P2C64_ARATH
ID P2C64_ARATH Reviewed; 400 AA.
AC Q5PNS9; Q8W4N8; Q9SZN2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable protein phosphatase 2C 64 {ECO:0000303|PubMed:19021904};
DE Short=AtPP2C64 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q9LHJ9};
GN Name=PP2C64 {ECO:0000303|PubMed:19021904};
GN Synonyms=PP2C-D5 {ECO:0000303|PubMed:24858935};
GN OrderedLocusNames=At4g38520 {ECO:0000312|Araport:AT4G38520};
GN ORFNames=F20M13.80 {ECO:0000312|EMBL:CAB37508.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2005) 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, INTERACTION WITH SAUR19, GENE FAMILY, AND
RP 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: Dephosphorylates and represses 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 -!- SUBUNIT: Interacts with SAUR19. {ECO:0000269|PubMed:24858935}.
CC -!- DISRUPTION PHENOTYPE: Slight increase in hypocotyl length
CC (PubMed:24858935). 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 (PubMed:24858935). {ECO:0000269|PubMed:24858935}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37508.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80516.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL035540; CAB37508.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161593; CAB80516.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86941.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86942.1; -; Genomic_DNA.
DR EMBL; AY062454; AAL32532.1; -; mRNA.
DR EMBL; BT020368; AAV85723.1; -; mRNA.
DR EMBL; BT021094; AAX12864.1; -; mRNA.
DR PIR; T05680; T05680.
DR RefSeq; NP_195564.2; NM_120013.6.
DR RefSeq; NP_974708.1; NM_202979.1.
DR AlphaFoldDB; Q5PNS9; -.
DR SMR; Q5PNS9; -.
DR BioGRID; 15289; 3.
DR IntAct; Q5PNS9; 2.
DR MINT; Q5PNS9; -.
DR STRING; 3702.AT4G38520.2; -.
DR PaxDb; Q5PNS9; -.
DR PRIDE; Q5PNS9; -.
DR ProteomicsDB; 250971; -.
DR EnsemblPlants; AT4G38520.1; AT4G38520.1; AT4G38520.
DR EnsemblPlants; AT4G38520.2; AT4G38520.2; AT4G38520.
DR GeneID; 830009; -.
DR Gramene; AT4G38520.1; AT4G38520.1; AT4G38520.
DR Gramene; AT4G38520.2; AT4G38520.2; AT4G38520.
DR KEGG; ath:AT4G38520; -.
DR Araport; AT4G38520; -.
DR TAIR; locus:2121234; AT4G38520.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_013173_2_0_1; -.
DR InParanoid; Q5PNS9; -.
DR OMA; CMSSEVI; -.
DR OrthoDB; 461546at2759; -.
DR PhylomeDB; Q5PNS9; -.
DR PRO; PR:Q5PNS9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5PNS9; baseline and differential.
DR Genevisible; Q5PNS9; 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 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..400
FT /note="Probable protein phosphatase 2C 64"
FT /id="PRO_0000367986"
FT DOMAIN 47..355
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 86
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
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 287
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LHJ9"
FT CONFLICT 38
FT /note="R -> S (in Ref. 3; AAL32532)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 44123 MW; 66AA091D20562CE3 CRC64;
MLSGLMNFLN ACLWPRSDQQ ARSASDSGGR QEGLLWFRDS GQHVFGDFSM AVVQANSLLE
DQSQLESGSL SSHDSGPFGT FVGVYDGHGG PETSRFINDH MFHHLKRFTA EQQCMSSEVI
KKAFQATEEG FLSIVTNQFQ TRPQIATVGS CCLVSVICDG KLYVANAGDS RAVLGQVMRV
TGEAHATQLS AEHNASIESV RRELQALHPD HPDIVVLKHN VWRVKGIIQV SRSIGDVYLK
RSEFNREPLY AKFRLRSPFS KPLLSAEPAI TVHTLEPHDQ FIICASDGLW EHMSNQEAVD
IVQNHPRNGI AKRLVKVALQ EAAKKREMRY SDLKKIDRGV RRHFHDDITV IVVFFDTNLV
SRGSMLRGPA VSVRGAGVNL PHNTLAPCTT PTQAAAAGAS
