ID BIP2C_ORYSI Reviewed; 569 AA. AC Q6J2K6; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=Probable protein phosphatase 2C BIPP2C1; DE EC=3.1.3.16; DE AltName: Full=BTH-induced protein phosphatase 2C 1; DE Short=OsBIPP2C1; GN Name=BIPP2C1; OS Oryza sativa subsp. indica (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=39946; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INDUCTION. RC STRAIN=cv. Yuanfengzao; TISSUE=Seedling; RX AGRICOLA=IND43812072; RA Hu X., Song F., Zheng Z.; RT "Molecular characterization and expression analysis of a rice protein RT phosphatase 2C gene, OsBIPP2C1, and overexpression in transgenic tobacco RT conferred enhanced disease resistance and abiotic tolerance."; RL Physiol. Plantarum 127:225-236(2006). CC -!- FUNCTION: May play a role in responses to biotic and abiotic stresses. CC {ECO:0000269|Ref.1}. 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6J2K6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6J2K6-2; Sequence=VSP_036283; CC Name=3; CC IsoId=Q6J2K6-3; Sequence=VSP_036284; CC Name=4; CC IsoId=Q6J2K6-4; Sequence=VSP_036285; CC -!- INDUCTION: By salicylic acid (SA), benzothiadiazole (BTH), hydrogen CC peroxide, abscisic acid (ABA), wounding, salt, cold and osmotic CC stresses. {ECO:0000269|Ref.1}. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing donor splice CC site. {ECO:0000305}. 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; AY603974; AAT35116.1; -; mRNA. DR AlphaFoldDB; Q6J2K6; -. DR SMR; Q6J2K6; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR InterPro; IPR039123; PPTC7. DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1. DR PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding; KW Protein phosphatase. FT CHAIN 1..569 FT /note="Probable protein phosphatase 2C BIPP2C1" FT /id="PRO_0000363326" FT DOMAIN 329..564 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082" FT REGION 166..212 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 251..279 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 255..279 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 358 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 358 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 359 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 488 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 555 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT VAR_SEQ 1..36 FT /note="MDEEARAAGCSPAPPRAPAASCGAAAELCLCSPTGV -> MKRRAPPDAPQR FT RPARRLLPVALPPSSASAPLQVWVRGIHACLISFGFGSRFDLVLVWFGVGLDA (in FT isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_036283" FT VAR_SEQ 35..36 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_036284" FT VAR_SEQ 121..256 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_036285" SQ SEQUENCE 569 AA; 58675 MW; DEC2D71CDF4363C6 CRC64; MDEEARAAGC SPAPPRAPAA SCGAAAELCL CSPTGVEGIE QVPGCPCFED AGAVVVSGEA PEGPGVLCSG DGAELKLAEQ GALDVRLGSP AVGIHEQQLL HRGTSGSDEA GAINEISPVE VSPSEASSNL DTAGAIGGSP LMLESLPETS DTRGCEQEVM PGVVVGSSNR DASSEVGVES ECGSDADGRN GLGEGELVSS VDGGGAEKSS KVTGVLSEEG VDGMETALEP CVASVGSITQ VEEGVDRMET SLDDSEASDG STTQDFDTDV ETESSGSSIE EQDMGYGVHI PHTEQAICEV ARGNKSSEVK SSDRMSSVTL PTLILASGAA MLPHPSKVLT GGEDAYFIAC DGWFGVADGV GQWSFEGINA GLYARELMDG CKKAVMESQG APEMRTEEVL AKAADEARSP GSSTVLVAHF DGQVLHACNI GDSGFLVIRN GEIYQKSKPM TYGFNFPLQI EKGDDPFKLV QKYTIDLQEG DAIVTATDGL FDNVYEEEIA AVISKSLEAG LKPSEIAEFL VARAKEVGRS ATCRSPFSDA ALAVGYLGYS GGKLDDVTVV VSVVRKSEV //