PPM1B_BOVIN
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 03-AUG-2022, entry version 144.
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; O62830; -.
DR PRIDE; O62830; -.
DR Ensembl; ENSBTAT00000046197; ENSBTAP00000043518; ENSBTAG00000000223. [O62830-1]
DR Ensembl; ENSBTAT00000050064; ENSBTAP00000046832; ENSBTAG00000000223. [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; IYDVMEN; -.
DR OrthoDB; 957254at2759; -.
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 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: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; IBA:GO_Central.
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..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
