ID   P2C29_ARATH             Reviewed;         783 AA.
AC   O82302; Q0WN23;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Protein phosphatase 2C 29;
DE            Short=AtPP2C29;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein POLTERGEIST-LIKE 1;
DE   AltName: Full=Protein phosphatase 2C PLL1;
DE            Short=PP2C PLL1;
GN   Name=PLL1; OrderedLocusNames=At2g35350; ORFNames=T32F12.27;
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=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   [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] OF 148-783.
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP   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   [6]
RP   FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
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   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
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   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
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: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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, inflorescences,
CC       flowers and developing vascular tissue. {ECO:0000269|PubMed:16112663}.
CC   -!- DOMAIN: The conserved PP2C phosphatase domain (257-736) is interrupted
CC       by an insertion of approximately 200 amino acids.
CC   -!- DISRUPTION PHENOTYPE: Loss-of-function mutant pll1-1 (T-DNA insertion)
CC       shows suppression of clavata mutant phenotypes. Redundant with POL. Pol
CC       and pll1 double mutant inis seedling lethal.
CC       {ECO:0000269|PubMed:17079273}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC36186.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAF01477.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF01477.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AC005314; AAC36186.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC09098.1; -; Genomic_DNA.
DR   EMBL; AK229632; BAF01477.1; ALT_SEQ; mRNA.
DR   PIR; E84767; E84767.
DR   RefSeq; NP_181078.2; NM_129087.3.
DR   AlphaFoldDB; O82302; -.
DR   SMR; O82302; -.
DR   STRING; 3702.O82302; -.
DR   iPTMnet; O82302; -.
DR   PaxDb; 3702-AT2G35350-1; -.
DR   ProteomicsDB; 248796; -.
DR   EnsemblPlants; AT2G35350.1; AT2G35350.1; AT2G35350.
DR   GeneID; 818102; -.
DR   Gramene; AT2G35350.1; AT2G35350.1; AT2G35350.
DR   KEGG; ath:AT2G35350; -.
DR   Araport; AT2G35350; -.
DR   TAIR; AT2G35350; PLL1.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_12_1_1; -.
DR   InParanoid; O82302; -.
DR   OMA; EDGVQWA; -.
DR   OrthoDB; 999128at2759; -.
DR   PhylomeDB; O82302; -.
DR   PRO; PR:O82302; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O82302; baseline and differential.
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:0010074; P:maintenance of meristem identity; IGI:TAIR.
DR   GO; GO:0009933; P:meristem structural organization; IGI:TAIR.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IGI:TAIR.
DR   GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF301; PROTEIN PHOSPHATASE 2C 29; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 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..783
FT                   /note="Protein phosphatase 2C 29"
FT                   /id="PRO_0000301259"
FT   DOMAIN          260..770
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          151..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..583
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         701
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         761
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:14506206,
FT                   ECO:0007744|PubMed:15308754"
SQ   SEQUENCE   783 AA;  86523 MW;  431BC94F054E5FD5 CRC64;
     MGSGFSSLLP CFNQGHRNRR RHSSAANPSH SDLIDSFREP LDETLGHSYC YVPSSSNRFI
     SPFPSDRFVS PTASFRLSPP HEPGRIRGSG SSEQLHTGFR AISGASVSAN TSNSKTVLQL
     EDIYDDATES SFGGGVRRSV VNANGFEGTS SFSALPLQPG PDRSGLFMSG PIERGATSGP
     LDPPAGEISR SNSAGVHFSA PLGGVYSKKR RKKKKKSLSW HPIFGGEKKQ RPWVLPVSNF
     VVGAKKENIV RPDVEAMAAS SGENDLQWAL GKAGEDRVQL AVFEKQGWLF AGIYDGFNGP
     DAPEFLMANL YRAVHSELQG LFWELEEEDD NPTDISTREL EQQGEFEDHV NEMASSSCPA
     TEKEEEEMGK RLTSSLEVVE VKERKRLWEL LAEAQAEDAL DLSGSDRFAF SVDDAIGAGN
     AVSVGSKRWL LLSKLKQGLS KQGISGRKLF PWKSGVEENE TEEVDNVGVE EGVDKRRKRR
     KAGTVDHELV LKAMSNGLEA TEQAFLEMTD KVLETNPELA LMGSCLLVAL MRDDDVYIMN
     IGDSRALVAQ YQVEETGESV ETAERVEERR NDLDRDDGNK EPLVVDSSDS TVNNEAPLPQ
     TKLVALQLTT DHSTSIEDEV TRIKNEHPDD NHCIVNDRVK GRLKVTRAFG AGFLKQPKLN
     DALLEMFRNE YIGTDPYISC TPSLRHYRLT ENDQFMVLSS DGLYQYLSNV EVVSLAMEKF
     PDGDPAQHVI QELLVRAAKK AGMDFHELLD IPQGDRRKYH DDCTVLVIAL GGSRIWKSSG
     KYL
//