P2C29_ARATH
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 03-AUG-2022, entry version 138.
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.AT2G35350.1; -.
DR iPTMnet; O82302; -.
DR PaxDb; O82302; -.
DR PRIDE; O82302; -.
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; locus:2062481; AT2G35350.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_1_1; -.
DR InParanoid; O82302; -.
DR OMA; SAYLDMT; -.
DR OrthoDB; 461546at2759; -.
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:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
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..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
