ID P2C72_ORYSJ Reviewed; 393 AA. AC Q7XCJ7; B9G1Z8; Q9AV42; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 24-JAN-2024, entry version 125. DE RecName: Full=Probable protein phosphatase 2C 72; DE Short=OsPP2C72; DE EC=3.1.3.16; GN OrderedLocusNames=Os10g0544900, LOC_Os10g39780; GN ORFNames=OsJ_026955, OsJ_28079 {ECO:0000312|EMBL:EEE69065.1}, GN OSJNBa0001O14.1; 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=12791992; DOI=10.1126/science.1083523; RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M., RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.; RT "In-depth view of structure, activity, and evolution of rice chromosome RT 10."; RL Science 300:1566-1569(2003). 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] (ISOFORM 1). 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 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q7XCJ7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7XCJ7-2; Sequence=VSP_036281, VSP_036282; CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK20060.1; Type=Erroneous initiation; 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; AC025783; AAK20060.1; ALT_INIT; Genomic_DNA. DR EMBL; DP000086; AAP54876.1; -; Genomic_DNA. DR EMBL; AP008216; BAF27117.1; -; Genomic_DNA. DR EMBL; AP014966; BAT11893.1; -; Genomic_DNA. DR EMBL; CM000145; EEE69065.1; -; Genomic_DNA. DR EMBL; AK119635; BAG99722.1; -; mRNA. DR RefSeq; XP_015614210.1; XM_015758724.1. DR AlphaFoldDB; Q7XCJ7; -. DR SMR; Q7XCJ7; -. DR STRING; 39947.Q7XCJ7; -. DR PaxDb; 39947-Q7XCJ7; -. DR EnsemblPlants; Os10t0544900-01; Os10t0544900-01; Os10g0544900. [Q7XCJ7-1] DR Gramene; Os10t0544900-01; Os10t0544900-01; Os10g0544900. [Q7XCJ7-1] DR KEGG; osa:4349275; -. DR eggNOG; KOG0700; Eukaryota. DR HOGENOM; CLU_013173_2_0_1; -. DR InParanoid; Q7XCJ7; -. DR OMA; WDYLSNE; -. DR OrthoDB; 999128at2759; -. DR Proteomes; UP000000763; Chromosome 10. DR Proteomes; UP000007752; Chromosome 8. DR Proteomes; UP000059680; Chromosome 10. DR GO; GO:0016020; C: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: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:SF23; PROTEIN PHOSPHATASE 2C 72-RELATED; 1. DR Pfam; PF00481; PP2C; 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; Q7XCJ7; OS. PE 2: Evidence at transcript level; KW Alternative splicing; Hydrolase; Magnesium; Manganese; Membrane; KW Metal-binding; Protein phosphatase; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..393 FT /note="Probable protein phosphatase 2C 72" FT /id="PRO_0000363319" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 49..357 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT BINDING 88 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 88 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 89 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 289 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 VAR_SEQ 311..334 FT /note="GIARRLVKAAMQQAAKKREMRYSD -> VCVLILCKLIISMAKCLFILLLVQ FT (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_036281" FT VAR_SEQ 335..393 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_036282" SQ SEQUENCE 393 AA; 43370 MW; B913270F7B7C4799 CRC64; MLSAAMEYLR SCWGPASSPA GRPRKGSDAA GRQDGLLWYK DAGQLVAGEF SMAVVQANNL LEDHSQVESG PLSTTDPNLQ GTLVGVYDGH GGPETARYIN DHLFNHLRGF ASEHKCMSAD VIRKAFRATE EGFFSVVSSQ WSMRPQLAAV GSCCLVGVIC AGNLYIANLG DSRAVLGRLV KGTGEVLAMQ LSAEHNASFE EVRRELQAAH PDDPHIVVLK HNVWRVKGII QITRSIGDVY LKKPEFNREP LHSKFRLQET FRRPLLSSEP AIVVHQLQTT DQFIIFASDG LWEHISNQEA VDLVQHNPRN GIARRLVKAA MQQAAKKREM RYSDLKKIDR GVRRHFHDDI TVVVVFFDSN AITTANWSRP SVSLRGGGVT LPANSLAPFS VPT //