PPM1B_RAT
ID PPM1B_RAT Reviewed; 390 AA.
AC P35815; Q546R0; Q64046;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein phosphatase 1B;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 2C isoform beta;
DE Short=PP2C-beta;
GN Name=Ppm1b; Synonyms=Pp2c2, Pppm1b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1312947; DOI=10.1016/0014-5793(92)80344-g;
RA Wenk J., Trompeter H.-I., Pettrich K.-G., Cohen P.T.W., Campbell D.G.,
RA Mieskes G.;
RT "Molecular cloning and primary structure of a protein phosphatase 2C
RT isoform.";
RL FEBS Lett. 297:135-138(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7532404; DOI=10.1006/bbrc.1995.1245;
RA Schafer K., Braun T.;
RT "Monoclonal anti-FLAG antibodies react with a new isoform of rat Mg2+
RT dependent protein phosphatase beta.";
RL Biochem. Biophys. Res. Commun. 207:708-714(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Seroussi E., Shani N., Hayut A., Faier S., Ben-Meir D., Divinski I.,
RA Smorodinsky N.I., Lavi S.;
RT "Protein phosphatase 1B. Cloning and characterization of two major
RT transcripts generated by alternative use of 3' exons.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enzyme with a broad specificity. Dephosphorylates PRKAA1 and
CC PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating
CC it at 'Ser-172'. Plays an important role in the termination of TNF-
CC alpha-mediated NF-kappa-B activation through dephosphorylating and
CC inactivating IKBKB/IKKB (By similarity). {ECO:0000250}.
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: Monomer. Interacts with PAK6. Interacts with the
CC phosphorylated form of IKBKB/IKKB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P36993}. Membrane
CC {ECO:0000250|UniProtKB:P36993}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P36993}. Note=Weakly associates at the membrane
CC and N-myristoylation mediates the membrane localization.
CC {ECO:0000250|UniProtKB:P36993}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. Isoforms appear to differ
CC in their C-terminus.;
CC Name=1; Synonyms=Beta-1;
CC IsoId=P35815-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta-MPP;
CC IsoId=P35815-2; Sequence=VSP_005093;
CC -!- PTM: Isgylation negatively regulates its activity. {ECO:0000250}.
CC -!- PTM: N-myristoylation is essential for the recognition of its
CC substrates for dephosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; S90449; AAB21898.1; -; mRNA.
DR EMBL; S74572; AAB33430.1; -; mRNA.
DR EMBL; AJ271837; CAC28067.1; -; mRNA.
DR PIR; JC2524; JC2524.
DR PIR; S20392; S20392.
DR RefSeq; NP_149087.1; NM_033096.2. [P35815-1]
DR AlphaFoldDB; P35815; -.
DR SMR; P35815; -.
DR STRING; 10116.ENSRNOP00000041472; -.
DR iPTMnet; P35815; -.
DR PhosphoSitePlus; P35815; -.
DR jPOST; P35815; -.
DR PaxDb; P35815; -.
DR PRIDE; P35815; -.
DR GeneID; 24667; -.
DR KEGG; rno:24667; -.
DR UCSC; RGD:3374; rat. [P35815-1]
DR CTD; 5495; -.
DR RGD; 3374; Ppm1b.
DR eggNOG; KOG0697; Eukaryota.
DR HOGENOM; CLU_013173_4_0_1; -.
DR InParanoid; P35815; -.
DR Reactome; R-RNO-1169408; ISG15 antiviral mechanism.
DR PRO; PR:P35815; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000030667; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; P35815; baseline and differential.
DR Genevisible; P35815; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0006499; P:N-terminal protein myristoylation; ISS:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 1.10.10.430; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR012911; PP2C_C.
DR InterPro; IPR036580; PP2C_C_sf.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR Pfam; PF07830; PP2C_C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81601; SSF81601; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Hydrolase; Isopeptide bond; Lipoprotein;
KW Magnesium; Manganese; Membrane; Metal-binding; Myristate; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT CHAIN 2..390
FT /note="Protein phosphatase 1B"
FT /id="PRO_0000057748"
FT DOMAIN 23..295
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 60
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O75688"
FT CROSSLNK 12
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 379..390
FT /note="GAGDLEDSLVAL -> FYQPSTPYSDNVSYYEWQT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7532404"
FT /id="VSP_005093"
SQ SEQUENCE 390 AA; 42889 MW; D147615BC2FA140B CRC64;
MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD
GHAGSRVANY CSTHLLEHIT TNEDFRAADK SGFALEPSVE NVKTGIRTGF LKIDEYMRNF
SDLRNGMDRS GSTAVGVMIS PTHIYFINCG DSRAVLCRNG QVCFSTQDHK PCNPMEKERI
QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFVVL
ACDGIWDVMS NEELCEFVNS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFANAPK
VSDEAVKRDL ELDKHLESRV EEIMQKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGKR
NVIEAVYSRL NPNKDNDGGA GDLEDSLVAL
