P2C07_ARATH
ID P2C07_ARATH Reviewed; 511 AA.
AC Q9LNP9; Q8GWS8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein phosphatase 2C 7;
DE Short=AtPP2C07;
DE EC=3.1.3.16;
DE AltName: Full=Protein HYPERSENSITIVE TO ABA 2;
DE AltName: Full=Protein phosphatase 2C HAB2;
DE Short=PP2C HAB2;
DE Flags: Precursor;
GN Name=HAB2; OrderedLocusNames=At1g17550; ORFNames=F1L3.32;
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP 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 [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 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 [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 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 [9]
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).
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 {ECO:0000250}.
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 -!- SUBUNIT: Interacts with PYL13. {ECO:0000269|PubMed:24165892}.
CC -!- INTERACTION:
CC Q9LNP9; Q8H1R0: PYL10; NbExp=3; IntAct=EBI-15803614, EBI-2363213;
CC Q9LNP9; Q9FLB1: PYL5; NbExp=5; IntAct=EBI-15803614, EBI-2363181;
CC Q9LNP9; Q8S8E3: PYL6; NbExp=5; IntAct=EBI-15803614, EBI-2363192;
CC Q9LNP9; Q1ECF1: PYL7; NbExp=3; IntAct=EBI-15803614, EBI-2363203;
CC Q9LNP9; Q9FGM1: PYL8; NbExp=5; IntAct=EBI-15803614, EBI-2429535;
CC Q9LNP9; Q84MC7: PYL9; NbExp=3; IntAct=EBI-15803614, EBI-2349513;
CC -!- TISSUE SPECIFICITY: Expressed in seeds. {ECO:0000269|PubMed:16339800}.
CC -!- INDUCTION: Repressed by MYB44. Induced by ABA.
CC {ECO:0000269|PubMed:14731256, ECO:0000269|PubMed:16339800,
CC ECO:0000269|PubMed:18162593}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79469.1; Type=Erroneous gene model prediction; 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; AC022492; AAF79469.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29605.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60722.1; -; Genomic_DNA.
DR EMBL; AK118656; BAC43252.1; -; mRNA.
DR RefSeq; NP_001322988.1; NM_001332312.1.
DR RefSeq; NP_173199.2; NM_101618.3.
DR AlphaFoldDB; Q9LNP9; -.
DR SMR; Q9LNP9; -.
DR BioGRID; 23570; 7.
DR DIP; DIP-48989N; -.
DR IntAct; Q9LNP9; 10.
DR STRING; 3702.AT1G17550.1; -.
DR PaxDb; Q9LNP9; -.
DR PRIDE; Q9LNP9; -.
DR ProteomicsDB; 248870; -.
DR EnsemblPlants; AT1G17550.1; AT1G17550.1; AT1G17550.
DR EnsemblPlants; AT1G17550.2; AT1G17550.2; AT1G17550.
DR GeneID; 838330; -.
DR Gramene; AT1G17550.1; AT1G17550.1; AT1G17550.
DR Gramene; AT1G17550.2; AT1G17550.2; AT1G17550.
DR KEGG; ath:AT1G17550; -.
DR Araport; AT1G17550; -.
DR TAIR; locus:2007943; AT1G17550.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_5_1; -.
DR InParanoid; Q9LNP9; -.
DR OMA; TISICGG; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9LNP9; -.
DR PRO; PR:Q9LNP9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNP9; baseline and differential.
DR Genevisible; Q9LNP9; AT.
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; IBA:GO_Central.
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 Abscisic acid signaling pathway; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Protein phosphatase; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..511
FT /note="Protein phosphatase 2C 7"
FT /id="PRO_0000344525"
FT DOMAIN 188..501
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 432
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 475
FT /note="Q -> R (in Ref. 3; BAC43252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56062 MW; 167CB9D9D5FF9A59 CRC64;
MEEISPAVAL TLGLANTMCD SGISSTFDIS ELENVTDAAD MLCNQKRQRY SNGVVDCIMG
SVSEEKTLSE VRSLSSDFSV TVQESEEDEP LVSDATIISE GLIVVDARSE ISLPDTVETD
NGRVLATAII LNETTIEQVP TAEVLIASLN HDVNMEVATS EVVIRLPEEN PNVARGSRSV
YELECIPLWG TISICGGRSE MEDAVRALPH FLKIPIKMLM GDHEGMSPSL PYLTSHFFGV
YDGHGGAQVA DYCHDRIHSA LAEEIERIKE ELCRRNTGEG RQVQWEKVFV DCYLKVDDEV
KGKINRPVVG SSDRMVLEAV SPETVGSTAV VALVCSSHII VSNCGDSRAV LLRGKDSMPL
SVDHKPDRED EYARIEKAGG KVIQWQGARV SGVLAMSRSI GDQYLEPFVI PDPEVTFMPR
AREDECLILA SDGLWDVMSN QEACDFARRR ILAWHKKNGA LPLAERGVGE DQACQAAAEY
LSKLAIQMGS KDNISIIVID LKAQRKFKTR S
