P2C68_ARATH
ID P2C68_ARATH Reviewed; 393 AA.
AC Q84JD5; Q8LFQ7; Q9FG32;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable protein phosphatase 2C 68 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C68 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
GN Name=PP2C68 {ECO:0000303|PubMed:19021904};
GN Synonyms=PP2C-D9 {ECO:0000303|PubMed:24858935};
GN OrderedLocusNames=At5g06750 {ECO:0000312|Araport:AT5G06750};
GN ORFNames=MPH15.11 {ECO:0000312|EMBL:BAB09809.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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=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 [6]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q84JD5-1; Sequence=Displayed;
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 -!- SEQUENCE CAUTION:
CC Sequence=BAB09809.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP002032; BAB09809.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED91058.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91060.1; -; Genomic_DNA.
DR EMBL; BT004178; AAO42197.1; -; mRNA.
DR EMBL; BT005462; AAO63882.1; -; mRNA.
DR EMBL; AY084703; AAM61277.1; -; mRNA.
DR RefSeq; NP_001119181.1; NM_001125709.1. [Q84JD5-1]
DR RefSeq; NP_568174.1; NM_120758.4. [Q84JD5-1]
DR AlphaFoldDB; Q84JD5; -.
DR SMR; Q84JD5; -.
DR BioGRID; 15843; 1.
DR IntAct; Q84JD5; 1.
DR MINT; Q84JD5; -.
DR STRING; 3702.AT5G06750.3; -.
DR PaxDb; Q84JD5; -.
DR PRIDE; Q84JD5; -.
DR ProteomicsDB; 250911; -. [Q84JD5-1]
DR EnsemblPlants; AT5G06750.1; AT5G06750.1; AT5G06750. [Q84JD5-1]
DR EnsemblPlants; AT5G06750.3; AT5G06750.3; AT5G06750. [Q84JD5-1]
DR GeneID; 830564; -.
DR Gramene; AT5G06750.1; AT5G06750.1; AT5G06750. [Q84JD5-1]
DR Gramene; AT5G06750.3; AT5G06750.3; AT5G06750. [Q84JD5-1]
DR KEGG; ath:AT5G06750; -.
DR Araport; AT5G06750; -.
DR TAIR; locus:2170234; AT5G06750.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_2_0_1; -.
DR InParanoid; Q84JD5; -.
DR OMA; GRMNRDD; -.
DR PhylomeDB; Q84JD5; -.
DR PRO; PR:Q84JD5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84JD5; baseline and differential.
DR Genevisible; Q84JD5; AT.
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: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 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..393
FT /note="Probable protein phosphatase 2C 68"
FT /id="PRO_0000367989"
FT DOMAIN 56..359
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 291
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 350
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT CONFLICT 268
FT /note="L -> S (in Ref. 4; AAM61277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 44140 MW; CAB959A38511D7B8 CRC64;
MFSWLARMAL FCLRPMRRYG RMNRDDDDDD DHDGDSSSSG DSLLWSRELE RHSFGDFSIA
VVQANEVIED HSQVETGNGA VFVGVYDGHG GPEASRYISD HLFSHLMRVS RERSCISEEA
LRAAFSATEE GFLTLVRRTC GLKPLIAAVG SCCLVGVIWK GTLLIANVGD SRAVLGSMGS
NNNRSNKIVA EQLTSDHNAA LEEVRQELRS LHPDDSHIVV LKHGVWRIKG IIQVSRSIGD
AYLKRPEFSL DPSFPRFHLA EELQRPVLSA EPCVYTRVLQ TSDKFVIFAS DGLWEQMTNQ
QAVEIVNKHP RPGIARRLVR RAITIAAKKR EMNYDDLKKV ERGVRRFFHD DITVVVIFID
NELLMVEKAT VPELSIKGFS HTVGPSKFSI FLS
