Q8CGA0 (PPM1F_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein phosphatase 1F
EC=3.1.3.16

Alternative name(s):
Ca(2+)/calmodulin-dependent protein kinase phosphatase
Short name=CaM-kinase phosphatase
Short name=CaMKPase

Gene names

Name:

Ppm1f

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 magnesium or manganese ions per subunit By similarity.
Subunit structure	Associates with FEM1B By similarity.
Sequence similarities	Belongs to the PP2C family.

Ontologies

Keywords
Biological process	Apoptosis
Ligand	Magnesium Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to drug Inferred from sequence or structural similarity. Source: UniProtKB intrinsic apoptotic signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of peptidyl-serine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein kinase activity by regulation of protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-threonine dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of focal adhesion assembly Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara protein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	calmodulin-dependent protein phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 452	452	Protein phosphatase 1F		PRO_0000057759
Regions
	Compositional bias	99 – 110	12	Poly-Glu
Sites
	Metal binding	195	1	Manganese 1 By similarity
	Metal binding	195	1	Manganese 2 By similarity
	Metal binding	196	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	357	1	Manganese 2 By similarity
	Metal binding	401	1	Manganese 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CGA0 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 7C8ED2E597F9D1B8	FASTA	452	49,611
	10 20 30 40 50 60 MASGAAQNSS QMACDSEIPG FLDAFLQDFP APLSLESPLP WKVPGTVLSQ EEVEAELIEL 70 80 90 100 110 120 ALGFLGSRNA PPSFAVAVTH EAISQLLQTD LSEFKRLPEQ EEEEEEEEEE KALVTLLDAK 130 140 150 160 170 180 GLARSFFNCL WKVCSQWQKQ VPLTAQAPQW QWLVSIHAIR NTRRKMEDRH VSLPAFNHLF 190 200 210 220 230 240 GLSDSVHRAY FAVFDGHGGV DAARYASVHV HTNASHQPEL RTNPAAALKE AFRLTDEMFL 250 260 270 280 290 300 QKAKRERLQS GTTGVCALIA GAALHVAWLG DSQVILVQQG RVVKLMEPHK PERQDEKARI 310 320 330 340 350 360 EALGGFVSLM DCWRVNGTLA VSRAIGDVFQ KPYVSGEADA ASRELTGSED YLLLACDGFF 370 380 390 400 410 420 DVVPHHEVTG LVHGHLLRHK GNGMRIAEEL VAVARDRGSH DNITVMVVFL REPLELLEGG 430 440 450 VQGTGDAQAD VGSQDLSTGL SELEISNTSQ RS

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK154192 mRNA. Translation: BAE32429.1. AK164964 mRNA. Translation: BAE37981.1. BC042570 mRNA. Translation: AAH42570.1.
IPI	IPI00275512.
RefSeq	NP_789803.1. NM_176833.4.
UniGene	Mm.230296.
3D structure databases
ProteinModelPortal	Q8CGA0.
SMR	Q8CGA0. Positions 153-411.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000027373.
PTM databases
PhosphoSite	Q8CGA0.
Proteomic databases
PaxDb	Q8CGA0.
PRIDE	Q8CGA0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027373; ENSMUSP00000027373; ENSMUSG00000026181.
GeneID	68606.
KEGG	mmu:68606.
UCSC	uc007yjo.2. mouse.
Organism-specific databases
CTD	9647.
MGI	MGI:1918464. Ppm1f.
Phylogenomic databases
eggNOG	COG0631.
GeneTree	ENSGT00690000101775.
HOGENOM	HOG000232094.
HOVERGEN	HBG053656.
InParanoid	Q8CGA0.
KO	K01090.
OMA	GDVFQKP.
OrthoDB	EOG4JM7PR.
Gene expression databases
Bgee	Q8CGA0.
CleanEx	MM_PPM1F.
Genevestigator	Q8CGA0.
GermOnline	ENSMUSG00000026181. Mus musculus.
Family and domain databases
Gene3D	3.60.40.10. 1 hit.
InterPro	IPR001932. PP2C-like. IPR000222. PP2C_Mn2_Asp60_BS. IPR015655. Protein_Pase_2C. [Graphical view]
PANTHER	PTHR13832. PTHR13832. 1 hit.
Pfam	PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00331. PP2C_SIG. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS01032. PP2C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PPM1F. mouse.
NextBio	327542.
SOURCE	Search...

Entry information

Entry name

PPM1F_MOUSE

Accession

Primary (citable) accession number: Q8CGA0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program