ID   P2C38_ARATH             Reviewed;         385 AA.
AC   Q9LHJ9; Q9C7B3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Probable protein phosphatase 2C 38 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C38 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:27494702};
GN   Name=PP2C38 {ECO:0000303|PubMed:27494702};
GN   Synonyms=PP2C-D3 {ECO:0000303|PubMed:24858935};
GN   OrderedLocusNames=At3g12620 {ECO:0000312|Araport:AT3G12620};
GN   ORFNames=MMF12.6 {ECO:0000312|EMBL:BAB02253.1}, T2E22.7
GN   {ECO:0000312|EMBL:AAG51012.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [6]
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   [7]
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   [8]
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).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH BIK1, SUBCELLULAR LOCATION,
RP   PHOSPHORYLATION AT SER-77, AND MUTAGENESIS OF ASP-88 AND ASP-289.
RX   PubMed=27494702; DOI=10.1371/journal.ppat.1005811;
RA   Couto D., Niebergall R., Liang X., Buecherl C.A., Sklenar J., Macho A.P.,
RA   Ntoukakis V., Derbyshire P., Altenbach D., Maclean D., Robatzek S.,
RA   Uhrig J., Menke F., Zhou J.M., Zipfel C.;
RT   "The Arabidopsis protein phosphatase PP2C38 negatively regulates the
RT   central immune kinase BIK1.";
RL   PLoS Pathog. 12:E1005811-E1005811(2016).
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 (By similarity). Involved in pathogen-
CC       associated molecular pattern (PAMP)-triggered immunity (PTI) signaling
CC       (PubMed:27494702). Negatively regulates immune responses by controlling
CC       the phosphorylation and activation status of BIK1, a central rate-
CC       limiting kinase in PTI signaling (PubMed:27494702). Impairs the
CC       phosphorylation of the NADPH oxidase RBOHD by BIK1 (PubMed:27494702).
CC       {ECO:0000250|UniProtKB:Q84JD5, ECO:0000269|PubMed:27494702}.
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:0000269|PubMed:27494702};
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:0000269|PubMed:27494702};
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 BIK1. {ECO:0000269|PubMed:27494702}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27494702};
CC       Peripheral membrane protein {ECO:0000305}.
CC   -!- PTM: Phosphorylation at Ser-77 induces dissociation of PP2C38 from
CC       BIK1. {ECO:0000269|PubMed:27494702}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51012.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC069474; AAG51012.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP002044; BAB02253.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75224.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75225.1; -; Genomic_DNA.
DR   EMBL; BT004824; AAO44090.1; -; mRNA.
DR   EMBL; AK317334; BAH20008.1; -; mRNA.
DR   EMBL; AK317402; BAH20072.1; -; mRNA.
DR   EMBL; AK227879; BAE99854.1; -; mRNA.
DR   RefSeq; NP_001030682.1; NM_001035605.2.
DR   RefSeq; NP_187868.2; NM_112097.5.
DR   AlphaFoldDB; Q9LHJ9; -.
DR   SMR; Q9LHJ9; -.
DR   BioGRID; 5776; 3.
DR   IntAct; Q9LHJ9; 3.
DR   STRING; 3702.Q9LHJ9; -.
DR   iPTMnet; Q9LHJ9; -.
DR   PaxDb; 3702-AT3G12620-2; -.
DR   ProteomicsDB; 248795; -.
DR   DNASU; 820442; -.
DR   EnsemblPlants; AT3G12620.1; AT3G12620.1; AT3G12620.
DR   EnsemblPlants; AT3G12620.2; AT3G12620.2; AT3G12620.
DR   GeneID; 820442; -.
DR   Gramene; AT3G12620.1; AT3G12620.1; AT3G12620.
DR   Gramene; AT3G12620.2; AT3G12620.2; AT3G12620.
DR   KEGG; ath:AT3G12620; -.
DR   Araport; AT3G12620; -.
DR   TAIR; AT3G12620; PP2C.D3.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_2_0_1; -.
DR   InParanoid; Q9LHJ9; -.
DR   OMA; MKHQVWR; -.
DR   OrthoDB; 999128at2759; -.
DR   PhylomeDB; Q9LHJ9; -.
DR   PRO; PR:Q9LHJ9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LHJ9; baseline and differential.
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:1900425; P:negative regulation of defense response to bacterium; IDA:UniProtKB.
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:SF69; PROTEIN PHOSPHATASE 2C 38-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; Q9LHJ9; AT.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW   Phosphoprotein; Protein phosphatase; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Probable protein phosphatase 2C 38"
FT                   /id="PRO_0000367963"
FT   DOMAIN          46..357
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
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         289
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         348
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:27494702"
FT   MUTAGEN         88
FT                   /note="D->N: Abolishes phosphatase activity; when
FT                   associated with N-289."
FT                   /evidence="ECO:0000269|PubMed:27494702"
FT   MUTAGEN         289
FT                   /note="D->N: Abolishes phosphatase activity; when
FT                   associated with N-88."
FT                   /evidence="ECO:0000269|PubMed:27494702"
SQ   SEQUENCE   385 AA;  42851 MW;  72F7C983DB972D48 CRC64;
     MVSSATILRM VAPCWRRPSV KGDHSTRDAN GRCDGLLWYK DSGNHVAGEF SMSVIQANNL
     LEDHSKLESG PVSMFDSGPQ ATFVGVYDGH GGPEAARFVN KHLFDNIRKF TSENHGMSAN
     VITKAFLATE EDFLSLVRRQ WQIKPQIASV GACCLVGIIC SGLLYIANAG DSRVVLGRLE
     KAFKIVKAVQ LSSEHNASLE SVREELRSLH PNDPQIVVLK HKVWRVKGII QVSRSIGDAY
     LKKAEFNREP LLAKFRVPEV FHKPILRAEP AITVHKIHPE DQFLIFASDG LWEHLSNQEA
     VDIVNTCPRN GIARKLIKTA LREAAKKREM RYSDLKKIDR GVRRHFHDDI TVIVVFLDSH
     LVSRSTSRRP LLSISGGGDL AGPST
//