P2C35_ORYSJ
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 03-AUG-2022, entry version 115.
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 Xantomonas 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; 4530.OS03T0821300-01; -.
DR PaxDb; Q84T94; -.
DR PRIDE; 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; LLWDQCE; -.
DR OrthoDB; 461546at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q84T94; baseline and differential.
DR Genevisible; Q84T94; OS.
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 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; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
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