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 27-MAR-2024, entry version 122. 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}; 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; 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.Q5PNS9; -. DR PaxDb; 3702-AT4G38520-2; -. 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; AT4G38520; APD6. DR eggNOG; KOG0700; Eukaryota. DR HOGENOM; CLU_013173_2_0_1; -. DR InParanoid; Q5PNS9; -. DR OMA; NACLWPR; -. DR OrthoDB; 999128at2759; -. DR PhylomeDB; Q5PNS9; -. DR PRO; PR:Q5PNS9; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q5PNS9; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. 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:SF169; PROTEIN PHOSPHATASE 2C 64-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; Q5PNS9; AT. 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 //