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 24-JAN-2024, entry version 119. 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}, OSJNBa0052K01.2 GN {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}. 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; 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. 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; 39947.Q6L5H6; -. DR PaxDb; 39947-Q6L5H6; -. DR EnsemblPlants; Os05t0537400-01; Os05t0537400-01; Os05g0537400. [Q6L5H6-1] DR EnsemblPlants; Os05t0537400-02; Os05t0537400-02; Os05g0537400. [Q6L5H6-2] DR GeneID; 4339454; -. DR Gramene; Os05t0537400-01; Os05t0537400-01; Os05g0537400. [Q6L5H6-1] DR Gramene; Os05t0537400-02; Os05t0537400-02; 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; 390861at2759; -. DR PlantReactome; R-OSA-3899351; Abscisic acid (ABA) mediated signaling. DR Proteomes; UP000000763; Chromosome 5. DR Proteomes; UP000059680; Chromosome 5. 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 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:SF84; PROTEIN PHOSPHATASE 2C 50; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 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 //