ID   P2C67_ARATH             Reviewed;         370 AA.
AC   Q501F9; Q9LZ09;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Probable protein phosphatase 2C 67 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C67 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
GN   Name=PP2C67 {ECO:0000303|PubMed:19021904};
GN   Synonyms=PP2C-D1 {ECO:0000303|PubMed:24858935};
GN   OrderedLocusNames=At5g02760 {ECO:0000312|Araport:AT5G02760};
GN   ORFNames=F9G14.70 {ECO:0000312|EMBL:CAB86030.1};
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, MUTAGENESIS OF ASP-276, DISRUPTION PHENOTYPE, INTERACTION WITH
RP   SAUR19 AND AHA2, SUBCELLULAR LOCATION, 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   -!- SUBUNIT: Interacts with SAUR19 (PubMed:24858935). Interacts with AHA2
CC       at the plasma membrane (PubMed:24858935).
CC       {ECO:0000269|PubMed:24858935}.
CC   -!- INTERACTION:
CC       Q501F9; Q41220: SAUR15; NbExp=3; IntAct=EBI-25520600, EBI-25520581;
CC       Q501F9; Q9FJG0: SAUR20; NbExp=3; IntAct=EBI-25520600, EBI-25522374;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24858935};
CC       Peripheral membrane protein {ECO:0000269|PubMed:24858935}.
CC   -!- DISRUPTION PHENOTYPE: Reduced apical hook maintenance in etiolated
CC       seedlings (PubMed:24858935). The pp2c-d1 pp2c-d2 double mutant displays
CC       a long hypocotyl phenotype and strongly reduced apical hook maintenance
CC       in etiolated seedlings (PubMed:24858935).
CC       {ECO:0000269|PubMed:24858935}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB86030.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL162973; CAB86030.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90514.1; -; Genomic_DNA.
DR   EMBL; BT022008; AAY25420.1; -; mRNA.
DR   EMBL; BT023482; AAY57321.1; -; mRNA.
DR   PIR; T48297; T48297.
DR   RefSeq; NP_195896.2; NM_120354.3.
DR   AlphaFoldDB; Q501F9; -.
DR   SMR; Q501F9; -.
DR   BioGRID; 16512; 6.
DR   IntAct; Q501F9; 2.
DR   STRING; 3702.Q501F9; -.
DR   PaxDb; 3702-AT5G02760-1; -.
DR   ProteomicsDB; 250973; -.
DR   EnsemblPlants; AT5G02760.1; AT5G02760.1; AT5G02760.
DR   GeneID; 831234; -.
DR   Gramene; AT5G02760.1; AT5G02760.1; AT5G02760.
DR   KEGG; ath:AT5G02760; -.
DR   Araport; AT5G02760; -.
DR   TAIR; AT5G02760; APD7.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_2_0_1; -.
DR   InParanoid; Q501F9; -.
DR   OMA; PCWRIGA; -.
DR   OrthoDB; 999128at2759; -.
DR   PhylomeDB; Q501F9; -.
DR   PRO; PR:Q501F9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q501F9; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0016791; F:phosphatase activity; IDA:TAIR.
DR   GO; GO:1900056; P:negative regulation of leaf senescence; IMP:TAIR.
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:SF243; PROTEIN PHOSPHATASE 2C 67-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 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; Q501F9; AT.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Probable protein phosphatase 2C 67"
FT                   /id="PRO_0000367988"
FT   DOMAIN          35..344
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         78
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         335
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   MUTAGEN         276
FT                   /note="D->N: Phosphatase-dead, unable to repress the plasma
FT                   membrane H(+)-ATPase AHA2 activity."
FT                   /evidence="ECO:0000269|PubMed:24858935"
SQ   SEQUENCE   370 AA;  41334 MW;  9F21EC0115FD62FD CRC64;
     MVKPCWRIGA GMERSKINPT KVDGLTWYKD LGLHTFGEFS MAMIQANSVM EDQCQIESGP
     LTFNNPTVQG TFVGVYDGHG GPEASRFIAD NIFPKLKKFA SEGREISEQV ISKAFAETDK
     DFLKTVTKQW PTNPQMASVG SCCLAGVICN GLVYIANTGD SRAVLGRSER GGVRAVQLSV
     EHNANLESAR QELWSLHPND PTILVMKHRL WRVKGVIQVT RSIGDAYLKR AEFNREPLLP
     KFRLPEHFTK PILSADPSVT ITRLSPQDEF IILASDGLWE HLSNQEAVDI VHNSPRQGIA
     RRLLKAALKE AAKKREMRYS DLTEIHPGVR RHFHDDITVI VVYLNPHPVK TNSWASPLSI
     RGGYPMHSTS
//