P2C78_ARATH
ID P2C78_ARATH Reviewed; 413 AA.
AC Q9FIF5; Q944I7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable protein phosphatase 2C 78;
DE Short=AtPP2C78;
DE EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU01082};
DE AltName: Full=Protein HIGHLY ABA-INDUCED 1 {ECO:0000303|PubMed:22198272};
DE AltName: Full=Protein SENESCENCE-ASSOCIATED GENE 113 {ECO:0000303|PubMed:22007837};
GN Name=SAG113 {ECO:0000303|PubMed:22007837};
GN Synonyms=HAI1 {ECO:0000303|PubMed:22198272}; OrderedLocusNames=At5g59220;
GN ORFNames=MNC17.110;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(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, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22007837; DOI=10.1111/j.1365-313x.2011.04821.x;
RA Zhang K., Xia X., Zhang Y., Gan S.S.;
RT "An ABA-regulated and Golgi-localized protein phosphatase controls water
RT loss during leaf senescence in Arabidopsis.";
RL Plant J. 69:667-678(2012).
RN [6]
RP FUNCTION.
RX PubMed=22184656; DOI=10.1104/pp.111.190876;
RA Zhang K., Gan S.S.;
RT "An abscisic acid-AtNAP transcription factor-SAG113 protein phosphatase 2C
RT regulatory chain for controlling dehydration in senescing Arabidopsis
RT leaves.";
RL Plant Physiol. 158:961-969(2012).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=22198272; DOI=10.1104/pp.111.188623;
RA Antoni R., Gonzalez-Guzman M., Rodriguez L., Rodrigues A., Pizzio G.A.,
RA Rodriguez P.L.;
RT "Selective inhibition of clade A phosphatases type 2C by PYR/PYL/RCAR
RT abscisic acid receptors.";
RL Plant Physiol. 158:970-980(2012).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22829320; DOI=10.1104/pp.112.202408;
RA Bhaskara G.B., Nguyen T.T., Verslues P.E.;
RT "Unique drought resistance functions of the highly ABA-induced clade A
RT protein phosphatase 2Cs.";
RL Plant Physiol. 160:379-395(2012).
CC -!- FUNCTION: Acts as negative regulator of abscisic acid (ABA) signaling
CC for stomatal closure in leaves, and controls water loss during leaf
CC senescence (PubMed:22007837, PubMed:22184656). Activated by the
CC NAC029/NAP transcription factor during ABA signaling in senescing
CC leaves (PubMed:22184656). Functions as negative regulator of osmotic
CC stress and ABA signaling (PubMed:22198272). Acts as negative regulator
CC of response to drought (PubMed:22829320). {ECO:0000269|PubMed:22007837,
CC ECO:0000269|PubMed:22184656, ECO:0000269|PubMed:22198272,
CC ECO:0000269|PubMed:22829320}.
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:0000255|PROSITE-
CC ProRule:PRU01082};
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:0000255|PROSITE-
CC ProRule:PRU01082};
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 -!- INTERACTION:
CC Q9FIF5; Q9SJ60: At2g35900; NbExp=3; IntAct=EBI-2363373, EBI-4456633;
CC Q9FIF5; Q8H1R0: PYL10; NbExp=3; IntAct=EBI-2363373, EBI-2363213;
CC Q9FIF5; Q9FGM1: PYL8; NbExp=5; IntAct=EBI-2363373, EBI-2429535;
CC Q9FIF5; Q9LJ97: RAB28; NbExp=3; IntAct=EBI-2363373, EBI-25520978;
CC Q9FIF5; Q93ZY2: ROPGEF1; NbExp=2; IntAct=EBI-2363373, EBI-4425188;
CC Q9FIF5; Q940H6: SRK2E; NbExp=2; IntAct=EBI-2363373, EBI-782514;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:22007837}.
CC Nucleus {ECO:0000269|PubMed:22198272, ECO:0000269|PubMed:22829320}.
CC -!- INDUCTION: By abscisic acid (ABA) (PubMed:22007837, PubMed:22198272).
CC Induced during leaf senescence (PubMed:22007837). Induced by osmotic
CC stress (PubMed:22198272). {ECO:0000269|PubMed:22007837,
CC ECO:0000269|PubMed:22198272}.
CC -!- DISRUPTION PHENOTYPE: Delayed senescence. Increased sensitivity to
CC abscisic acid (ABA). {ECO:0000269|PubMed:22007837}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AB016890; BAB09767.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97159.1; -; Genomic_DNA.
DR EMBL; AF428395; AAL16163.1; -; mRNA.
DR EMBL; AY054163; AAL06824.1; -; mRNA.
DR EMBL; AY074555; AAL67095.1; -; mRNA.
DR RefSeq; NP_200730.1; NM_125312.3.
DR AlphaFoldDB; Q9FIF5; -.
DR SMR; Q9FIF5; -.
DR BioGRID; 21284; 38.
DR DIP; DIP-48992N; -.
DR IntAct; Q9FIF5; 12.
DR STRING; 3702.AT5G59220.1; -.
DR PaxDb; Q9FIF5; -.
DR PRIDE; Q9FIF5; -.
DR ProteomicsDB; 250920; -.
DR EnsemblPlants; AT5G59220.1; AT5G59220.1; AT5G59220.
DR GeneID; 836040; -.
DR Gramene; AT5G59220.1; AT5G59220.1; AT5G59220.
DR KEGG; ath:AT5G59220; -.
DR Araport; AT5G59220; -.
DR TAIR; locus:2168449; AT5G59220.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_0_1; -.
DR InParanoid; Q9FIF5; -.
DR OMA; CYENESV; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9FIF5; -.
DR BRENDA; 3.1.3.16; 399.
DR PRO; PR:Q9FIF5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIF5; baseline and differential.
DR Genevisible; Q9FIF5; AT.
DR GO; GO:0033106; C:cis-Golgi network membrane; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; 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:0004722; F:protein serine/threonine phosphatase activity; IGI:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IGI:TAIR.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..413
FT /note="Probable protein phosphatase 2C 78"
FT /id="PRO_0000367997"
FT DOMAIN 111..409
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 21..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 103
FT /note="L -> F (in Ref. 3; AAL16163)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 413 AA; 45538 MW; 649CF986D17A92D7 CRC64;
MAEICYENET MMIETTATVV KKATTTTRRR ERSSSQAARR RRMEIRRFKF VSGEQEPVFV
DGDLQRRRRR ESTVAASTST VFYETAKEVV VLCESLSSTV VALPDPEAYP KYGVASVCGR
RREMEDAVAV HPFFSRHQTE YSSTGFHYCG VYDGHGCSHV AMKCRERLHE LVREEFEADA
DWEKSMARSF TRMDMEVVAL NADGAAKCRC ELQRPDCDAV GSTAVVSVLT PEKIIVANCG
DSRAVLCRNG KAIALSSDHK PDRPDELDRI QAAGGRVIYW DGPRVLGVLA MSRAIGDNYL
KPYVISRPEV TVTDRANGDD FLILASDGLW DVVSNETACS VVRMCLRGKV NGQVSSSPER
EMTGVGAGNV VVGGGDLPDK ACEEASLLLT RLALARQSSD NVSVVVVDLR RDT
