P2C51_ORYSJ
ID P2C51_ORYSJ Reviewed; 381 AA.
AC Q65XK7; B9FIF4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein phosphatase 2C 51 {ECO:0000305};
DE Short=OsPP2C51 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000269|PubMed:28000033};
GN Name=PP2C51 {ECO:0000303|PubMed:19021904};
GN OrderedLocusNames=Os05g0572700 {ECO:0000312|EMBL:BAS95440.1},
GN LOC_Os05g49730 {ECO:0000305};
GN ORFNames=OJ1735_C10.11 {ECO:0000312|EMBL:AAU44100.1}, OsJ_018833,
GN OsJ_19620 {ECO:0000312|EMBL:EEE64764.1};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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 SUBCELLULAR LOCATION.
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).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABI5; PYL5 AND SAPK2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY ABSCISIC ACID.
RX PubMed=28000033; DOI=10.1007/s11103-016-0568-2;
RA Bhatnagar N., Min M.K., Choi E.H., Kim N., Moon S.J., Yoon I., Kwon T.,
RA Jung K.H., Kim B.G.;
RT "The protein phosphatase 2C clade A protein OsPP2C51 positively regulates
RT seed germination by directly inactivating OsbZIP10.";
RL Plant Mol. Biol. 93:389-401(2017).
CC -!- FUNCTION: Protein phosphatase that acts as positive regulator of seed
CC germination. Involved in the positive regulation of alpha-amylase gene
CC expression. Acts as negative regulator of abscisic acid-mediated
CC responses. May function directly by dephosphorylating ABI5 and
CC suppressing its activity. {ECO:0000269|PubMed:28000033}.
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:0000269|PubMed:28000033};
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:0000269|PubMed:28000033};
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 ABI5 and PYL5. Binding to PYL5 is dependent on
CC the presence of abscisic acid (ABA). {ECO:0000269|PubMed:28000033}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:28000033}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the embryo of mature
CC seed. {ECO:0000269|PubMed:28000033}.
CC -!- INDUCTION: Induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:28000033}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC104284; AAU44100.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18292.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95440.1; -; Genomic_DNA.
DR EMBL; CM000142; EAZ35350.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64764.1; -; Genomic_DNA.
DR EMBL; AK108969; BAG98572.1; -; mRNA.
DR RefSeq; XP_015638143.1; XM_015782657.1.
DR AlphaFoldDB; Q65XK7; -.
DR SMR; Q65XK7; -.
DR STRING; 4530.OS05T0572700-02; -.
DR PaxDb; Q65XK7; -.
DR PRIDE; Q65XK7; -.
DR EnsemblPlants; Os05t0572700-02; Os05t0572700-02; Os05g0572700.
DR GeneID; 4339671; -.
DR Gramene; Os05t0572700-02; Os05t0572700-02; Os05g0572700.
DR KEGG; osa:4339671; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_0_1; -.
DR InParanoid; Q65XK7; -.
DR OMA; VIVIELR; -.
DR OrthoDB; 1044139at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; Q65XK7; baseline and differential.
DR Genevisible; Q65XK7; 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; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR GO; GO:0010030; P:positive regulation of seed germination; 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; SM00331; PP2C_SIG; 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..381
FT /note="Protein phosphatase 2C 51"
FT /id="PRO_0000363298"
FT DOMAIN 77..373
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 50..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 381 AA; 40349 MW; 451258562D67F818 CRC64;
MRETGATDEG HACEVVVAGG DGKAAAARRR RRLELRRLGL AAEDDAAAKR IRSVKDGSSS
DDSSTEVVPR SWPACVSHGS VSVIGRRREM EDAVAIERTF MASTGDGAGA IRGGGEGEED
FFAVYDGHGG SRVAEACRKR MHVVLAEEVS LRRLRGQSAS GGDVRWKEAM LASFARMDGE
VVGSVAAAAP RVDGTEPSGF RTVGSTAVVA VVGRRRIVVA NCGDSRAVLS RGGVALPLST
DHKPDRPDEL ERVEAAGGRV INWNGYRVLG VLATSRSIGD YYLKPFVSAE PEVRVVERTD
KDEFLILASD GLWDVVSNEV ACKIARNCLN GRAASMFPES VSGSSAADAA ALLAELAVSR
GSRDNISVVV VELRRLKSRA A
