PPM1F_RAT
ID PPM1F_RAT Reviewed; 450 AA.
AC Q9WVR7;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein phosphatase 1F;
DE EC=3.1.3.16;
DE AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase;
DE Short=CaM-kinase phosphatase;
DE Short=CaMKPase;
DE AltName: Full=Partner of PIX 2;
GN Name=Ppm1f; Synonyms=Popx2;
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].
RC TISSUE=Brain;
RX PubMed=10348902; DOI=10.1093/oxfordjournals.jbchem.a022381;
RA Kitani T., Ishida A., Okuno S., Takeuchi M., Kameshita I., Fujisawa H.;
RT "Molecular cloning of Ca2+/Calmodulin-dependent protein kinase
RT phosphatase.";
RL J. Biochem. 125:1022-1028(1999).
CC -!- FUNCTION: Dephosphorylates and concomitantly deactivates CaM-kinase II
CC activated upon autophosphorylation, and CaM-kinases IV and I activated
CC upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.
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: Associates with FEM1B. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AB023634; BAA82477.1; -; mRNA.
DR RefSeq; NP_786931.1; NM_175755.2.
DR RefSeq; XP_006248736.1; XM_006248674.2.
DR AlphaFoldDB; Q9WVR7; -.
DR SMR; Q9WVR7; -.
DR BioGRID; 252383; 1.
DR IntAct; Q9WVR7; 1.
DR MINT; Q9WVR7; -.
DR STRING; 10116.ENSRNOP00000002530; -.
DR PhosphoSitePlus; Q9WVR7; -.
DR jPOST; Q9WVR7; -.
DR PaxDb; Q9WVR7; -.
DR PRIDE; Q9WVR7; -.
DR Ensembl; ENSRNOT00000002530; ENSRNOP00000002530; ENSRNOG00000037909.
DR GeneID; 287931; -.
DR KEGG; rno:287931; -.
DR CTD; 9647; -.
DR RGD; 631363; Ppm1f.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000158884; -.
DR HOGENOM; CLU_013173_15_0_1; -.
DR InParanoid; Q9WVR7; -.
DR OMA; NQLWEVC; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q9WVR7; -.
DR TreeFam; TF317617; -.
DR PRO; PR:Q9WVR7; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000037909; Expressed in lung and 19 other tissues.
DR ExpressionAtlas; Q9WVR7; baseline and differential.
DR Genevisible; Q9WVR7; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0033192; F:calmodulin-dependent protein phosphatase activity; ISS:UniProtKB.
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:0004721; F:phosphoprotein phosphatase activity; TAS:RGD.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:RGD.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051224; P:negative regulation of protein transport; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISO:RGD.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
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 Apoptosis; Hydrolase; Magnesium; Manganese; Metal-binding; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..450
FT /note="Protein phosphatase 1F"
FT /id="PRO_0000057760"
FT DOMAIN 152..409
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 420..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 400
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49593"
SQ SEQUENCE 450 AA; 49165 MW; 67626542F32B2FD0 CRC64;
MASGAPQNSS QMACDGEIPG FLDTLLQDFP APLSLESPLP WKVPGTVLGQ EEVEAELTEL
AMGFLGSRNA PPAVAAAVTH EAISQLLQTD LSEFKRLPEQ EEEEEEEEER VLTTLLDAKG
LSRSFFNCLW EVCSQWQKRV PLTAQAPQRK WLVSIHAIRN TRRKMEDRHV SLPAFNHLFG
LSDSVHRAYF AVFDGHGGVD AARYASVHVH TNASHQPELL TDPAAALKEA FRHTDQMFLQ
KAKRERLQSG TTGVCALITG AALHVAWLGD SQVILVQQGQ VVKLMEPHKP ERQDEKSRIE
ALGGFVSLMD CWRVNGTLAV SRAIGDVFQK PYVSGEADAA SRELTGLEDY LLLACDGFFD
VVPHHEIPGL VHGHLLRQKG SGMHVAEELV AVARDRGSHD NITVMVVFLR DPLELLEGGG
QGAGGAQADV GSQDLSTGLS ELEINTSQRS
