P2C38_ARATH
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 03-AUG-2022, entry version 131.
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},
GN T2E22.7 {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.AT3G12620.2; -.
DR iPTMnet; Q9LHJ9; -.
DR PaxDb; Q9LHJ9; -.
DR PRIDE; Q9LHJ9; -.
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; locus:2091265; AT3G12620.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_2_0_1; -.
DR InParanoid; Q9LHJ9; -.
DR OMA; HGMSANV; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q9LHJ9; -.
DR PRO; PR:Q9LHJ9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHJ9; baseline and differential.
DR Genevisible; Q9LHJ9; AT.
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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IDA:UniProtKB.
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 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
