P2C16_ARATH
ID P2C16_ARATH Reviewed; 511 AA.
AC Q9CAJ0; C0Z251; O81709; Q0WLM7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein phosphatase 2C 16;
DE Short=AtPP2C16;
DE EC=3.1.3.16;
DE AltName: Full=AtP2C-HA;
DE AltName: Full=Protein HYPERSENSITIVE TO ABA 1;
DE AltName: Full=Protein phosphatase 2C HAB1;
DE Short=PP2C HAB1;
DE Flags: Precursor;
GN Name=HAB1; Synonyms=P2C-HA; OrderedLocusNames=At1g72770; ORFNames=F28P22.4;
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 [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INDUCTION BY ABA.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9862504; DOI=10.1023/a:1006012218704;
RA Rodriguez P.L., Leube M.P., Grill E.;
RT "Molecular cloning in Arabidopsis thaliana of a new protein phosphatase 2C
RT (PP2C) with homology to ABI1 and ABI2.";
RL Plant Mol. Biol. 38:879-883(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-511 (ISOFORM 1).
RC TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ABA.
RX PubMed=14731256; DOI=10.1046/j.1365-313x.2003.01966.x;
RA Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P.,
RA Nicolas C., Lorenzo O., Rodriguez P.L.;
RT "Gain-of-function and loss-of-function phenotypes of the protein
RT phosphatase 2C HAB1 reveal its role as a negative regulator of abscisic
RT acid signalling.";
RL Plant J. 37:354-369(2004).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
RA Schweighofer A., Hirt H., Meskiene I.;
RT "Plant PP2C phosphatases: emerging functions in stress signaling.";
RL Trends Plant Sci. 9:236-243(2004).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLY-246.
RX PubMed=16876791; DOI=10.1016/j.febslet.2006.07.047;
RA Robert N., Merlot S., N'guyen V., Boisson-Dernier A., Schroeder J.I.;
RT "A hypermorphic mutation in the protein phosphatase 2C HAB1 strongly
RT affects ABA signaling in Arabidopsis.";
RL FEBS Lett. 580:4691-4696(2006).
RN [10]
RP INDUCTION BY ABA, AND TISSUE SPECIFICITY.
RX PubMed=16339800; DOI=10.1104/pp.105.070128;
RA Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T.,
RA Shinozaki K., Hirayama T.;
RT "ABA-hypersensitive germination3 encodes a protein phosphatase 2C (AtPP2CA)
RT that strongly regulates abscisic acid signaling during germination among
RT Arabidopsis protein phosphatase 2Cs.";
RL Plant Physiol. 140:115-126(2006).
RN [11]
RP FUNCTION.
RX PubMed=16798945; DOI=10.1104/pp.106.081018;
RA Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R.,
RA Rodriguez P.L.;
RT "Enhancement of abscisic acid sensitivity and reduction of water
RT consumption in Arabidopsis by combined inactivation of the protein
RT phosphatases type 2C ABI1 and HAB1.";
RL Plant Physiol. 141:1389-1399(2006).
RN [12]
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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SWI3B, AND MUTAGENESIS OF
RP GLY-246.
RX PubMed=19033529; DOI=10.1105/tpc.107.056705;
RA Saez A., Rodrigues A., Santiago J., Rubio S., Rodriguez P.L.;
RT "HAB1-SWI3B interaction reveals a link between abscisic acid signaling and
RT putative SWI/SNF chromatin-remodeling complexes in Arabidopsis.";
RL Plant Cell 20:2972-2988(2008).
RN [14]
RP INDUCTION BY MYB44.
RX PubMed=18162593; DOI=10.1104/pp.107.110981;
RA Jung C., Seo J.S., Han S.W., Koo Y.J., Kim C.H., Song S.I., Nahm B.H.,
RA Choi Y.D., Cheong J.-J.;
RT "Overexpression of AtMYB44 enhances stomatal closure to confer abiotic
RT stress tolerance in transgenic Arabidopsis.";
RL Plant Physiol. 146:623-635(2008).
RN [15]
RP INTERACTION WITH PYL5; PYL6 AND PYL8, AND MUTAGENESIS OF GLY-246.
RX PubMed=19624469; DOI=10.1111/j.1365-313x.2009.03981.x;
RA Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F.,
RA Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.;
RT "Modulation of drought resistance by the abscisic acid receptor PYL5
RT through inhibition of clade A PP2Cs.";
RL Plant J. 60:575-588(2009).
RN [16]
RP INTERACTION WITH PYL9/RCAR1.
RX PubMed=19407143; DOI=10.1126/science.1172408;
RA Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A.,
RA Grill E.;
RT "Regulators of PP2C phosphatase activity function as abscisic acid
RT sensors.";
RL Science 324:1064-1068(2009).
RN [17]
RP INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, AND ACTIVITY REGULATION.
RX PubMed=19407142; DOI=10.1126/science.1173041;
RA Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y.,
RA Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E., Bonetta D.,
RA Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L., McCourt P.,
RA Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.;
RT "Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family
RT of START proteins.";
RL Science 324:1068-1071(2009).
RN [18]
RP INTERACTION WITH PYL13.
RX PubMed=24165892; DOI=10.1038/cr.2013.143;
RA Li W., Wang L., Sheng X., Yan C., Zhou R., Hang J., Yin P., Yan N.;
RT "Molecular basis for the selective and ABA-independent inhibition of PP2CA
RT by PYL13.";
RL Cell Res. 23:1369-1379(2013).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 186-506 IN COMPLEX WITH
RP MAGNESIUM; ABSCISIC ACID AND PYL2, INTERACTION WITH PYR1; PYL1; PYL2; PYL3;
RP PYL4; PYL5 AND PYL6, AND LOCK SITE.
RX PubMed=19898420; DOI=10.1038/nature08613;
RA Melcher K., Ng L.-M., Zhou X.E., Soon F.-F., Xu Y., Suino-Powell K.M.,
RA Park S.-Y., Weiner J.J., Fujii H., Chinnusamy V., Kovach A., Li J.,
RA Wang Y., Li J., Peterson F.C., Jensen D.R., Yong E.-L., Volkman B.F.,
RA Cutler S.R., Zhu J.-K., Xu H.E.;
RT "A gate-latch-lock mechanism for hormone signalling by abscisic acid
RT receptors.";
RL Nature 462:602-608(2009).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 172-511 IN COMPLEX WITH
RP MAGNESIUM, AND INTERACTION WITH PYL10.
RX PubMed=21658606; DOI=10.1016/j.molcel.2011.05.011;
RA Hao Q., Yin P., Li W., Wang L., Yan C., Lin Z., Wu J.Z., Wang J., Yan S.F.,
RA Yan N.;
RT "The molecular basis of ABA-independent inhibition of PP2Cs by a subclass
RT of PYL proteins.";
RL Mol. Cell 42:662-672(2011).
CC -!- FUNCTION: Key component and repressor of the abscisic acid (ABA)
CC signaling pathway that regulates numerous ABA responses, such as
CC stomatal closure, seed germination and inhibition of vegetative growth.
CC Confers enhanced sensitivity to drought. {ECO:0000269|PubMed:14731256,
CC ECO:0000269|PubMed:16798945, ECO:0000269|PubMed:16876791,
CC ECO:0000269|PubMed:19033529}.
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;
CC Evidence={ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Repressed by PYR/PYL/RCAR ABA receptors in an ABA-
CC dependent manner. {ECO:0000269|PubMed:19407142}.
CC -!- SUBUNIT: Interacts with SWI3B (via N-terminus). Interacts with ABA-
CC bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL8 and PYL9, and
CC with free PYL2, PYL3, PYL4, PYL10 and PYL13.
CC {ECO:0000269|PubMed:19033529, ECO:0000269|PubMed:19407142,
CC ECO:0000269|PubMed:19407143, ECO:0000269|PubMed:19624469,
CC ECO:0000269|PubMed:19898420, ECO:0000269|PubMed:21658606,
CC ECO:0000269|PubMed:24165892}.
CC -!- INTERACTION:
CC Q9CAJ0; Q8VZS8: PYL1; NbExp=7; IntAct=EBI-2309302, EBI-2363104;
CC Q9CAJ0; Q8H1R0: PYL10; NbExp=4; IntAct=EBI-2309302, EBI-2363213;
CC Q9CAJ0; Q9FJ50: PYL11; NbExp=4; IntAct=EBI-2309302, EBI-2363233;
CC Q9CAJ0; Q9FJ49: PYL12; NbExp=4; IntAct=EBI-2309302, EBI-2363244;
CC Q9CAJ0; O80992: PYL2; NbExp=10; IntAct=EBI-2309302, EBI-2363125;
CC Q9CAJ0; Q9SSM7: PYL3; NbExp=10; IntAct=EBI-2309302, EBI-2363144;
CC Q9CAJ0; O80920: PYL4; NbExp=8; IntAct=EBI-2309302, EBI-2349683;
CC Q9CAJ0; Q9FLB1: PYL5; NbExp=11; IntAct=EBI-2309302, EBI-2363181;
CC Q9CAJ0; Q8S8E3: PYL6; NbExp=9; IntAct=EBI-2309302, EBI-2363192;
CC Q9CAJ0; Q1ECF1: PYL7; NbExp=4; IntAct=EBI-2309302, EBI-2363203;
CC Q9CAJ0; Q9FGM1: PYL8; NbExp=7; IntAct=EBI-2309302, EBI-2429535;
CC Q9CAJ0; Q84MC7: PYL9; NbExp=5; IntAct=EBI-2309302, EBI-2349513;
CC Q9CAJ0; O49686: PYR1; NbExp=17; IntAct=EBI-2309302, EBI-2349590;
CC Q9CAJ0; Q39192: SRK2D; NbExp=2; IntAct=EBI-2309302, EBI-2363308;
CC Q9CAJ0; Q940H6: SRK2E; NbExp=5; IntAct=EBI-2309302, EBI-782514;
CC Q9CAJ0; Q39193: SRK2I; NbExp=2; IntAct=EBI-2309302, EBI-2620383;
CC Q9CAJ0; Q84JG2: SWI3B; NbExp=4; IntAct=EBI-2309302, EBI-1102271;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19033529}. Nucleus
CC {ECO:0000269|PubMed:19033529}. Note=Mainly cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CAJ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CAJ0-2; Sequence=VSP_034844, VSP_034845;
CC -!- TISSUE SPECIFICITY: Expressed in seeds, roots, stems, leaves and
CC flowers, especially in meristematic tissues, guard cells, embryo and
CC siliques. {ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16339800,
CC ECO:0000269|PubMed:9862504}.
CC -!- INDUCTION: Repressed by MYB44. Induced by ABA.
CC {ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16339800,
CC ECO:0000269|PubMed:18162593, ECO:0000269|PubMed:9862504}.
CC -!- DOMAIN: The 'lock' site stabilizes the complex made of PP2C, ABA and
CC PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in
CC closed positions.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH56780.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ003119; CAA05875.1; -; Genomic_DNA.
DR EMBL; AC010926; AAG51849.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35370.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35371.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35372.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58361.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58362.1; -; Genomic_DNA.
DR EMBL; BT015409; AAU05532.1; -; mRNA.
DR EMBL; AK230171; BAF01980.1; -; mRNA.
DR EMBL; AK318665; BAH56780.1; ALT_INIT; mRNA.
DR PIR; F96752; F96752.
DR RefSeq; NP_001077815.1; NM_001084346.3. [Q9CAJ0-2]
DR RefSeq; NP_001185385.1; NM_001198456.1. [Q9CAJ0-1]
DR RefSeq; NP_001320804.1; NM_001334550.1. [Q9CAJ0-1]
DR RefSeq; NP_001320805.1; NM_001334551.1. [Q9CAJ0-2]
DR RefSeq; NP_177421.1; NM_105936.4. [Q9CAJ0-1]
DR PDB; 3KB3; X-ray; 1.95 A; B=186-506.
DR PDB; 3NMT; X-ray; 2.56 A; B=172-511.
DR PDB; 3QN1; X-ray; 1.80 A; B=178-511.
DR PDB; 3RT0; X-ray; 2.11 A; A/B=172-511.
DR PDB; 3UJG; X-ray; 2.60 A; B=172-511.
DR PDB; 3ZVU; X-ray; 2.10 A; B=178-511.
DR PDB; 4DS8; X-ray; 2.21 A; B=169-511.
DR PDB; 4LA7; X-ray; 1.98 A; B=178-505.
DR PDB; 4LG5; X-ray; 2.88 A; B=172-511.
DR PDB; 4LGA; X-ray; 2.70 A; B=172-511.
DR PDB; 4LGB; X-ray; 3.15 A; B=172-511.
DR PDB; 4WVO; X-ray; 2.25 A; B=178-505.
DR PDB; 5JO1; X-ray; 2.30 A; B=172-506.
DR PDB; 5JO2; X-ray; 2.42 A; B=172-506.
DR PDB; 5MN0; X-ray; 2.00 A; B=179-511.
DR PDB; 5OR2; X-ray; 2.50 A; B=178-511.
DR PDB; 5OR6; X-ray; 2.40 A; B=178-511.
DR PDB; 5VR7; X-ray; 2.61 A; B=172-511.
DR PDB; 5VRO; X-ray; 2.26 A; B=172-511.
DR PDB; 5VS5; X-ray; 2.80 A; B=172-511.
DR PDB; 5VSQ; X-ray; 2.62 A; B=172-511.
DR PDB; 5VSR; X-ray; 2.62 A; B=172-511.
DR PDB; 5VT7; X-ray; 2.62 A; B=172-511.
DR PDB; 6ZUC; X-ray; 2.37 A; B=179-505.
DR PDBsum; 3KB3; -.
DR PDBsum; 3NMT; -.
DR PDBsum; 3QN1; -.
DR PDBsum; 3RT0; -.
DR PDBsum; 3UJG; -.
DR PDBsum; 3ZVU; -.
DR PDBsum; 4DS8; -.
DR PDBsum; 4LA7; -.
DR PDBsum; 4LG5; -.
DR PDBsum; 4LGA; -.
DR PDBsum; 4LGB; -.
DR PDBsum; 4WVO; -.
DR PDBsum; 5JO1; -.
DR PDBsum; 5JO2; -.
DR PDBsum; 5MN0; -.
DR PDBsum; 5OR2; -.
DR PDBsum; 5OR6; -.
DR PDBsum; 5VR7; -.
DR PDBsum; 5VRO; -.
DR PDBsum; 5VS5; -.
DR PDBsum; 5VSQ; -.
DR PDBsum; 5VSR; -.
DR PDBsum; 5VT7; -.
DR PDBsum; 6ZUC; -.
DR AlphaFoldDB; Q9CAJ0; -.
DR SMR; Q9CAJ0; -.
DR BioGRID; 28828; 25.
DR DIP; DIP-48988N; -.
DR IntAct; Q9CAJ0; 22.
DR MINT; Q9CAJ0; -.
DR STRING; 3702.AT1G72770.1; -.
DR BindingDB; Q9CAJ0; -.
DR PaxDb; Q9CAJ0; -.
DR PRIDE; Q9CAJ0; -.
DR ProteomicsDB; 248872; -. [Q9CAJ0-1]
DR EnsemblPlants; AT1G72770.1; AT1G72770.1; AT1G72770. [Q9CAJ0-1]
DR EnsemblPlants; AT1G72770.2; AT1G72770.2; AT1G72770. [Q9CAJ0-2]
DR EnsemblPlants; AT1G72770.3; AT1G72770.3; AT1G72770. [Q9CAJ0-1]
DR EnsemblPlants; AT1G72770.4; AT1G72770.4; AT1G72770. [Q9CAJ0-1]
DR EnsemblPlants; AT1G72770.5; AT1G72770.5; AT1G72770. [Q9CAJ0-2]
DR GeneID; 843609; -.
DR Gramene; AT1G72770.1; AT1G72770.1; AT1G72770. [Q9CAJ0-1]
DR Gramene; AT1G72770.2; AT1G72770.2; AT1G72770. [Q9CAJ0-2]
DR Gramene; AT1G72770.3; AT1G72770.3; AT1G72770. [Q9CAJ0-1]
DR Gramene; AT1G72770.4; AT1G72770.4; AT1G72770. [Q9CAJ0-1]
DR Gramene; AT1G72770.5; AT1G72770.5; AT1G72770. [Q9CAJ0-2]
DR KEGG; ath:AT1G72770; -.
DR Araport; AT1G72770; -.
DR TAIR; locus:2030230; AT1G72770.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_5_1; -.
DR InParanoid; Q9CAJ0; -.
DR OMA; QEVCEIA; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9CAJ0; -.
DR EvolutionaryTrace; Q9CAJ0; -.
DR PRO; PR:Q9CAJ0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAJ0; baseline and differential.
DR Genevisible; Q9CAJ0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004722; F:protein serine/threonine phosphatase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Alternative splicing;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..511
FT /note="Protein phosphatase 2C 16"
FT /id="PRO_0000344524"
FT DOMAIN 189..501
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19898420,
FT ECO:0007744|PDB:3KB3"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21658606,
FT ECO:0007744|PDB:3NMT, ECO:0007744|PDB:3QN1,
FT ECO:0007744|PDB:3RT0, ECO:0007744|PDB:3UJG,
FT ECO:0007744|PDB:3ZVU, ECO:0007744|PDB:4LA7,
FT ECO:0007744|PDB:4LG5, ECO:0007744|PDB:4LGA,
FT ECO:0007744|PDB:4WVO"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19898420,
FT ECO:0007744|PDB:3KB3"
FT BINDING 432
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21658606,
FT ECO:0007744|PDB:3NMT, ECO:0007744|PDB:3QN1,
FT ECO:0007744|PDB:3RT0, ECO:0007744|PDB:3UJG,
FT ECO:0007744|PDB:3ZVU, ECO:0007744|PDB:4LA7,
FT ECO:0007744|PDB:4LG5, ECO:0007744|PDB:4LGA,
FT ECO:0007744|PDB:4WVO"
FT BINDING 492
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21658606,
FT ECO:0007744|PDB:3NMT, ECO:0007744|PDB:3QN1,
FT ECO:0007744|PDB:3RT0, ECO:0007744|PDB:3UJG,
FT ECO:0007744|PDB:3ZVU, ECO:0007744|PDB:4LA7,
FT ECO:0007744|PDB:4LG5, ECO:0007744|PDB:4LGA,
FT ECO:0007744|PDB:4WVO"
FT SITE 385
FT /note="Lock"
FT VAR_SEQ 402..406
FT /note="DRYLK -> KHCFF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_034844"
FT VAR_SEQ 407..511
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_034845"
FT MUTAGEN 246
FT /note="G->D: Reduced phosphatase activity, impaired
FT affinity for PYR/PYL/RCAR receptors, and insensitivity to
FT ABA."
FT /evidence="ECO:0000269|PubMed:16876791,
FT ECO:0000269|PubMed:19033529, ECO:0000269|PubMed:19624469"
FT CONFLICT 46
FT /note="Q -> P (in Ref. 1; CAA05875)"
FT /evidence="ECO:0000305"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3RT0"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 204..216
FT /evidence="ECO:0007829|PDB:3QN1"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 233..248
FT /evidence="ECO:0007829|PDB:3QN1"
FT HELIX 249..268
FT /evidence="ECO:0007829|PDB:3QN1"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:4LA7"
FT HELIX 284..302
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:5VRO"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5VRO"
FT HELIX 314..322
FT /evidence="ECO:0007829|PDB:5VSR"
FT STRAND 329..334
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 336..346
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:3QN1"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:3QN1"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:3QN1"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:3QN1"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:3QN1"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:3QN1"
FT HELIX 440..458
FT /evidence="ECO:0007829|PDB:3QN1"
FT TURN 463..468
FT /evidence="ECO:0007829|PDB:3KB3"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:3QN1"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:3QN1"
SQ SEQUENCE 511 AA; 55744 MW; B001BAF0DD8333E1 CRC64;
MEEMTPAVAM TLSLAANTMC ESSPVEITQL KNVTDAADLL SDSENQSFCN GGTECTMEDV
SELEEVGEQD LLKTLSDTRS GSSNVFDEDD VLSVVEDNSA VISEGLLVVD AGSELSLSNT
AMEIDNGRVL ATAIIVGESS IEQVPTAEVL IAGVNQDTNT SEVVIRLPDE NSNHLVKGRS
VYELDCIPLW GTVSIQGNRS EMEDAFAVSP HFLKLPIKML MGDHEGMSPS LTHLTGHFFG
VYDGHGGHKV ADYCRDRLHF ALAEEIERIK DELCKRNTGE GRQVQWDKVF TSCFLTVDGE
IEGKIGRAVV GSSDKVLEAV ASETVGSTAV VALVCSSHIV VSNCGDSRAV LFRGKEAMPL
SVDHKPDRED EYARIENAGG KVIQWQGARV FGVLAMSRSI GDRYLKPYVI PEPEVTFMPR
SREDECLILA SDGLWDVMNN QEVCEIARRR ILMWHKKNGA PPLAERGKGI DPACQAAADY
LSMLALQKGS KDNISIIVID LKAQRKFKTR T
