PPM1L_BOVIN
ID PPM1L_BOVIN Reviewed; 360 AA.
AC A5PJZ2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein phosphatase 1L;
DE EC=3.1.3.16;
DE AltName: Full=Protein phosphatase 1-like;
DE AltName: Full=Protein phosphatase 2C isoform epsilon;
DE Short=PP2C-epsilon;
GN Name=PPM1L; Synonyms=PP2CE;
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a suppressor of the SAPK signaling pathways by
CC associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by
CC attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6.
CC {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: Interacts with MAP3K7/TAK1 and MAP3K5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; BC142293; AAI42294.1; -; mRNA.
DR RefSeq; NP_001092588.1; NM_001099118.2.
DR AlphaFoldDB; A5PJZ2; -.
DR SMR; A5PJZ2; -.
DR STRING; 9913.ENSBTAP00000050151; -.
DR PaxDb; A5PJZ2; -.
DR GeneID; 541235; -.
DR KEGG; bta:541235; -.
DR CTD; 151742; -.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_11_0_1; -.
DR InParanoid; A5PJZ2; -.
DR OrthoDB; 1044139at2759; -.
DR TreeFam; TF332888; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 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 Hydrolase; Magnesium; Manganese; Membrane; Metal-binding;
KW Protein phosphatase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..360
FT /note="Protein phosphatase 1L"
FT /id="PRO_0000354704"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 92..351
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 41042 MW; 4BD0763B7B2AF8D7 CRC64;
MIEDTMTLLS LLGRIMRYFL LRPETLFLLC ISLALWSYFF HTDEVKTIVK SSRDAVKMVK
GKVAEIMQND RLGGLDVLEA EFSKTWEFKS HNVAVYSIQG RRDHMEDRFE VLMDLANKTH
PSIFGIFDGH GGETAAEYVK SRLPEALKQH LQDYEKDKEN SVLSYQTILE QQILSIDREM
LEKLTVSYDE AGTTCLIALL SDKDLTVANV GDSRGVLCDK DGNAIPLSHD HKPYQLKERK
RIKRAGGFIS FNGSWRVQGI LAMSRSLGDY PLKNLNVVIP DPDILTFDLD KLQPEFMILA
SDGLWDAFSN EEAVRFIKDR LDEPHFGAKS IVLQSFYRGC PDNITVMVVK FRNSSKTEEQ
