ID P2C30_ORYSJ Reviewed; 404 AA. AC Q84JI0; A0A0N7KH02; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Probable protein phosphatase 2C 30 {ECO:0000305}; DE Short=OsPP2C30 {ECO:0000303|PubMed:19021904}; DE EC=3.1.3.16 {ECO:0000305}; GN Name=PP2C30 {ECO:0000303|PubMed:19021904}; GN OrderedLocusNames=Os03g0268600 {ECO:0000312|EMBL:BAS83449.1}, GN LOC_Os03g16170 {ECO:0000312|EMBL:ABF95181.1}; GN ORFNames=OJA1364E02.13 {ECO:0000312|EMBL:AAP06902.1}, OsJ_009875 GN {ECO:0000312|EMBL:EAZ26392.1}, OSJNBa0071M09.4 GN {ECO:0000312|EMBL:AAP06912.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16109971; DOI=10.1101/gr.3869505; RG The rice chromosome 3 sequencing consortium; RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B., RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T., RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K., RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T., RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R., RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J., RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S., RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M., RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M., RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L., RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R., RA Jin W., Lee H.R., Jiang J., Jackson S.; RT "Sequence, annotation, and analysis of synteny between rice chromosome 3 RT and diverged grass species."; RL Genome Res. 15:1284-1291(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=18089549; DOI=10.1093/nar/gkm978; RG The rice annotation project (RAP); RT "The rice annotation project database (RAP-DB): 2008 update."; RL Nucleic Acids Res. 36:D1028-D1033(2008). RN [4] RP GENOME REANNOTATION. RC STRAIN=cv. Nipponbare; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12869764; DOI=10.1126/science.1081288; RG The rice full-length cDNA consortium; RT "Collection, mapping, and annotation of over 28,000 cDNA clones from RT japonica rice."; RL Science 301:376-379(2003). RN [7] 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 [8] RP FUNCTION, INTERACTION WITH PYL5 AND SAPK2, AND SUBCELLULAR LOCATION. RX PubMed=22071266; DOI=10.1093/jxb/err338; RA Kim H., Hwang H., Hong J.W., Lee Y.N., Ahn I.P., Yoon I.S., Yoo S.D., RA Lee S., Lee S.C., Kim B.G.; RT "A rice orthologue of the ABA receptor, OsPYL/RCAR5, is a positive RT regulator of the ABA signal transduction pathway in seed germination and RT early seedling growth."; RL J. Exp. Bot. 63:1013-1024(2012). RN [9] RP INTERACTION WITH PYL3; PYL5 AND PYL9, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=26362328; DOI=10.1186/s12284-015-0061-6; RA Tian X., Wang Z., Li X., Lv T., Liu H., Wang L., Niu H., Bu Q.; RT "Characterization and functional analysis of pyrabactin resistance-like RT abscisic acid receptor family in rice."; RL Rice 8:28-28(2015). CC -!- FUNCTION: Together with ABI5, PYL5 and SAPK2, is part of an abscisic CC acid (ABA) signaling unit that modulates seed germination and early CC seedling growth. {ECO:0000269|PubMed:22071266}. 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:0000305}; 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:0000305}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Interacts with PYL5 and SAPK2. Binding to PYL5 is dependent on CC the presence of abscisic acid (ABA) (PubMed:22071266). Interacts with CC PYL3, PYL5 and PYL9. Binding to PYL5 and PYL9 is dependent on the CC presence of ABA (PubMed:26362328). {ECO:0000269|PubMed:22071266, CC ECO:0000269|PubMed:26362328}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22071266, CC ECO:0000269|PubMed:26362328}. 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; AC135209; AAP06912.1; -; Genomic_DNA. DR EMBL; AC139168; AAP06902.1; -; Genomic_DNA. DR EMBL; DP000009; ABF95181.1; -; Genomic_DNA. DR EMBL; AP008209; BAF11588.1; -; Genomic_DNA. DR EMBL; AP014959; BAS83449.1; -; Genomic_DNA. DR EMBL; CM000140; EAZ26392.1; -; Genomic_DNA. DR EMBL; AK069274; BAG91354.1; -; mRNA. DR RefSeq; XP_015628825.1; XM_015773339.1. DR AlphaFoldDB; Q84JI0; -. DR SMR; Q84JI0; -. DR STRING; 39947.Q84JI0; -. DR PaxDb; 39947-Q84JI0; -. DR EnsemblPlants; Os03t0268600-01; Os03t0268600-01; Os03g0268600. DR GeneID; 4332374; -. DR Gramene; Os03t0268600-01; Os03t0268600-01; Os03g0268600. DR KEGG; osa:4332374; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_20_0_1; -. DR InParanoid; Q84JI0; -. DR OMA; DLRRNHH; -. DR OrthoDB; 415067at2759; -. DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling. DR Proteomes; UP000000763; Chromosome 3. DR Proteomes; UP000007752; Chromosome 3. DR Proteomes; UP000059680; Chromosome 3. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. 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:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB. DR GO; GO:0009845; P:seed germination; IMP:UniProtKB. DR GO; GO:0090351; P:seedling development; IMP:UniProtKB. 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:SF176; PROTEIN PHOSPHATASE 2C 30-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; Q84JI0; OS. PE 1: Evidence at protein level; KW Abscisic acid signaling pathway; Hydrolase; Magnesium; Manganese; KW Metal-binding; Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..404 FT /note="Probable protein phosphatase 2C 30" FT /id="PRO_0000363276" FT DOMAIN 77..399 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 42..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 321..369 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 326..347 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 111 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 111 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 112 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 298 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 390 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 404 AA; 43282 MW; AE54FDF177D0B6BF CRC64; MAEICCEVVA GSSSEGKGPE CDTGSRAARR RRMEIRRLRV VAERGAEEET SGKRRRLDGG GGEASTDEED REVERARYGF TSVCGRRRDM EDSVSACPGF LPGHHFFGVF DGHGCSHVAT SCGQRMHEIV VDEAGAAAGS AGLDEEARWR GVMERSFARM DAEAVASSRG SVAPAPTCRC EMQLPKCDHV GSTAVVAVLG PRHVVVANCG DSRAVLCRGG AAIPLSCDHK PDRPDELERI HAAGGRVIFW DGARVFGMLA MSRAIGDSYL KPYVICDPEV RVMERKDGED EFLILASDGL WDVVSNEVAC NVVRACLRSS GRRERNRSSP TSNLSPRQSS SSGDEAPNDG APSAAAGSES DEESAAEEDK ACAEAAVLLT KLALARQTSD NVSVVVVNLR RRKL //