C42_ARATH             Reviewed;         384 AA.
AC   Q0V7V2; Q2V3V2; Q8LEW2; Q9LSN8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Probable protein phosphatase 2C 42 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C42 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
GN   Name=PP2C42 {ECO:0000303|PubMed:19021904};
GN   Synonyms=PP2C-D2 {ECO:0000303|PubMed:24858935};
GN   OrderedLocusNames=At3g17090 {ECO:0000312|Araport:AT3G17090};
GN   ORFNames=K14A17.16 {ECO:0000312|EMBL:BAA94987.1}, K14A17.4
GN   {ECO:0000312|EMBL:BAA94987.1};
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [5]
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   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, 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: Dephosphorylates and represses plasma membrane H(+)-ATPases
CC       (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively
CC       plant growth and fitness (PubMed:24858935). Promotes the apical hook
CC       maintenance of etiolated seedlings (PubMed:24858935).
CC       {ECO:0000269|PubMed:24858935}.
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   -!- INTERACTION:
CC       Q0V7V2; Q41220: SAUR15; NbExp=3; IntAct=EBI-25517797, EBI-25520581;
CC       Q0V7V2; Q9FJG0: SAUR20; NbExp=3; IntAct=EBI-25517797, EBI-25522374;
CC       Q0V7V2; A0A1I9LQF0: SAUR57; NbExp=3; IntAct=EBI-25517797, EBI-25517419;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0V7V2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0V7V2-2; Sequence=VSP_036770, VSP_036771;
CC   -!- DISRUPTION PHENOTYPE: The pp2c-d1 pp2c-d2 double mutant displays a long
CC       hypocotyl phenotype and strongly reduced apical hook maintenance in
CC       etiolated seedlings (PubMed:24858935). Plants missing PP2C42/PP2C-D2,
CC       PP2C64/PP2C-D5, PP2C79/PP2C-D7, PP2C63/PP2C-D8 and PP2C68/PP2C-D9
CC       exhibit an increased hypocotyl length, as well as an enhanced
CC       sensitivity to LiCl and media acidification (PubMed:24858935).
CC       {ECO:0000269|PubMed:24858935}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA94987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB026636; BAA94987.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE75902.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75903.1; -; Genomic_DNA.
DR   EMBL; BT026468; ABH04575.1; -; mRNA.
DR   EMBL; AY085196; AAM61747.1; -; mRNA.
DR   RefSeq; NP_001030714.1; NM_001035637.1. [Q0V7V2-2]
DR   RefSeq; NP_566566.1; NM_112585.3. [Q0V7V2-1]
DR   AlphaFoldDB; Q0V7V2; -.
DR   SMR; Q0V7V2; -.
DR   BioGRID; 6299; 3.
DR   IntAct; Q0V7V2; 3.
DR   STRING; 3702.Q0V7V2; -.
DR   PaxDb; 3702-AT3G17090-1; -.
DR   ProteomicsDB; 248878; -. [Q0V7V2-1]
DR   EnsemblPlants; AT3G17090.1; AT3G17090.1; AT3G17090. [Q0V7V2-1]
DR   EnsemblPlants; AT3G17090.2; AT3G17090.2; AT3G17090. [Q0V7V2-2]
DR   GeneID; 820966; -.
DR   Gramene; AT3G17090.1; AT3G17090.1; AT3G17090. [Q0V7V2-1]
DR   Gramene; AT3G17090.2; AT3G17090.2; AT3G17090. [Q0V7V2-2]
DR   KEGG; ath:AT3G17090; -.
DR   Araport; AT3G17090; -.
DR   TAIR; AT3G17090; PP2C.D2.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_2_0_1; -.
DR   InParanoid; Q0V7V2; -.
DR   OMA; FHDIGNC; -.
DR   OrthoDB; 999128at2759; -.
DR   PhylomeDB; Q0V7V2; -.
DR   PRO; PR:Q0V7V2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q0V7V2; 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:SF159; PROTEIN PHOSPHATASE 2C 42-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; Q0V7V2; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..384
FT                   /note="Probable protein phosphatase 2C 42"
FT                   /id="PRO_0000367966"
FT   DOMAIN          58..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   VAR_SEQ         312..316
FT                   /note="GSAKR -> VTQRD (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036770"
FT   VAR_SEQ         317..384
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_036771"
FT   CONFLICT        39
FT                   /note="G -> R (in Ref. 4; AAM61747)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   384 AA;  42489 MW;  5F732834DB387794 CRC64;
     MSGSLMNLFS LCFKPFGHVC DNSEAGSGGG GGVSGGTGGE GKDGLLWFRD LGKYCGGDFS
     MAVIQANQVL EDQSQVESGN FGTFVGVYDG HGGPEAARYV CDHLFNHFRE ISAETQGVVT
     RETIERAFHA TEEGFASIVS ELWQEIPNLA TVGTCCLVGV IYQNTLFVAS LGDSRVVLGK
     KGNCGGLSAI QLSTEHNANN EDIRWELKDL HPDDPQIVVF RHGVWRVKGI IQVSRSIGDM
     YMKRPEFNKE PISQKFRIAE PMKRPLMSAT PTILSHPLHP NDSFLIFASD GLWEHLTNEK
     AVEIVHNHPR AGSAKRLIKA ALHEAARKRE MRYSDLRKID KKVRRHFHDD ITVIVVFLNH
     DLISRGHINS TQDTTVSIRS ALEH
//