P2C06_ORYSJ
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 03-AUG-2022, entry version 103.
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};
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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; 4530.OS01T0583100-01; -.
DR PaxDb; Q0JLP9; -.
DR PRIDE; Q0JLP9; -.
DR GeneID; 4324201; -.
DR KEGG; osa:4324201; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_20_4_1; -.
DR InParanoid; Q0JLP9; -.
DR OrthoDB; 1044139at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q0JLP9; 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; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
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; 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
