P2C30_ORYSJ
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 03-AUG-2022, entry version 129.
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},
GN OsJ_009875 {ECO:0000312|EMBL:EAZ26392.1},
GN OSJNBa0071M09.4 {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}.
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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; 4530.OS03T0268600-01; -.
DR PaxDb; Q84JI0; -.
DR PRIDE; 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; GCHFYGV; -.
DR OrthoDB; 1044139at2759; -.
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 Genevisible; Q84JI0; OS.
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:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
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; -; 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 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
