ID P2C08_ORYSJ Reviewed; 403 AA. AC Q5SN75; A0A0P0V628; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Probable protein phosphatase 2C 8; DE Short=OsPP2C08; DE EC=3.1.3.16; GN OrderedLocusNames=Os01g0656200, LOC_Os01g46760; GN ORFNames=OSJNBa0049H05.30; 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=12447438; DOI=10.1038/nature01184; RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M., RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.; RT "The genome sequence and structure of rice chromosome 1."; RL Nature 420:312-316(2002). 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 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 [6] 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). 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 -!- SIMILARITY: Belongs to the PP2C family. {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; AP003212; BAD72331.1; -; Genomic_DNA. DR EMBL; AP008207; BAF05668.1; -; Genomic_DNA. DR EMBL; AP014957; BAS73501.1; -; Genomic_DNA. DR EMBL; AK068272; BAG90835.1; -; mRNA. DR RefSeq; XP_015614087.1; XM_015758601.1. DR AlphaFoldDB; Q5SN75; -. DR SMR; Q5SN75; -. DR BioGRID; 793219; 1. DR STRING; 39947.Q5SN75; -. DR PaxDb; 39947-Q5SN75; -. DR EnsemblPlants; Os01t0656200-01; Os01t0656200-01; Os01g0656200. DR GeneID; 4324182; -. DR Gramene; Os01t0656200-01; Os01t0656200-01; Os01g0656200. DR KEGG; osa:4324182; -. DR eggNOG; KOG0698; Eukaryota. DR HOGENOM; CLU_013173_20_0_1; -. DR InParanoid; Q5SN75; -. DR OMA; NKGRMAE; -. DR OrthoDB; 1702801at2759; -. DR Proteomes; UP000000763; Chromosome 1. DR Proteomes; UP000059680; Chromosome 1. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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 CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR47992:SF245; PROTEIN PHOSPHATASE 2C 8-RELATED; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q5SN75; OS. PE 2: Evidence at transcript level; KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..403 FT /note="Probable protein phosphatase 2C 8" FT /id="PRO_0000363254" FT DOMAIN 90..388 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 42..80 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..60 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 144 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 144 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 145 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 325 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 379 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" SQ SEQUENCE 403 AA; 42998 MW; 3DADB7EC1E3E3261 CRC64; MSSDTSRRDH AAMAVREVLA GDRKVGTVSR SARRRRLELR RLGRTASAVA EDDAAKRVRP ASDSSSDSSE SAKVAPEPTA EVARWPACVS HGAVSVIGRR REMEDAIFVA APFLAASKEA AVEGSGVAEE EGKEEDEGFF AVYDGHGGSR VAEACRERMH VVLAEEVRVR RLLQGGGGGA DVEDEDRARW KEAMAACFTR VDGEVGGAEE ADTGEQTVGS TAVVAVVGPR RIVVANCGDS RAVLSRGGVA VPLSSDHKPD RPDEMERVEA AGGRVINWNG YRILGVLATS RSIGDYYLKP YVIAEPEVTV MDRTDKDEFL ILASDGLWDV VSNDVACKIA RNCLSGRAAS KYPESVSGST AADAAALLVE LAISRGSKDN ISVVVVELRR LRSRTTASKE NGR //