P2C50_ORYSJ
ID P2C50_ORYSJ Reviewed; 387 AA.
AC Q6L5H6; Q0DGE0;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein phosphatase 2C 50 {ECO:0000305};
DE Short=OsPP2C50 {ECO:0000303|PubMed:19021904};
DE EC=3.1.3.16 {ECO:0000269|PubMed:28827170};
DE AltName: Full=ABI1-like protein 3 {ECO:0000305};
DE Short=OsABI-LIKE3 {ECO:0000303|PubMed:26491145};
DE Short=OsABIL3 {ECO:0000303|PubMed:26491145};
GN Name=PP2C50 {ECO:0000303|PubMed:19021904};
GN Synonyms=ABIL3 {ECO:0000303|PubMed:26491145};
GN OrderedLocusNames=Os05g0537400 {ECO:0000312|EMBL:BAS95091.1},
GN LOC_Os05g46040 {ECO:0000305};
GN ORFNames=OJ1741_B01.18 {ECO:0000312|EMBL:AAT39223.1},
GN OSJNBa0052K01.2 {ECO:0000312|EMBL:AAV59393.1};
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 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 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 59-385, FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH PYL3; PYL5; PYL9; PYL10 AND SAPK10, VXGXL MOTIF,
RP AND MUTAGENESIS OF SER-265 AND ILE-267.
RX PubMed=28827170; DOI=10.1016/j.molp.2017.08.003;
RA Han S., Min M.K., Lee S.Y., Lim C.W., Bhatnagar N., Lee Y., Shin D.,
RA Chung K.Y., Lee S.C., Kim B.G., Lee S.;
RT "Modulation of ABA signaling by altering VxGL motif of PP2Cs in Oryza
RT sativa.";
RL Mol. Plant 10:1190-1205(2017).
CC -!- FUNCTION: Protein phosphatase involved in abscisic acid (ABA)
CC signaling. Together with PYL3 and SAPK10, may form an ABA signaling
CC module involved in stress response. {ECO:0000269|PubMed:28827170}.
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:28827170};
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:28827170};
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 PYL3, PYL5, PYL9 and PYL10. Binding to PYL3,
CC PYL5, PYL9 and PYL10 is dependent on the presence of abscisic acid
CC (ABA). Interacts with SAPK10. {ECO:0000269|PubMed:28827170}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6L5H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6L5H6-2; Sequence=VSP_036271, VSP_036272;
CC -!- INDUCTION: Induced by abscisic acid (ABA).
CC {ECO:0000269|PubMed:26491145}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC097112; AAT39223.1; -; Genomic_DNA.
DR EMBL; AC119291; AAV59393.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF18083.2; -; Genomic_DNA.
DR EMBL; AP014961; BAS95091.1; -; Genomic_DNA.
DR RefSeq; XP_015639502.1; XM_015784016.1. [Q6L5H6-1]
DR PDB; 5GWO; X-ray; 2.82 A; A/B=59-385.
DR PDB; 5GWP; X-ray; 2.58 A; A/B=59-385.
DR PDB; 5ZCG; X-ray; 2.10 A; A/B=58-385.
DR PDB; 5ZCH; X-ray; 2.47 A; A/B=58-385.
DR PDB; 5ZCL; X-ray; 2.66 A; A/B=58-385.
DR PDB; 5ZCU; X-ray; 2.41 A; A/B=58-385.
DR PDBsum; 5GWO; -.
DR PDBsum; 5GWP; -.
DR PDBsum; 5ZCG; -.
DR PDBsum; 5ZCH; -.
DR PDBsum; 5ZCL; -.
DR PDBsum; 5ZCU; -.
DR AlphaFoldDB; Q6L5H6; -.
DR SMR; Q6L5H6; -.
DR STRING; 4530.OS05T0537400-00; -.
DR PaxDb; Q6L5H6; -.
DR PRIDE; Q6L5H6; -.
DR EnsemblPlants; Os05t0537400-00; Os05t0537400-00; Os05g0537400. [Q6L5H6-2]
DR GeneID; 4339454; -.
DR Gramene; Os05t0537400-00; Os05t0537400-00; Os05g0537400. [Q6L5H6-2]
DR KEGG; osa:4339454; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_4_1; -.
DR InParanoid; Q6L5H6; -.
DR OMA; HIDPCAR; -.
DR OrthoDB; 1044139at2759; -.
DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IMP:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
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 3D-structure; Abscisic acid signaling pathway; Alternative splicing;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..387
FT /note="Protein phosphatase 2C 50"
FT /id="PRO_0000363297"
FT DOMAIN 60..377
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT MOTIF 264..268
FT /note="Modulates binding affinity to PYR/PYL/RCAR abscisic
FT acid intracellular receptors"
FT /evidence="ECO:0000269|PubMed:28827170"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 276..296
FT /note="DRYLKPFVIPKPEVMVVPRAK -> MHIDPCARSRLKHLSVSFPCK (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036271"
FT VAR_SEQ 297..387
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036272"
FT MUTAGEN 265
FT /note="S->F: Decreases binding affinity to PYL3 15-fold;
FT when associated with M-267."
FT /evidence="ECO:0000269|PubMed:28827170"
FT MUTAGEN 265
FT /note="S->K: Abolishes interaction with PYR/PYL/RCAR
FT abscisic acid intracellular receptors; when associated with
FT K-267."
FT /evidence="ECO:0000269|PubMed:28827170"
FT MUTAGEN 267
FT /note="I->K: Abolishes interaction with PYR/PYL/RCAR
FT abscisic acid intracellular receptors; when associated with
FT K-265."
FT /evidence="ECO:0000269|PubMed:28827170"
FT MUTAGEN 267
FT /note="I->M: Decreases binding affinity to PYL3 15-fold;
FT when associated with F-265."
FT /evidence="ECO:0000269|PubMed:28827170"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:5ZCG"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5ZCG"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 110..123
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 124..148
FT /evidence="ECO:0007829|PDB:5ZCG"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5GWO"
FT HELIX 156..175
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5ZCL"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5ZCL"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:5ZCL"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5ZCL"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 256..264
FT /evidence="ECO:0007829|PDB:5ZCG"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5ZCG"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 314..331
FT /evidence="ECO:0007829|PDB:5ZCG"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:5ZCG"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:5ZCG"
SQ SEQUENCE 387 AA; 41554 MW; 8DE5BAF0E1CCA2E6 CRC64;
MAAAAAAAAI CGEDETAARV GCTGEWAGGI ERVDLGERKE AVAAAGAGKR SVYLMDCAPV
WGCASTRGRS AEMEDASAAV PRFADVPVRL LASRRDLDAL GLDADALRLP AHLFGVFDGH
GGAEVANYCR ERIHVVLSEE LKRLGKNLGE MGEVDMKEHW DDVFTKCFQR VDDEVSGRVT
RVVNGGGEVR SEPVTAENVG STAVVALVCS SHVVVANCGD SRIVLCRGKE PVALSIDHKP
DRKDERARIE AQGGKVIQWN GYRVSGILAM SRSIGDRYLK PFVIPKPEVM VVPRAKDDDC
LILASDGLWD VVSNEEACKV ARRQILLWHK NNGAASPLSD EGEGSTDPAA QAAADYLMRL
ALKKGSEDNI TVIVVDLKPR KKLKNIS
