P2C03_ARATH
ID P2C03_ARATH Reviewed; 442 AA.
AC Q9LNW3; Q8LFK5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein phosphatase 2C 3 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C03 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000305};
DE AltName: Full=Protein AKT1-INTERACTING 1 {ECO:0000303|PubMed:17898163};
DE AltName: Full=Protein HIGHLY ABA-INDUCED PP2C 2 {ECO:0000303|PubMed:19880399};
DE AltName: Full=Protein HONSU {ECO:0000303|PubMed:23378449};
DE AltName: Full=Protein phosphatase 2C AIP1 {ECO:0000303|PubMed:17898163};
DE Short=PP2C AIP1 {ECO:0000303|PubMed:17898163};
GN Name=AIP1 {ECO:0000303|PubMed:17898163};
GN Synonyms=HAI2 {ECO:0000303|PubMed:19880399},
GN HON {ECO:0000303|PubMed:23378449};
GN OrderedLocusNames=At1g07430 {ECO:0000312|Araport:AT1G07430};
GN ORFNames=F22G5.22 {ECO:0000312|EMBL:AAF79555.1};
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=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 [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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH AKT1 AND CIPK23, AND SUBCELLULAR LOCATION.
RX PubMed=17898163; DOI=10.1073/pnas.0707912104;
RA Lee S.-C., Lan W.-Z., Kim B.-G., Li L., Cheong Y.H., Pandey G.K., Lu G.,
RA Buchanan B.B., Luan S.;
RT "A protein phosphorylation/dephosphorylation network regulates a plant
RT potassium channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15959-15964(2007).
RN [7]
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 [8]
RP INDUCTION BY ABSCISIC ACID.
RX PubMed=19880399; DOI=10.1093/pcp/pcp147;
RA Fujita Y., Nakashima K., Yoshida T., Katagiri T., Kidokoro S., Kanamori N.,
RA Umezawa T., Fujita M., Maruyama K., Ishiyama K., Kobayashi M., Nakasone S.,
RA Yamada K., Ito T., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Three SnRK2 protein kinases are the main positive regulators of abscisic
RT acid signaling in response to water stress in Arabidopsis.";
RL Plant Cell Physiol. 50:2123-2132(2009).
RN [9]
RP FUNCTION, INTERACTION WITH PYL8/RCAR3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22404835; DOI=10.1016/j.plantsci.2012.01.013;
RA Lim C.W., Kim J.H., Baek W., Kim B.S., Lee S.C.;
RT "Functional roles of the protein phosphatase 2C, AtAIP1, in abscisic acid
RT signaling and sugar tolerance in Arabidopsis.";
RL Plant Sci. 187:83-88(2012).
RN [10]
RP FUNCTION, INTERACTION WITH PYR1/RCAR11, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=23378449; DOI=10.1093/pcp/pct017;
RA Kim W., Lee Y., Park J., Lee N., Choi G.;
RT "HONSU, a protein phosphatase 2C, regulates seed dormancy by inhibiting ABA
RT signaling in Arabidopsis.";
RL Plant Cell Physiol. 54:555-572(2013).
CC -!- FUNCTION: Involved in the negative regulation of the K(+) potassium
CC channel AKT1 by its dephosphorylation, antagonistically to CIPK
CC proteins (e.g. CIPK23) (PubMed:17898163). Functions as positive
CC regulator of abscisic acid-mediated cell signaling during seedling
CC growth (PubMed:22404835). Involved in the regulation of seed dormancy
CC (PubMed:23378449). Acts as negative regulator of seed dormancy by
CC inhibiting abscisic signaling and subsequently activating gibberellic
CC acid signaling (PubMed:23378449). {ECO:0000269|PubMed:17898163,
CC ECO:0000269|PubMed:22404835, ECO:0000269|PubMed:23378449}.
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; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- SUBUNIT: Part of a K(+)-channel calcium-sensing kinase/phosphatase
CC complex composed by a calcium sensor CBL (CBL1, CBL2, CBL3 or CBL9), a
CC kinase CIPK (CIPK6, CIPK16 or CIPK23), a phosphatase PP2C (AIP1) and a
CC K(+)-channel (AKT1) (PubMed:17898163). Interacts with AKT1 and CIPK23
CC (PubMed:17898163). Interacts with PYL8/RCAR3 in an abscisic acid-
CC independent (PubMed:22404835). Interacts with PYR1/RCAR11 in an
CC abscisic acid-dependent manner (PubMed:23378449).
CC {ECO:0000269|PubMed:17898163, ECO:0000269|PubMed:22404835,
CC ECO:0000269|PubMed:23378449}.
CC -!- INTERACTION:
CC Q9LNW3; C0SUW7: ARID6; NbExp=3; IntAct=EBI-1573499, EBI-15192335;
CC Q9LNW3; A0A1I9LTW1: At3g54390; NbExp=3; IntAct=EBI-1573499, EBI-15191983;
CC Q9LNW3; Q1PF16: BHLH19; NbExp=3; IntAct=EBI-1573499, EBI-2367867;
CC Q9LNW3; A0SVK0: DOG1; NbExp=5; IntAct=EBI-1573499, EBI-25512274;
CC Q9LNW3; O23160: MYB73; NbExp=3; IntAct=EBI-1573499, EBI-25506855;
CC Q9LNW3; B3H506: NAC061; NbExp=3; IntAct=EBI-1573499, EBI-15195677;
CC Q9LNW3; Q8H1R0: PYL10; NbExp=3; IntAct=EBI-1573499, EBI-2363213;
CC Q9LNW3; Q9FJ50: PYL11; NbExp=3; IntAct=EBI-1573499, EBI-2363233;
CC Q9LNW3; Q9FJ49: PYL12; NbExp=3; IntAct=EBI-1573499, EBI-2363244;
CC Q9LNW3; Q9SN51: PYL13; NbExp=7; IntAct=EBI-1573499, EBI-25515027;
CC Q9LNW3; O80992: PYL2; NbExp=3; IntAct=EBI-1573499, EBI-2363125;
CC Q9LNW3; Q9SSM7: PYL3; NbExp=3; IntAct=EBI-1573499, EBI-2363144;
CC Q9LNW3; O80920: PYL4; NbExp=3; IntAct=EBI-1573499, EBI-2349683;
CC Q9LNW3; Q9FLB1: PYL5; NbExp=3; IntAct=EBI-1573499, EBI-2363181;
CC Q9LNW3; Q8S8E3: PYL6; NbExp=3; IntAct=EBI-1573499, EBI-2363192;
CC Q9LNW3; Q1ECF1: PYL7; NbExp=7; IntAct=EBI-1573499, EBI-2363203;
CC Q9LNW3; Q9FGM1: PYL8; NbExp=9; IntAct=EBI-1573499, EBI-2429535;
CC Q9LNW3; Q84MC7: PYL9; NbExp=9; IntAct=EBI-1573499, EBI-2349513;
CC Q9LNW3; O49686: PYR1; NbExp=3; IntAct=EBI-1573499, EBI-2349590;
CC Q9LNW3; Q9FMX2: TCP7; NbExp=4; IntAct=EBI-1573499, EBI-15192677;
CC Q9LNW3; Q8GY55: TIFY4B; NbExp=3; IntAct=EBI-1573499, EBI-15206004;
CC Q9LNW3; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-1573499, EBI-15193683;
CC Q9LNW3; Q9SK33: WRKY60; NbExp=3; IntAct=EBI-1573499, EBI-2112777;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17898163}.
CC Cytoplasm {ECO:0000269|PubMed:22404835}. Nucleus
CC {ECO:0000269|PubMed:22404835}. Note=Probably associated to the plasma
CC membrane when interacting with AKT1 and CIPK23 (Probable). Localizes to
CC nucleus when interacting with PYL8/RCAR3 (PubMed:22404835).
CC {ECO:0000269|PubMed:22404835, ECO:0000305|PubMed:17898163}.
CC -!- TISSUE SPECIFICITY: Expressed in shoot meristem, vascular tissues of
CC cotyledons, and in primary roots surrounding the root meristem
CC (PubMed:22404835). Highly expressed in seeds (PubMed:23378449).
CC {ECO:0000269|PubMed:22404835, ECO:0000269|PubMed:23378449}.
CC -!- INDUCTION: Induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:19880399}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit reduced sensitivity to abscisic
CC acid (ABA) and glucose during seed germination and seedling stage
CC (PubMed:22404835). Freshly harvested seeds of mutant plants exhibit
CC increased seed dormancy (PubMed:23378449).
CC {ECO:0000269|PubMed:22404835, ECO:0000269|PubMed:23378449}.
CC -!- MISCELLANEOUS: Honsu means abnormal drowsiness in Korean.
CC {ECO:0000305|PubMed:23378449}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC022464; AAF79555.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28124.1; -; Genomic_DNA.
DR EMBL; AY070089; AAL49783.1; -; mRNA.
DR EMBL; AY091341; AAM14280.1; -; mRNA.
DR EMBL; AY084794; AAM61361.1; -; mRNA.
DR PIR; B86209; B86209.
DR RefSeq; NP_172223.1; NM_100617.3.
DR AlphaFoldDB; Q9LNW3; -.
DR SMR; Q9LNW3; -.
DR BioGRID; 22496; 28.
DR DIP; DIP-40200N; -.
DR IntAct; Q9LNW3; 28.
DR STRING; 3702.AT1G07430.1; -.
DR iPTMnet; Q9LNW3; -.
DR PaxDb; Q9LNW3; -.
DR PRIDE; Q9LNW3; -.
DR ProteomicsDB; 248698; -.
DR EnsemblPlants; AT1G07430.1; AT1G07430.1; AT1G07430.
DR GeneID; 837255; -.
DR Gramene; AT1G07430.1; AT1G07430.1; AT1G07430.
DR KEGG; ath:AT1G07430; -.
DR Araport; AT1G07430; -.
DR TAIR; locus:2025087; AT1G07430.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_0_1; -.
DR InParanoid; Q9LNW3; -.
DR OMA; MSANCKC; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9LNW3; -.
DR PRO; PR:Q9LNW3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNW3; baseline and differential.
DR Genevisible; Q9LNW3; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; 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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:1902039; P:negative regulation of seed dormancy process; IMP:TAIR.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0048838; P:release of seed from dormancy; IMP:TAIR.
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 Cell membrane; Cytoplasm; Growth regulation; Hydrolase; Magnesium;
KW Manganese; Membrane; Metal-binding; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..442
FT /note="Protein phosphatase 2C 3"
FT /id="PRO_0000344523"
FT DOMAIN 120..433
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 30..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT BINDING 162
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9CAJ0"
FT CONFLICT 253
FT /note="D -> G (in Ref. 4; AAM61361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49763 MW; 892DB70AB83312AD CRC64;
MADICYEDET SACESRPLWS SRKWRIGVQR FRMSPSEMNP TASTTEEEDK SEGIYNKRNK
QEEYDFMNCA SSSPSQSSPE EESVSLEDSD VSISDGNSSV NDVAVIPSKK TVKETDLRPR
YGVASVCGRR RDMEDAVALH PSFVRKQTEF SRTRWHYFGV YDGHGCSHVA ARCKERLHEL
VQEEALSDKK EEWKKMMERS FTRMDKEVVR WGETVMSANC RCELQTPDCD AVGSTAVVSV
ITPEKIIVAN CGDSRAVLCR NGKAVPLSTD HKPDRPDELD RIQEAGGRVI YWDGARVLGV
LAMSRAIGDN YLKPYVTSEP EVTVTDRTEE DEFLILATDG LWDVVTNEAA CTMVRMCLNR
KSGRGRRRGE TQTPGRRSEE EGKEEEEKVV GSRKNGKRGE ITDKACTEAS VLLTKLALAK
HSSDNVSVVV IDLRRRRKRH VA
