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 24-JAN-2024, entry version 156. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10116-ENSRNOP00000002530; -. DR Ensembl; ENSRNOT00000002530.6; ENSRNOP00000002530.3; ENSRNOG00000037909.3. DR Ensembl; ENSRNOT00055006013; ENSRNOP00055004536; ENSRNOG00055003813. DR Ensembl; ENSRNOT00060004159; ENSRNOP00060002935; ENSRNOG00060002590. DR Ensembl; ENSRNOT00065013430; ENSRNOP00065009956; ENSRNOG00065008468. DR GeneID; 287931; -. DR KEGG; rno:287931; -. DR AGR; RGD:631363; -. 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; GDICQKP; -. DR OrthoDB; 202023at2759; -. DR PhylomeDB; Q9WVR7; -. DR TreeFam; TF317617; -. DR PRO; PR:Q9WVR7; -. DR Proteomes; UP000002494; Chromosome 11. DR Bgee; ENSRNOG00000037909; Expressed in lung and 19 other cell types or tissues. DR ExpressionAtlas; Q9WVR7; baseline and differential. 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; IDA: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:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. 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: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:0032880; P:regulation of protein localization; ISO:RGD. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR000222; PP2C_BS. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR13832:SF233; PROTEIN PHOSPHATASE 1F; 1. DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1. DR Pfam; PF00481; PP2C; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS01032; PPM_1; 1. DR PROSITE; PS51746; PPM_2; 1. DR Genevisible; Q9WVR7; RN. 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 //