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P2C13_ORYSJ
ID   P2C13_ORYSJ             Reviewed;         363 AA.
AC   Q6EN45; A0A0P0VH70;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable protein phosphatase 2C member 13, mitochondrial {ECO:0000305};
DE            Short=OsPP2C13 {ECO:0000303|PubMed:19021904};
DE            EC=3.1.3.16 {ECO:0000305};
DE   AltName: Full=Protein DOWNREGULATED IN CW-CMS 11 {ECO:0000303|PubMed:18308761};
DE   Flags: Precursor;
GN   Name=PP2C13 {ECO:0000303|PubMed:19021904};
GN   Synonyms=DCW11 {ECO:0000303|PubMed:18308761};
GN   OrderedLocusNames=Os02g0255100 {ECO:0000312|EMBL:BAS77942.1},
GN   LOC_Os02g15594 {ECO:0000305};
GN   ORFNames=OSJNBa0052K15.14 {ECO:0000312|EMBL:BAD29690.1};
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=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].
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   [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   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=18308761; DOI=10.1093/pcp/pcn036;
RA   Fujii S., Toriyama K.;
RT   "DCW11, down-regulated gene 11 in CW-type cytoplasmic male sterile rice,
RT   encoding mitochondrial protein phosphatase 2c is related to cytoplasmic
RT   male sterility.";
RL   Plant Cell Physiol. 49:633-640(2008).
CC   -!- FUNCTION: Probable protein phosphatase that may play a role as a
CC       mitochondrial signal transduction mediator in pollen germination. May
CC       function in retrograde signaling from the mitochondria to the nucleus.
CC       May be a downstream factor of cytoplasmic male sterility (CMS). CMS is
CC       caused by genetic incompatibility between nuclei and mitochondria
CC       within male reproductive organs. {ECO:0000269|PubMed:18308761}.
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   -!- 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   -!- 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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:18308761}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in mature pollen grains.
CC       {ECO:0000269|PubMed:18308761}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in anthers from the bi-cellular to the
CC       tri-cellular pollen stage. {ECO:0000269|PubMed:18308761}.
CC   -!- MISCELLANEOUS: Plants silencing PP2C13 exhibit a major loss of seed-set
CC       fertility, without visible defect in pollen development. Plants
CC       silencing PP2C13 show up-regulation of AOX1A gene which is regulated by
CC       mitochondrial retrograde signaling. {ECO:0000269|PubMed:18308761}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK069289; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP006844; BAD29690.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08375.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS77942.1; -; Genomic_DNA.
DR   EMBL; AK069289; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015625481.1; XM_015769995.1.
DR   AlphaFoldDB; Q6EN45; -.
DR   SMR; Q6EN45; -.
DR   STRING; 4530.OS02T0255100-01; -.
DR   PaxDb; Q6EN45; -.
DR   PRIDE; Q6EN45; -.
DR   EnsemblPlants; Os02t0255100-01; Os02t0255100-01; Os02g0255100.
DR   GeneID; 4328913; -.
DR   Gramene; Os02t0255100-01; Os02t0255100-01; Os02g0255100.
DR   KEGG; osa:4328913; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   HOGENOM; CLU_013173_0_6_1; -.
DR   InParanoid; Q6EN45; -.
DR   OMA; IFDGHSN; -.
DR   OrthoDB; 1044139at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   ExpressionAtlas; Q6EN45; baseline and differential.
DR   Genevisible; Q6EN45; OS.
DR   GO; GO:0005739; C:mitochondrion; 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:0009846; P:pollen germination; IMP:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase_dom.
DR   PANTHER; PTHR13832; PTHR13832; 1.
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   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   Protein phosphatase; Reference proteome; Transit peptide.
FT   TRANSIT         1..59
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           60..363
FT                   /note="Probable protein phosphatase 2C member 13,
FT                   mitochondrial"
FT                   /id="PRO_0000363259"
FT   DOMAIN          111..357
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        261
FT                   /note="Missing (in Ref. 4; AK069289)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  38958 MW;  CD1318CCA7E043C7 CRC64;
     MVCFASLRRA LPLLLRATTT TTPRFLLPRA LSGGVGGGAA VDARALLRGH SGWRGLRVAA
     RMMLDSSDSA AAAGQMQPQQ RAAGAVACSA QDGGAAGYAS GGWAREDGKL KCGYSSFRGK
     RATMEDFYDV KLTEIDGQAV SLFGVFDGHG GPRAAEYLKE NLFENLLKHP EFLTDTKLAI
     SETYQKTDTD FLESESNAFR DDGSTASTAV LVGGHLYVAN VGDSRAVVSK AGKAMALSED
     HKPNRSDERK RIENAGGVVI WAGTWRVGGV LAMSRAFGNR LLKPFVVAEP EIQEELVNED
     LECLVLASDG LWDVVENEEA VSLAKTEDLP ESVARKLTEI AYSRGSADNI TCIVVQFHHD
     KTE
 
 
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