BIP2C_ORYSI
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 03-AUG-2022, entry version 74.
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}.
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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; -; 2.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PTHR12320; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 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
