P2C53_ORYSJ
ID P2C53_ORYSJ Reviewed; 445 AA.
AC Q6L4R7; B7EHS4; B9FJ05;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein phosphatase 2C 53 {ECO:0000305};
DE Short=OsPP2C53 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000269|PubMed:26491145};
DE AltName: Full=ABI1-like protein 2 {ECO:0000305};
DE Short=OsABI-LIKE2 {ECO:0000303|PubMed:26491145};
DE Short=OsABIL2 {ECO:0000303|PubMed:26491145};
GN Name=PP2C53 {ECO:0000303|PubMed:19021904};
GN Synonyms=ABIL2 {ECO:0000303|PubMed:26491145};
GN OrderedLocusNames=Os05g0592800 {ECO:0000312|EMBL:BAS95645.1},
GN LOC_Os05g51510 {ECO:0000305};
GN ORFNames=OsJ_018965, OsJ_19760 {ECO:0000312|EMBL:EEE64901.1},
GN P0663C08.11 {ECO:0000312|EMBL:AAT44303.1};
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] (ISOFORMS 1 AND 2).
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, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH PYL10;
RP SAPK8 AND SAPK10, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND LACK OF
RP INDUCTION BY ABSCISIC ACID.
RX PubMed=26491145; DOI=10.1093/pcp/pcv154;
RA Li C., Shen H., Wang T., Wang X.;
RT "ABA regulates subcellular redistribution of OsABI-LIKE2, a negative
RT regulator in ABA signaling, to control root architecture and drought
RT resistance in Oryza sativa.";
RL Plant Cell Physiol. 56:2396-2408(2015).
RN [9]
RP INTERACTION WITH PYL3; PYL5; PYL9 AND PYL10, AND 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).
CC -!- FUNCTION: Protein phosphatase that acts as negative regulator of
CC abscisic acid (ABA) signaling. Involved in the regulation of root
CC architecture development and drought resistance. Can dephosphorylate
CC SAPK8 and SAPK10 in vitro. Together with PYL10, SAPK8 and SAPK10, may
CC form an ABA signaling module involved in stress response.
CC {ECO:0000269|PubMed:26491145}.
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:26491145};
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:26491145};
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 -!- ACTIVITY REGULATION: Repressed by abscisic acid-bound PYL1.
CC {ECO:0000269|PubMed:26491145}.
CC -!- SUBUNIT: Interacts with PYL10, SAPK8 and SAPK10. Binding to PYL10 is
CC dependent on the presence of abscisic acid (ABA) (PubMed:26491145).
CC Interacts with PYL3, PYL5, PYL9 and PYL10. Binding to PYL9 and PYL10 is
CC dependent on the presence of ABA (PubMed:26362328).
CC {ECO:0000269|PubMed:26362328, ECO:0000269|PubMed:26491145}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:26491145}. Nucleus {ECO:0000269|PubMed:26362328,
CC ECO:0000269|PubMed:26491145}. Note=Treatment with abscisic acid (ABA)
CC reduces the nuclear localization and enhances the cytosolic
CC localization. {ECO:0000269|PubMed:26491145}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6L4R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6L4R7-2; Sequence=VSP_036273, VSP_036274;
CC -!- TISSUE SPECIFICITY: Expressed in leaf blades, leaf sheaths and lamina
CC joints. Expressed at low levels in roots, stems, flowers and panicles.
CC {ECO:0000269|PubMed:26491145}.
CC -!- INDUCTION: Not induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:26491145}.
CC -!- MISCELLANEOUS: Plants overexpressing PP2C53 are insensitive to abscisic
CC acid (ABA), exhibit altered stomatal density and root architecture, and
CC are hypersensitive to drought stress. {ECO:0000269|PubMed:26491145}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC130728; AAT44303.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18412.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS95645.1; -; Genomic_DNA.
DR EMBL; CM000142; EAZ35482.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64901.1; -; Genomic_DNA.
DR EMBL; AK067627; BAG90506.1; -; mRNA.
DR EMBL; AK070388; BAG91921.1; -; mRNA.
DR RefSeq; XP_015640522.1; XM_015785036.1. [Q6L4R7-1]
DR AlphaFoldDB; Q6L4R7; -.
DR SMR; Q6L4R7; -.
DR STRING; 4530.OS05T0592800-02; -.
DR PaxDb; Q6L4R7; -.
DR PRIDE; Q6L4R7; -.
DR EnsemblPlants; Os05t0592800-01; Os05t0592800-01; Os05g0592800. [Q6L4R7-2]
DR EnsemblPlants; Os05t0592800-02; Os05t0592800-02; Os05g0592800. [Q6L4R7-1]
DR EnsemblPlants; Os05t0592800-03; Os05t0592800-03; Os05g0592800. [Q6L4R7-1]
DR GeneID; 4339797; -.
DR Gramene; Os05t0592800-01; Os05t0592800-01; Os05g0592800. [Q6L4R7-2]
DR Gramene; Os05t0592800-02; Os05t0592800-02; Os05g0592800. [Q6L4R7-1]
DR Gramene; Os05t0592800-03; Os05t0592800-03; Os05g0592800. [Q6L4R7-1]
DR KEGG; osa:4339797; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_4_1; -.
DR InParanoid; Q6L4R7; -.
DR OMA; LFELGNM; -.
DR OrthoDB; 1044139at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR PlantReactome; R-OSA-9639861; Development of root hair.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; Q6L4R7; OS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:0009414; P:response to water deprivation; IMP:UniProtKB.
DR GO; GO:0048364; P:root 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; 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; Alternative splicing; Cytoplasm;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..445
FT /note="Protein phosphatase 2C 53"
FT /id="PRO_0000363300"
FT DOMAIN 124..435
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 180
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_036273"
FT VAR_SEQ 145..186
FT /note="PRFFDLPLWMVAGDAAVDGLDRASFRLPAHFFAVYDGHGGVQ -> MPWSRD
FT FSTFLCGWLPATRQSTASTGPPSAFQPISSPSTMAT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_036274"
SQ SEQUENCE 445 AA; 46684 MW; E06D4D4A57E97FC1 CRC64;
MEDLALPAAP PAPTLSFTLL AAAAAVAEAM EEALGAALPP LTAPVPAPGD DSACGSPCSV
ASDCSSVASA DFEGFAELGT SLLAGPAVLF DDLTAASVAV AEAAEPRAVG ATARSVFAMD
CVPLWGLESI CGRRPEMEDD YAVVPRFFDL PLWMVAGDAA VDGLDRASFR LPAHFFAVYD
GHGGVQVANY CRKRIHAVLT EELRRAEDDA CGSDLSGLES KKLWEKAFVD CFSRVDAEVG
GNAASGAPPV APDTVGSTAV VAVVCSSHVI VANCGDSRAV LCRGKQPLPL SLDHKPNRED
EYARIEALGG KVIQWNGYRV LGVLAMSRSI GDKYLKPYII PVPEVTVVAR AKDDDCLILA
SDGLWDVMSN EEVCDAARKR ILLWHKKNAA TASTSSAQIS GDSSDPAAQA AADYLSKLAL
QKGSKDNITV VVIDLKAHRK FKSKA
