P2C32_ARATH
ID P2C32_ARATH Reviewed; 856 AA.
AC Q8RWN7; O80732;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein phosphatase 2C 32;
DE Short=AtPP2C32;
DE EC=3.1.3.16;
DE AltName: Full=Protein POLTERGEIST;
DE AltName: Full=Protein phosphatase 2C POL;
DE Short=PP2C POL;
GN Name=POL; OrderedLocusNames=At2g46920; ORFNames=F14M4.25;
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 [GENOMIC DNA], MUTAGENESIS OF GLU-287 AND
RP 443-GLN--ARG-856, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION, AND
RP ACTIVITY REGULATION.
RX PubMed=12573213; DOI=10.1016/s0960-9822(03)00042-3;
RA Yu L.P., Miller A.K., Clark S.E.;
RT "POLTERGEIST encodes a protein phosphatase 2C that regulates CLAVATA
RT pathways controlling stem cell identity at Arabidopsis shoot and flower
RT meristems.";
RL Curr. Biol. 13:179-188(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION.
RX PubMed=10725242; DOI=10.1242/dev.127.8.1661;
RA Yu L.P., Simon E.J., Trotochaud A.E., Clark S.E.;
RT "POLTERGEIST functions to regulate meristem development downstream of the
RT CLAVATA loci.";
RL Development 127:1661-1670(2000).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-189, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152 AND SER-189, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16112663; DOI=10.1016/j.ydbio.2005.06.020;
RA Song S.-K., Clark S.E.;
RT "POL and related phosphatases are dosage-sensitive regulators of meristem
RT and organ development in Arabidopsis.";
RL Dev. Biol. 285:272-284(2005).
RN [9]
RP FUNCTION.
RX PubMed=17079273; DOI=10.1242/dev.02652;
RA Song S.-K., Lee M.M., Clark S.E.;
RT "POL and PLL1 phosphatases are CLAVATA1 signaling intermediates required
RT for Arabidopsis shoot and floral stem cells.";
RL Development 133:4691-4698(2006).
RN [10]
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).
CC -!- FUNCTION: Involved in the regulation of pedicel length and of CLAVATA
CC pathways controlling stem cell identity at shoot and flower meristems.
CC {ECO:0000269|PubMed:10725242, ECO:0000269|PubMed:12573213,
CC ECO:0000269|PubMed:16112663, ECO:0000269|PubMed:17079273}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Insensitive to okadaic acid.
CC {ECO:0000269|PubMed:12573213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, inflorescences,
CC flowers and throughout the shoot meristem.
CC {ECO:0000269|PubMed:12573213, ECO:0000269|PubMed:16112663}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development of the floral
CC meristem, in all four floral whorls and as floral organs matured,
CC limited to the ovule. {ECO:0000269|PubMed:12573213}.
CC -!- DOMAIN: The N-terminal domain (1-233) has a regulatory function and
CC inhibits phosphatase activity.
CC -!- DOMAIN: The conserved PP2C phosphatase domain (271-833) is interrupted
CC by an insertion of approximately 200 amino acids.
CC -!- DISRUPTION PHENOTYPE: Loss-of-function mutant pol-6 (T-DNA insertion)
CC shows suppression of clavata mutant phenotypes. The catalytic activity
CC of POL may be functionally replaced by the activity of PLL1. Pol and
CC pll1 double mutant is seedling lethal. {ECO:0000269|PubMed:16112663}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004411; AAC34239.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10772.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10773.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63296.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63297.1; -; Genomic_DNA.
DR EMBL; AY092972; AAM12971.1; -; mRNA.
DR PIR; T02195; T02195.
DR RefSeq; NP_001325391.1; NM_001337224.1.
DR RefSeq; NP_001325392.1; NM_001337223.1.
DR RefSeq; NP_850463.1; NM_180132.3.
DR RefSeq; NP_850464.1; NM_180133.2.
DR AlphaFoldDB; Q8RWN7; -.
DR SMR; Q8RWN7; -.
DR IntAct; Q8RWN7; 1.
DR MINT; Q8RWN7; -.
DR STRING; 3702.AT2G46920.1; -.
DR iPTMnet; Q8RWN7; -.
DR PaxDb; Q8RWN7; -.
DR PRIDE; Q8RWN7; -.
DR ProteomicsDB; 248712; -.
DR EnsemblPlants; AT2G46920.1; AT2G46920.1; AT2G46920.
DR EnsemblPlants; AT2G46920.2; AT2G46920.2; AT2G46920.
DR EnsemblPlants; AT2G46920.3; AT2G46920.3; AT2G46920.
DR EnsemblPlants; AT2G46920.4; AT2G46920.4; AT2G46920.
DR GeneID; 819306; -.
DR Gramene; AT2G46920.1; AT2G46920.1; AT2G46920.
DR Gramene; AT2G46920.2; AT2G46920.2; AT2G46920.
DR Gramene; AT2G46920.3; AT2G46920.3; AT2G46920.
DR Gramene; AT2G46920.4; AT2G46920.4; AT2G46920.
DR KEGG; ath:AT2G46920; -.
DR Araport; AT2G46920; -.
DR TAIR; locus:2041444; AT2G46920.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_1_1; -.
DR InParanoid; Q8RWN7; -.
DR OMA; CSNDRFL; -.
DR OrthoDB; 461546at2759; -.
DR PRO; PR:Q8RWN7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RWN7; baseline and differential.
DR Genevisible; Q8RWN7; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0005543; F:phospholipid binding; IDA:TAIR.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
DR GO; GO:0010074; P:maintenance of meristem identity; IGI:TAIR.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:TAIR.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 2.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 2.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..856
FT /note="Protein phosphatase 2C 32"
FT /id="PRO_0000301258"
FT DOMAIN 269..835
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 340..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 763
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 826
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O82302"
FT MUTAGEN 287
FT /note="E->K: In pol-1; reduced catalytic activity and
FT partial phenotypic suppression of mutations within
FT CLAVATA."
FT /evidence="ECO:0000269|PubMed:12573213"
FT MUTAGEN 443..856
FT /note="Missing: In pol-3; weak phenotypic suppression of
FT mutations within CLAVATA."
FT /evidence="ECO:0000269|PubMed:12573213"
FT CONFLICT 769
FT /note="F -> Y (in Ref. 4; AAM12971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 856 AA; 95571 MW; 95BDFC8DEB5DE4F2 CRC64;
MGNGTSRVVG CFVPSNDKNG VDLEFLEPLD EGLGHSFCYV RPSIFESPDI TPSNSERFTI
DSSTIDSETL TGSFRNDIVD DPSFLNRHNS KGLAETTFKA ISGASVSANV STARTGNQMA
LCSSDVLEPA ASFESTSSFA SIPLQPLPRG GSGPLNGFMS GPLERGFASG PLDRNNGFMS
GPIEKGVMSG PLDVSDRSNF SAPLSFRRKK PRFQRFMRSV SGPMKSTLAR TFSRRSGGLS
WMHRFFLHPE TRVSWAVGKD GKLHGEDPES CLESNRNLQW AHGKAGEDRV HVVLSEEQGW
LFIGIYDGFS GPDAPDFVMS HLYKAIDKEL EGLLWDYEEP SEDNQLQPDQ EPPTEENMCD
PESISEQHSK SVVAESEEVM IDDISSLGNT DTQIADGPPG DSAGPGKKSM RLYELLQLEQ
WEGEEIGLKR YGGNVALNNM TNQVENPSTS GGGAGNDPCT TDRSALDGIP NSGQRHGTKK
SQISSKIRRM YQKQKSLRKK LFPWSYDWHR EEGICVEEKI VESSGPIRRR WSGTVDHDAV
LRAMARALES TEEAYMDMVE KSLDINPELA LMGSCVLVML MKDQDVYVMN VGDSRAILAQ
ERLHDRHSNP GFGNDEGIGH KSRSRESLVR IELDRISEES PIHNQATPIS VSNKNRDVTS
YRLKMRAVQL SSDHSTSVEE EIWRIRSEHP EDDQSILKDR VKGQLKVTRA FGAGFLKKPN
FNEALLEMFQ VEYIGTDPYI TCEPCTVHHR LTSSDRFMVL SSDGLYEYFS NEEVVAHVTW
FIENVPEGDP AQYLIAELLS RAATKNGMEF HDLLDIPQGD RRKYHDDVSV MVVSLEGRIW
RSSGQYYPER KQKFNR
