ID   P2C79_ARATH             Reviewed;         385 AA.
AC   Q9FKX4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Probable protein phosphatase 2C 79 {ECO:0000303|PubMed:19021904};
DE            Short=AtPP2C79 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
DE   Flags: Precursor;
GN   Name=PP2C79 {ECO:0000303|PubMed:19021904};
GN   Synonyms=PP2C-D7 {ECO:0000303|PubMed:24858935};
GN   OrderedLocusNames=At5g66080 {ECO:0000312|Araport:AT5G66080};
GN   ORFNames=K2A18.16 {ECO:0000312|EMBL:BAB10413.1};
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=9679202; DOI=10.1093/dnares/5.2.131;
RA   Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT   features of the regions of 1,381,565 bp covered by twenty one physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:131-145(1998).
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   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   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=24858935; DOI=10.1105/tpc.114.126037;
RA   Spartz A.K., Ren H., Park M.Y., Grandt K.N., Lee S.H., Murphy A.S.,
RA   Sussman M.R., Overvoorde P.J., Gray W.M.;
RT   "SAUR inhibition of PP2C-D phosphatases activates plasma membrane H+-
RT   ATPases to promote cell expansion in Arabidopsis.";
RL   Plant Cell 26:2129-2142(2014).
CC   -!- FUNCTION: May dephosphorylate and repress plasma membrane H(+)-ATPases
CC       (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively
CC       plant growth and fitness. {ECO:0000269|PubMed:24858935}.
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         Evidence={ECO:0000250|UniProtKB:Q9LHJ9};
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         Evidence={ECO:0000250|UniProtKB:Q9LHJ9};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P35813};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P35813};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:P35813};
CC   -!- DISRUPTION PHENOTYPE: Plants missing PP2C42/PP2C-D2, PP2C64/PP2C-D5,
CC       PP2C79/PP2C-D7, PP2C63/PP2C-D8 and PP2C68/PP2C-D9 exhibit an increased
CC       hypocotyl length, as well as an enhanced sensitivity to LiCl and media
CC       acidification. {ECO:0000269|PubMed:24858935}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {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; AB011474; BAB10413.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED98157.1; -; Genomic_DNA.
DR   EMBL; AY062587; AAL32665.1; -; mRNA.
DR   EMBL; BT001229; AAN65116.1; -; mRNA.
DR   RefSeq; NP_201409.1; NM_126006.4.
DR   AlphaFoldDB; Q9FKX4; -.
DR   SMR; Q9FKX4; -.
DR   BioGRID; 21982; 2.
DR   IntAct; Q9FKX4; 2.
DR   MINT; Q9FKX4; -.
DR   STRING; 3702.Q9FKX4; -.
DR   PaxDb; 3702-AT5G66080-1; -.
DR   EnsemblPlants; AT5G66080.1; AT5G66080.1; AT5G66080.
DR   GeneID; 836740; -.
DR   Gramene; AT5G66080.1; AT5G66080.1; AT5G66080.
DR   KEGG; ath:AT5G66080; -.
DR   Araport; AT5G66080; -.
DR   TAIR; AT5G66080; APD9.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_2_0_1; -.
DR   InParanoid; Q9FKX4; -.
DR   OMA; HPESCYV; -.
DR   OrthoDB; 1131727at2759; -.
DR   PhylomeDB; Q9FKX4; -.
DR   PRO; PR:Q9FKX4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FKX4; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:1900036; P:positive regulation of cellular response to heat; IMP:TAIR.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR47992:SF258; PROTEIN PHOSPHATASE 2C 46-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q9FKX4; AT.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW   Protein phosphatase; Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..385
FT                   /note="Probable protein phosphatase 2C 79"
FT                   /id="PRO_0000367998"
FT   DOMAIN          47..356
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         87
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         87
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         88
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         288
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   BINDING         347
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P35813"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LHJ9"
SQ   SEQUENCE   385 AA;  42963 MW;  C28A2ABB7F243B2D CRC64;
     MLSLFFNFLT SCLWPSSSTT SHTYSDSKGK QDGLLWYKDS AHHLFGDFSM AVVQANNLLE
     DQSQVESGPL TTLSSSGPYG TFVGVYDGHG GPETSRFVND HLFHHLKRFA AEQDSMSVDV
     IRKAYEATEE GFLGVVAKQW AVKPHIAAVG SCCLIGVVCD GKLYVANVGD SRAVLGKVIK
     ATGEVNALQL SAEHNVSIES VRQEMHSLHP DDSHIVVLKH NVWRVKGIIQ VSRSIGDVYL
     KKSEFNKEPL YTKYRLREPM KRPILSWEPS ITVHDLQPDD QFLIFASDGL WEQLSNQEAV
     EIVQNHPRNG IARRLVKAAL QEAAKKREMR YSDLNKIERG VRRHFHDDIT VVVLFLDTNL
     LSRASSLKTP SVSIRGGGIT LPKKL
//