PPTC7_MOUSE
ID PPTC7_MOUSE Reviewed; 310 AA.
AC Q6NVE9; Q3TS53; Q8BVC7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein phosphatase PTC7 homolog;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q8NI37};
DE AltName: Full=T-cell activation protein phosphatase 2C;
DE Short=TA-PP2C;
DE Flags: Precursor;
GN Name=Pptc7; Synonyms=Tapp2c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cecum, Egg, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Protein phosphatase which positively regulates biosynthesis
CC of the ubiquinone, coenzyme Q (By similarity). Dephosphorylates the
CC ubiquinone biosynthesis protein COQ7 which is likely to lead to its
CC activation (By similarity). {ECO:0000250|UniProtKB:Q8NI37}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01082};
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 Evidence={ECO:0000250|UniProtKB:Q8NI37};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8NI37};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8NI37};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q8NI37}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NVE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NVE9-2; Sequence=VSP_032772;
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AK078914; BAC37456.1; -; mRNA.
DR EMBL; AK135118; BAE22428.1; -; mRNA.
DR EMBL; AK162261; BAE36822.1; -; mRNA.
DR EMBL; BC068149; AAH68149.1; -; mRNA.
DR CCDS; CCDS39255.1; -. [Q6NVE9-1]
DR RefSeq; NP_796216.2; NM_177242.4. [Q6NVE9-1]
DR AlphaFoldDB; Q6NVE9; -.
DR SMR; Q6NVE9; -.
DR STRING; 10090.ENSMUSP00000051838; -.
DR iPTMnet; Q6NVE9; -.
DR PhosphoSitePlus; Q6NVE9; -.
DR EPD; Q6NVE9; -.
DR MaxQB; Q6NVE9; -.
DR PaxDb; Q6NVE9; -.
DR PeptideAtlas; Q6NVE9; -.
DR PRIDE; Q6NVE9; -.
DR ProteomicsDB; 289818; -. [Q6NVE9-1]
DR ProteomicsDB; 289819; -. [Q6NVE9-2]
DR Antibodypedia; 50198; 120 antibodies from 17 providers.
DR DNASU; 320717; -.
DR Ensembl; ENSMUST00000053426; ENSMUSP00000051838; ENSMUSG00000038582. [Q6NVE9-1]
DR Ensembl; ENSMUST00000119015; ENSMUSP00000113194; ENSMUSG00000038582. [Q6NVE9-2]
DR GeneID; 320717; -.
DR KEGG; mmu:320717; -.
DR UCSC; uc008zky.1; mouse. [Q6NVE9-1]
DR CTD; 160760; -.
DR MGI; MGI:2444593; Pptc7.
DR VEuPathDB; HostDB:ENSMUSG00000038582; -.
DR eggNOG; KOG1379; Eukaryota.
DR GeneTree; ENSGT00390000011937; -.
DR HOGENOM; CLU_029404_3_0_1; -.
DR InParanoid; Q6NVE9; -.
DR OMA; MQSIYWT; -.
DR OrthoDB; 826926at2759; -.
DR PhylomeDB; Q6NVE9; -.
DR TreeFam; TF315105; -.
DR BioGRID-ORCS; 320717; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Pptc7; mouse.
DR PRO; PR:Q6NVE9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6NVE9; protein.
DR Bgee; ENSMUSG00000038582; Expressed in ileal epithelium and 255 other tissues.
DR Genevisible; Q6NVE9; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0004722; F:protein serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; ISS:UniProtKB.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PTHR12320; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; Protein phosphatase; Reference proteome; Transit peptide.
FT TRANSIT 1..74
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 75..310
FT /note="Protein phosphatase PTC7 homolog"
FT /id="PRO_0000328746"
FT DOMAIN 75..305
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 84
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 85
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P35813"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032772"
SQ SEQUENCE 310 AA; 33048 MW; 36F226F82515DB7B CRC64;
MFSVLSYGRL VARAVLGGLS QTDPRAGGGG GGGGGSSGDY GLVTAGCGFG KDFRKGLLKK
GACYGDDACF VARHRSADVL GVADGVGGWR DYGVDPSQFS GTLMRTCERL VKEGRFVPSN
PVGILTTSYC ELLQNKVPLL GSSTACIVVL DRSSHRLHTA NLGDSGFLVV RGGEVVHRSD
EQQHYFNTPF QLSIAPPEAE GVVLSDSPDA ADSTSFDVQL GDIILTATDG LFDNMPDYMI
LQELKKLKNS NYESIQRTAR SIAEQAHELA YDPNYMSPFA QFACDNGLNV RGGKPDDITV
LLSIVAEYTD
