ID   PPM1B_BOVIN             Reviewed;         484 AA.
AC   O62830; Q2T9W5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   27-MAR-2024, entry version 152.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-2).
RC   TISSUE=Retina;
RX   PubMed=9486768;
RX   DOI=10.1002/(sici)1097-4547(19980201)51:3<328::aid-jnr6>3.0.co;2-i;
RA   Klumpp S., Selke D., Fischer D., Baumann A., Mueller F., Thanos S.;
RT   "Protein phosphatase type-2C isozymes present in vertebrate retinae:
RT   purification, characterization, and localization in photoreceptors.";
RL   J. Neurosci. Res. 51:328-338(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-1).
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) 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       Name=Beta-1;
CC         IsoId=O62830-1; Sequence=Displayed;
CC       Name=Beta-2;
CC         IsoId=O62830-2; Sequence=VSP_020009, VSP_020010, VSP_020011;
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; AJ005458; CAA06555.1; -; mRNA.
DR   EMBL; BC111235; AAI11236.1; -; mRNA.
DR   RefSeq; NP_776855.1; NM_174430.2. [O62830-2]
DR   AlphaFoldDB; O62830; -.
DR   SMR; O62830; -.
DR   STRING; 9913.ENSBTAP00000043518; -.
DR   PaxDb; 9913-ENSBTAP00000043518; -.
DR   Ensembl; ENSBTAT00000046197.3; ENSBTAP00000043518.2; ENSBTAG00000000223.6. [O62830-1]
DR   Ensembl; ENSBTAT00000050064.3; ENSBTAP00000046832.2; ENSBTAG00000000223.6. [O62830-2]
DR   GeneID; 281995; -.
DR   KEGG; bta:281995; -.
DR   CTD; 5495; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000223; -.
DR   eggNOG; KOG0697; Eukaryota.
DR   GeneTree; ENSGT00940000156070; -.
DR   HOGENOM; CLU_013173_4_0_1; -.
DR   InParanoid; O62830; -.
DR   OMA; MQGYRMT; -.
DR   TreeFam; TF313590; -.
DR   Reactome; R-BTA-1169408; ISG15 antiviral mechanism.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000000223; Expressed in semitendinosus and 106 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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; IBA:GO_Central.
DR   GO; GO:0006499; P:N-terminal protein myristoylation; ISS:UniProtKB.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
DR   GO; GO:0032688; P:negative regulation of interferon-beta production; ISS:UniProtKB.
DR   GO; GO:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; ISS:UniProtKB.
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; Phosphatase 2C, C-terminal domain suprefamily; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR012911; PP2C_C.
DR   InterPro; IPR036580; PP2C_C_sf.
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:SF105; PROTEIN PHOSPHATASE 1B; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   Pfam; PF07830; PP2C_C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF81601; Protein serine/threonine phosphatase 2C, C-terminal domain; 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..484
FT                   /note="Protein phosphatase 1B"
FT                   /id="PRO_0000057745"
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          431..484
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   COMPBIAS        437..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..484
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         391
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   CROSSLNK        142
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ISG15)"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         359..364
FT                   /note="NIIFFR -> K (in isoform Beta-2)"
FT                   /evidence="ECO:0000303|PubMed:9486768"
FT                   /id="VSP_020009"
FT   VAR_SEQ         384..392
FT                   /note="ASDEAEESG -> GAGDLEDPW (in isoform Beta-2)"
FT                   /evidence="ECO:0000303|PubMed:9486768"
FT                   /id="VSP_020010"
FT   VAR_SEQ         393..484
FT                   /note="Missing (in isoform Beta-2)"
FT                   /evidence="ECO:0000303|PubMed:9486768"
FT                   /id="VSP_020011"
SQ   SEQUENCE   484 AA;  53431 MW;  453DD1E6E7D47D27 CRC64;
     MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL EDWSFFAVYD
     GHAGSRVANY CSTHLLEHIT NNEDFRAAGK SGSALEPSVE NVKNGIRTGF LKIDEYMRNF
     SDLRNGMDRS GSTAVGVMIS PKHIYFINCG DSRAVLYRSG QVCFSTQDHK PCNPREKERI
     QNAGGSVMIQ RVNGSLAVSR ALGDYDYKCV DGKGPTEQLV SPEPEVYEIL RAEEDEFIIL
     ACDGIWDVMS NEELCEFVKS RLEVSDDLEN VCNWVVDTCL HKGSRDNMSI VLVCFSNAPK
     VSDEAMRKDS ELDKYLESRV EEIMEKSGEE GMPDLAHVMR ILSAENIPNL PPGGGLAGNI
     IFFRRHVIEA VYSRLNPHRE SDGASDEAEE SGSQGKLVEA LRQMRINHRG NYRQLLEEML
     TSYRLAKVEG EENPAEQAAT AASSNSDAGN TVAMQESHTE SKSDLAELDS CTEDAGTKMS
     GEKL
//