ID   P2C66_ARATH             Reviewed;         674 AA.
AC   Q9LZ86;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Probable protein phosphatase 2C 66;
DE            Short=AtPP2C66;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein POLTERGEIST-LIKE 2;
DE   AltName: Full=Protein phosphatase 2C PLL2;
DE            Short=PP2C PLL2;
GN   Name=PLL2; OrderedLocusNames=At5g02400; ORFNames=T1E22.160;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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   TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION 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   [4]
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   -!- 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 at low level in seedlings, roots, leaves,
CC       stems, young inflorescences, flowers and siliques.
CC       {ECO:0000269|PubMed:16112663}.
CC   -!- DOMAIN: The conserved PP2C phosphatase domain (244-663) is interrupted
CC       by an insertion of approximately 100 amino acids.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:16112663}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AL162874; CAB85545.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90468.1; -; Genomic_DNA.
DR   PIR; T48261; T48261.
DR   RefSeq; NP_195860.1; NM_120318.2.
DR   AlphaFoldDB; Q9LZ86; -.
DR   SMR; Q9LZ86; -.
DR   STRING; 3702.Q9LZ86; -.
DR   PaxDb; 3702-AT5G02400-1; -.
DR   EnsemblPlants; AT5G02400.1; AT5G02400.1; AT5G02400.
DR   GeneID; 830937; -.
DR   Gramene; AT5G02400.1; AT5G02400.1; AT5G02400.
DR   KEGG; ath:AT5G02400; -.
DR   Araport; AT5G02400; -.
DR   TAIR; AT5G02400; PLL2.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_12_1_1; -.
DR   InParanoid; Q9LZ86; -.
DR   OMA; KWRCEWE; -.
DR   OrthoDB; 676440at2759; -.
DR   PhylomeDB; Q9LZ86; -.
DR   PRO; PR:Q9LZ86; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZ86; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:SF671; PROTEIN PHOSPHATASE 2C 66-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..674
FT                   /note="Probable protein phosphatase 2C 66"
FT                   /id="PRO_0000301260"
FT   DOMAIN          244..665
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          153..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          373..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         593
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         656
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RWN7"
SQ   SEQUENCE   674 AA;  74838 MW;  CA2DE97E69791B0D CRC64;
     MGNGVTTLTG CCTGTLAGEI SRRYDVSLVH DGLGHSFCYI RPDLPGVVLP SPESPLRSDH
     IQETTFRSIS GASVSANPST ALSGALSSDS DCPYSSAVSA SAFESSGNFA SLPLQPVPRG
     STWQSGPIVN ESGLGSAPFE RRFLSGPIES GLYSGPIEST KKTEKEKPKK IRKKPKSKKN
     FLTFKTLFAN LISNNNKPRL KKSVIEPING SDSSDSGRLH HEPVITSSRS NENPKSDLEE
     EDEKQSMNSV LDVQWAQGKA GEDRVHVVVS EDNGWVFVGI YDGFSGPDAP DYLLNNLYTA
     VQKELNGLLW NDEKLRSLGE NGMTKTGKCS DEEDPESGKE NCPVINNDDA VASGARNQAK
     SLKWRCEWEK KSNNKTKSDN RCDQKGSNST TTNHKDVLKA LLQALRKTED AYLELADQMV
     KENPELALMG SCVLVTLMKG EDVYVMNVGD SRAVLGRKPN LATGRKRQKE LERIREDSSL
     EDKEILMNGA MRNTLVPLQL NMEHSTRIEE EVRRIKKEHP DDDCAVENDR VKGYLKVTRA
     FGAGFLKQPK WNDALLEMFR IDYIGTSPYI TCSPSLCHHK LTSRDKFLIL SSDGLYEYFS
     NQEAIFEVES FISAFPEGDP AQHLIQEVLL RAANKFGMDF HELLEIPQGD RRRYHDDVSV
     IVISLEGRIW RSSM
//