P2C36_ARATH
ID P2C36_ARATH Reviewed; 650 AA.
AC Q9SR24;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable protein phosphatase 2C 36;
DE Short=AtPP2C36;
DE EC=3.1.3.16;
DE AltName: Full=Protein POLTERGEIST-LIKE 3;
DE AltName: Full=Protein phosphatase 2C PLL3;
DE Short=PP2C PLL3;
GN Name=PLL3; OrderedLocusNames=At3g09400; ORFNames=F3L24.29;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SR24-1; Sequence=Displayed;
CC -!- DOMAIN: The conserved PP2C phosphatase domain (240-639) 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; AC011436; AAF14035.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74761.1; -; Genomic_DNA.
DR RefSeq; NP_187551.1; NM_111774.2. [Q9SR24-1]
DR AlphaFoldDB; Q9SR24; -.
DR SMR; Q9SR24; -.
DR STRING; 3702.AT3G09400.1; -.
DR PaxDb; Q9SR24; -.
DR PRIDE; Q9SR24; -.
DR ProteomicsDB; 248875; -. [Q9SR24-1]
DR EnsemblPlants; AT3G09400.1; AT3G09400.1; AT3G09400. [Q9SR24-1]
DR GeneID; 820099; -.
DR Gramene; AT3G09400.1; AT3G09400.1; AT3G09400. [Q9SR24-1]
DR KEGG; ath:AT3G09400; -.
DR Araport; AT3G09400; -.
DR TAIR; locus:2083539; AT3G09400.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_12_1_1; -.
DR InParanoid; Q9SR24; -.
DR OMA; INKNSTH; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q9SR24; -.
DR PRO; PR:Q9SR24; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR24; 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 3: Inferred from homology;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..650
FT /note="Probable protein phosphatase 2C 36"
FT /id="PRO_0000301261"
FT DOMAIN 239..641
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 632
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 650 AA; 72381 MW; 54B6EBB6A4264106 CRC64;
MGNGVASFSG CCAGTTAGEI SGRYVTGVGL VQENLGHSFC YVRPVLTGSK SSFPPEPPLR
PDPIPGTTTT FRSISGASVS ANTSTALSTS LSTDTSGIAS AFESSNRFAS LPLQPVPRSP
IKKSDHGSGL FERRFLSGPI ESGLVSGKKT KEKAKLKKSG SKSFTKPKLK KSESKIFTFK
NVFTNLSCSK KSVIKPINGF DSFDGSSDTD RYIPEINSLS TIVSSHEKPR IKEEEDKTES
ALEEPKIQWA QGKAGEDRVH VILSEENGWL FVGIYDGFSG PDPPDYLIKN LYTAVLRELK
GLLWIDKGES YNRNGESNIE KQSTVEHASD SDQENCPVMN GNDVACGSRN ITSDVKKLQW
RCEWEHNSSN KSNNINHKDV LRALQQALEK TEESFDLMVN ENPELALMGS CVLVTLMKGE
DVYVMSVGDS RAVLARRPNV EKMKMQKELE RVKEESPLET LFITERGLSL LVPVQLNKEH
STSVEEEVRR IKKEHPDDIL AIENNRVKGY LKVTRAFGAG FLKQPKWNEA LLEMFRIDYV
GTSPYITCSP SLHHHRLSSR DKFLILSSDG LYEYFSNEEA IFEVDSFISA FPEGDPAQHL
IQEVLLRAAK KYGMDFHELL EIPQGDRRRY HDDVSVIVIS LEGRIWRSSM
