P2C66_ARATH
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 03-AUG-2022, entry version 124.
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.AT5G02400.1; -.
DR PaxDb; Q9LZ86; -.
DR PRIDE; Q9LZ86; -.
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; locus:2180152; AT5G02400.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_1_1; -.
DR InParanoid; Q9LZ86; -.
DR OMA; LDVQWAQ; -.
DR OrthoDB; 461546at2759; -.
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 GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
