P2C42_ARATH
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 03-AUG-2022, entry version 101.
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},
GN K14A17.4 {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.AT3G17090.1; -.
DR PaxDb; Q0V7V2; -.
DR PRIDE; Q0V7V2; -.
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; locus:2086097; AT3G17090.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_2_0_1; -.
DR InParanoid; Q0V7V2; -.
DR OMA; WDYLSNE; -.
DR PhylomeDB; Q0V7V2; -.
DR PRO; PR:Q0V7V2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0V7V2; baseline and differential.
DR Genevisible; Q0V7V2; 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 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
