ID   P2C35_ORYSJ             Reviewed;         639 AA.
AC   Q84T94; A0A0P0W4T8; A3AP53; Q70KS9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Protein phosphatase 2C 35;
DE            Short=OsPP2C35;
DE            EC=3.1.3.16;
DE   AltName: Full=XA21-binding protein 15;
GN   Name=XB15; OrderedLocusNames=Os03g0821300, LOC_Os03g60650;
GN   ORFNames=OJ1754_E06.28, OsJ_012575;
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=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 486-639.
RC   TISSUE=Embryo;
RX   PubMed=15078336; DOI=10.1111/j.1365-313x.2004.02037.x;
RA   Ye R., Yao Q.-H., Xu Z.-H., Xue H.-W.;
RT   "Development of an efficient method for the isolation of factors involved
RT   in gene transcription during rice embryo development.";
RL   Plant J. 38:348-357(2004).
RN   [8]
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   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP   XA21.
RX   PubMed=18817453; DOI=10.1371/journal.pbio.0060231;
RA   Park C.-J., Peng Y., Chen X., Dardick C., Ruan D., Bart R., Canlas P.E.,
RA   Ronald P.C.;
RT   "Rice XB15, a protein phosphatase 2C, negatively regulates cell death and
RT   XA21-mediated innate immunity.";
RL   PLoS Biol. 6:E231-E231(2008).
CC   -!- FUNCTION: Protein phosphatase that acts on XA21 pathogen recognition
CC       receptor. Negatively regulates cell death and XA21-mediated innate
CC       immunity. {ECO:0000269|PubMed:18817453}.
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   -!- SUBUNIT: Interacts with XA21 (via juxtamembrane and kinase domains).
CC       {ECO:0000269|PubMed:18817453}.
CC   -!- INTERACTION:
CC       Q84T94; Q40640: Xa21; Xeno; NbExp=4; IntAct=EBI-15730564, EBI-15730546;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18817453};
CC       Peripheral membrane protein {ECO:0000269|PubMed:18817453}; Cytoplasmic
CC       side {ECO:0000269|PubMed:18817453}. Note=Associated with XA21 receptor
CC       kinase.
CC   -!- DISRUPTION PHENOTYPE: Enhanced resistance to Xanthomonas oryzae pv.
CC       oryzae (Xoo), expression of defense-related genes and cell death
CC       (necrotic lesions). {ECO:0000269|PubMed:18817453}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR   EMBL; AC104433; AAO65883.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF99594.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13640.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS87094.1; -; Genomic_DNA.
DR   EMBL; CM000140; EAZ29092.1; -; Genomic_DNA.
DR   EMBL; AK071722; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AJ575237; CAE00873.1; -; mRNA.
DR   RefSeq; XP_015632569.1; XM_015777083.1.
DR   AlphaFoldDB; Q84T94; -.
DR   SMR; Q84T94; -.
DR   DIP; DIP-46055N; -.
DR   IntAct; Q84T94; 1.
DR   STRING; 39947.Q84T94; -.
DR   PaxDb; 39947-Q84T94; -.
DR   EnsemblPlants; Os03t0821300-01; Os03t0821300-01; Os03g0821300.
DR   GeneID; 4334600; -.
DR   Gramene; Os03t0821300-01; Os03t0821300-01; Os03g0821300.
DR   KEGG; osa:4334600; -.
DR   eggNOG; KOG0700; Eukaryota.
DR   HOGENOM; CLU_013173_12_1_1; -.
DR   InParanoid; Q84T94; -.
DR   OMA; LLWHQCE; -.
DR   OrthoDB; 999128at2759; -.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000007752; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   ExpressionAtlas; Q84T94; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0006952; P:defense response; 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; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF228; PROTEIN PHOSPHATASE 2C 4-RELATED; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
DR   Genevisible; Q84T94; OS.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW   Plant defense; Protein phosphatase; Reference proteome.
FT   CHAIN           1..639
FT                   /note="Protein phosphatase 2C 35"
FT                   /id="PRO_0000363282"
FT   DOMAIN          227..630
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   REGION          295..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         262
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         558
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         621
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        12..13
FT                   /note="GG -> CC (in Ref. 5; EAZ29092)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="A -> V (in Ref. 6; AK071722)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="P -> T (in Ref. 6; AK071722)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   639 AA;  69180 MW;  E64A0AED1838C00F CRC64;
     MGNSLACFCC GGGAGGRGGR HVAPAALPSD PAYDEGLGHS FCYVRPDKFV VPFSADDLVA
     DAKAAAAAEG EATTFRAISG AALSANVSTP LSTSVLLLMP EESSASATAS SGFESSESFA
     AVPLQPVPRF SSGPISAPFS GGFMSGPLER GFQSGPLDAA LLSGPLPGTA TSGRMGGAVP
     ALRRSLSHGG RRLRNFTRAL LARTEKFQDS ADLGSPDAAA AAVAACGGDP CGLQWAQGKA
     GEDRVHVVVS EERGWVFVGI YDGFNGPDAT DFLVSNLYAA VHRELRGLLW DQREQNVQHD
     QRPDQPGSAP STTASDNQDQ WGRRRRTRRS RPPRGADDDQ RRWKCEWEQE RDCSNLKPPT
     QQRLRCNSEN DHVAVLKALT RALHRTEEAY LDIADKMVGE FPELALMGSC VLAMLMKGED
     MYIMNVGDSR AVLATMDSVD LEQISQGSFD GSVGDCPPCL SAVQLTSDHS TSVEEEVIRI
     RNEHPDDPSA ISKDRVKGSL KVTRAFGAGF LKQPKWNDAL LEMFRIDYVG SSPYISCNPS
     LFHHKLSTRD RFLILSSDGL YQYFTNEEAV AQVEMFIATT PEGDPAQHLV EEVLFRAANK
     AGMDFHELIE IPHGDRRRYH DDVSVIVISL EGRIWRSCV
//