ID P2C06_ORYSJ Reviewed; 467 AA. AC Q0JLP9; A0A0P0V4J5; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 24-JAN-2024, entry version 108. DE RecName: Full=Probable protein phosphatase 2C 6 {ECO:0000305}; DE Short=OsPP2C06 {ECO:0000303|PubMed:19021904}; DE EC=3.1.3.16 {ECO:0000305}; DE AltName: Full=ABI1-like protein 1 {ECO:0000305}; DE Short=OsABI-LIKE1 {ECO:0000303|PubMed:26491145}; DE Short=OsABIL1 {ECO:0000303|PubMed:26491145}; GN Name=PP2C06 {ECO:0000303|PubMed:19021904}; GN Synonyms=ABIL1 {ECO:0000303|PubMed:26491145}; GN OrderedLocusNames=Os01g0583100 {ECO:0000312|EMBL:BAS72874.1}, GN LOC_Os01g40094 {ECO:0000305}; 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=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 [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 72-467. RC STRAIN=cv. Nipponbare; RG The rice full-length cDNA consortium; RT "Oryza sativa full length cDNA."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. 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 SUBCELLULAR LOCATION, AND 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 (2.00 ANGSTROMS), AND INTERACTION WITH PYL9. RX PubMed=24743650; DOI=10.1371/journal.pone.0095246; RA He Y., Hao Q., Li W., Yan C., Yan N., Yin P.; RT "Identification and characterization of ABA receptors in Oryza sativa."; RL PLoS ONE 9:E95246-E95246(2014). CC -!- FUNCTION: Probable protein phosphatase that may function in abscisic CC acid (ABA) signaling. {ECO:0000250|UniProtKB:Q6L4R7}. 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 PYL9. {ECO:0000269|PubMed:24743650}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26491145}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:26491145}. Note=Localizes predominantly in CC nucleus. {ECO:0000269|PubMed:26491145}. CC -!- INDUCTION: Induced by abscisic acid (ABA). CC {ECO:0000269|PubMed:26491145}. CC -!- MISCELLANEOUS: Plants overexpressing PP2C06 exhibit dramatically CC reduced fertility and severe pre-harvest sprouting. CC {ECO:0000269|PubMed:26491145}. CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAF05329.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAS72874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AP008207; BAF05329.2; ALT_SEQ; Genomic_DNA. DR EMBL; AP014957; BAS72874.1; ALT_INIT; Genomic_DNA. DR EMBL; AK242616; -; NOT_ANNOTATED_CDS; mRNA. DR RefSeq; XP_015621667.1; XM_015766181.1. DR PDB; 4OIC; X-ray; 2.00 A; B=1-467. DR PDBsum; 4OIC; -. DR AlphaFoldDB; Q0JLP9; -. DR SMR; Q0JLP9; -. DR BioGRID; 793238; 1. DR STRING; 39947.Q0JLP9; -. DR PaxDb; 39947-Q0JLP9; -. DR GeneID; 4324201; -. DR KEGG; osa:4324201; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_20_4_1; -. DR InParanoid; Q0JLP9; -. DR OrthoDB; 216736at2759; -. DR Proteomes; UP000000763; Chromosome 1. DR Proteomes; UP000059680; Chromosome 1. 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; IBA:GO_Central. DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW. 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:SF160; PROTEIN PHOSPHATASE 2C 77; 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. DR Genevisible; Q0JLP9; OS. PE 1: Evidence at protein level; KW 3D-structure; Abscisic acid signaling pathway; Cytoplasm; Hydrolase; KW Magnesium; Manganese; Metal-binding; Nucleus; Protein phosphatase; KW Reference proteome. FT CHAIN 1..467 FT /note="Probable protein phosphatase 2C 6" FT /id="PRO_0000363252" FT DOMAIN 149..457 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 61..81 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 205 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 205 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 206 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 386 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 448 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 164..176 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:4OIC" FT TURN 191..193 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 195..210 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 211..234 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 239..241 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 245..264 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 280..288 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 290..300 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 302..307 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 310..313 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 323..331 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 336..344 FT /evidence="ECO:0007829|PDB:4OIC" FT TURN 345..347 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 357..359 FT /evidence="ECO:0007829|PDB:4OIC" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 368..373 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 378..384 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 386..389 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 394..411 FT /evidence="ECO:0007829|PDB:4OIC" FT HELIX 428..443 FT /evidence="ECO:0007829|PDB:4OIC" FT STRAND 450..456 FT /evidence="ECO:0007829|PDB:4OIC" SQ SEQUENCE 467 AA; 48635 MW; 50CB687EAB641C5B CRC64; MEDVAVAAAL APAPATAPVF SPAAAGLTLI AAAAADPIAA VVAGAMDGVV TVPPVRTASA VEDDAVAPGR GEEGGEASAV GSPCSVTSDC SSVASADFEG VGLGFFGAAA DGGAAMVFED SAASAATVEA EARVAAGARS VFAVECVPLW GHKSICGRRP EMEDAVVAVS RFFDIPLWML TGNSVVDGLD PMSFRLPAHF FGVYDGHGGA QVANYCRERL HAALVEELSR IEGSVSGANL GSVEFKKKWE QAFVDCFSRV DEEVGGNASR GEAVAPETVG STAVVAVICS SHIIVANCGD SRAVLCRGKQ PVPLSVDHKP NREDEYARIE AEGGKVIQWN GYRVFGVLAM SRSIGDRYLK PWIIPVPEIT IVPRAKDDEC LVLASDGLWD VMSNEEVCDV ARKRILLWHK KNGTNPASAP RSGDSSDPAA EAAAECLSKL ALQKGSKDNI SVIVVDLKAH RKFKSKS //