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};
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; 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
